ABCA4_HUMAN
ID ABCA4_HUMAN Reviewed; 2273 AA.
AC P78363; O15112; O60438; O60915; Q0QD48; Q4LE31;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Retinal-specific phospholipid-transporting ATPase ABCA4 {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000269|PubMed:24097981};
DE AltName: Full=ATP-binding cassette sub-family A member 4;
DE AltName: Full=RIM ABC transporter;
DE Short=RIM proteinv;
DE Short=RmP;
DE AltName: Full=Retinal-specific ATP-binding cassette transporter;
DE AltName: Full=Stargardt disease protein;
GN Name=ABCA4 {ECO:0000312|HGNC:HGNC:34};
GN Synonyms=ABCR {ECO:0000303|PubMed:9054934};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1, AND VARIANTS HIS-846; GLN-943
RP AND ASP-1817.
RX PubMed=9054934; DOI=10.1038/ng0397-236;
RA Allikmets R., Singh N., Sun H., Shroyer N.F., Hutchinson A.,
RA Chidambaram A., Gerrard B., Baird L., Stauffer D., Peiffer A., Rattner A.,
RA Smallwood P.M., Li Y., Anderson K.L., Lewis R.A., Nathans J., Leppert M.,
RA Dean M., Lupski J.R.;
RT "A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is
RT mutated in recessive Stargardt macular dystrophy.";
RL Nat. Genet. 15:236-246(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9202155; DOI=10.1016/s0014-5793(97)00517-6;
RA Azarian S.M., Travis G.H.;
RT "The photoreceptor rim protein is an ABC transporter encoded by the gene
RT for recessive Stargardt's disease (ABCR).";
RL FEBS Lett. 409:247-252(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STGD1 TRP-18 AND CYS-212, AND
RP VARIANT ASP-1817.
RX PubMed=9503029; DOI=10.1006/geno.1997.5164;
RA Gerber S., Rozet J.-M., van de Pol T.J.R., Hoyng C.B., Munnich A.,
RA Blankenagel A., Kaplan J., Cremers F.P.M.;
RT "Complete exon-intron structure of the retina-specific ATP binding
RT transporter gene (ABCR) allows the identification of novel mutations
RT underlying Stargardt disease.";
RL Genomics 48:139-142(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS STGD1.
RX PubMed=9490294; DOI=10.1007/s004390050649;
RA Nasonkin I., Illing M., Koehler M.R., Schmid M., Molday R.S., Weber B.H.F.;
RT "Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and
RT identification of novel mutations in Stargardt's disease.";
RL Hum. Genet. 102:21-26(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-943.
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-29.
RC TISSUE=Retina;
RX PubMed=17286855; DOI=10.1186/1471-2164-8-42;
RA Roni V., Carpio R., Wissinger B.;
RT "Mapping of transcription start sites of human retina expressed genes.";
RL BMC Genomics 8:42-42(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10075733; DOI=10.1074/jbc.274.12.8269;
RA Sun H., Molday R.S., Nathans J.;
RT "Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the
RT photoreceptor-specific ATP-binding cassette transporter responsible for
RT Stargardt disease.";
RL J. Biol. Chem. 274:8269-8281(1999).
RN [9]
RP INVOLVEMENT IN RP19.
RX PubMed=9466990; DOI=10.1093/hmg/7.3.355;
RA Cremers F.P.M., van de Pol D.J.R., van Driel M.A., den Hollander A.I.,
RA van Haren F.J.J., Knoers N.V.A.M., Tijmes N., Bergen A.A.B.,
RA Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Deutman A.F.,
RA Hoyng C.B.;
RT "Autosomal recessive retinitis pigmentosa and cone-rod dystrophy caused by
RT splice site mutations in the Stargardt's disease gene ABCR.";
RL Hum. Mol. Genet. 7:355-362(1998).
RN [10]
RP MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; ASN-504;
RP ASN-1469; ASN-1529; ASN-1588 AND ASN-1662.
RX PubMed=11320094; DOI=10.1074/jbc.m101902200;
RA Bungert S., Molday L.L., Molday R.S.;
RT "Membrane topology of the ATP binding cassette transporter ABCR and its
RT relationship to ABC1 and related ABCA transporters: identification of N-
RT linked glycosylation sites.";
RL J. Biol. Chem. 276:23539-23546(2001).
RN [11]
RP DOMAIN, FUNCTION, VARIANTS STGD1 LEU-1408; HIS-1443 AND ARG-1488, AND
RP CHARACTERIZATION OF VARIANTS STGD1 LEU-1408; HIS-1443 AND ARG-1488.
RX PubMed=20404325; DOI=10.1074/jbc.m110.112896;
RA Biswas-Fiss E.E., Kurpad D.S., Joshi K., Biswas S.B.;
RT "Interaction of extracellular domain 2 of the human retina-specific ATP-
RT binding cassette transporter (ABCA4) with all-trans-retinal.";
RL J. Biol. Chem. 285:19372-19383(2010).
RN [12]
RP DOMAIN, FUNCTION, VARIANT STGD1 ALA-863, CHARACTERIZATION OF VARIANT STGD1
RP ALA-863, MUTAGENESIS OF PRO-940, AND VARIANT GLN-943.
RX PubMed=23144455; DOI=10.1074/jbc.m112.409623;
RA Biswas-Fiss E.E., Affet S., Ha M., Biswas S.B.;
RT "Retinoid binding properties of nucleotide binding domain 1 of the
RT Stargardt disease-associated ATP binding cassette (ABC) transporter,
RT ABCA4.";
RL J. Biol. Chem. 287:44097-44107(2012).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-969 AND LYS-1978, VARIANTS
RP STGD1 ALA-863 AND SER-965, AND CHARACTERIZATION OF VARIANTS STGD1 ALA-863
RP AND SER-965.
RX PubMed=22735453; DOI=10.1038/ncomms1927;
RA Quazi F., Lenevich S., Molday R.S.;
RT "ABCA4 is an N-retinylidene-phosphatidylethanolamine and
RT phosphatidylethanolamine importer.";
RL Nat. Commun. 3:925-925(2012).
RN [14]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, FUNCTION, SUBCELLULAR LOCATION,
RP VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND MET-1537,
RP CHARACTERIZATION OF VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND
RP MET-1537, AND MUTAGENESIS OF CYS-1502; ARG-2107 AND PRO-2180.
RX PubMed=24097981; DOI=10.1074/jbc.m113.508812;
RA Quazi F., Molday R.S.;
RT "Differential phospholipid substrates and directional transport by ATP-
RT binding cassette proteins ABCA1, ABCA7, and ABCA4 and disease-causing
RT mutants.";
RL J. Biol. Chem. 288:34414-34426(2013).
RN [15]
RP REGION.
RX PubMed=31481235; DOI=10.1016/j.bbrc.2019.08.121;
RA Patel M.J., Biswas S.B., Biswas-Fiss E.E.;
RT "Functional significance of the conserved C-Terminal VFVNFA motif in the
RT retina-specific ABC transporter, ABCA4, and its role in inherited visual
RT disease.";
RL Biochem. Biophys. Res. Commun. 519:46-52(2019).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS) IN COMPLEX WITH ATP,
RP MUTAGENESIS OF GLU-1087 AND GLU-2096, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISULFIDE BOND, GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; ASN-504;
RP ASN-1469; ASN-1529; ASN-1588 AND ASN-1662, AND ATP BINDING SITE.
RX PubMed=33605212; DOI=10.7554/elife.63524;
RA Liu F., Lee J., Chen J.;
RT "Molecular structures of the eukaryotic retinal importer ABCA4.";
RL Elife 10:0-0(2021).
RN [17]
RP VARIANTS ARMD2, AND VARIANTS.
RX PubMed=9295268; DOI=10.1126/science.277.5333.1805;
RA Allikmets R., Shroyer N.F., Singh N., Seddon J.M., Lewis R.A.,
RA Bernstein P.S., Peiffer A., Zabriskie N.A., Li Y., Hutchinson A., Dean M.,
RA Lupski J.R., Leppert M.;
RT "Mutation of the Stargardt disease gene (ABCR) in age-related macular
RT degeneration.";
RL Science 277:1805-1807(1997).
RN [18]
RP VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108;
RP TRP-1640; SER-1977 AND HIS-2107, AND VARIANTS FFM PRO-11; PRO-541;
RP VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971.
RX PubMed=9781034; DOI=10.1038/sj.ejhg.5200221;
RA Rozet J.-M., Gerber S., Souied E., Perrault I., Chatelin S., Ghazi I.,
RA Leowski C., Dufier J.-L., Munnich A., Kaplan J.;
RT "Spectrum of ABCR gene mutations in autosomal recessive macular
RT dystrophies.";
RL Eur. J. Hum. Genet. 6:291-295(1998).
RN [19]
RP VARIANTS STGD1.
RX PubMed=9973280; DOI=10.1086/302251;
RA Lewis R.A., Shroyer N.F., Singh N., Allikmets R., Hutchinson A., Li Y.,
RA Lupski J.R., Leppert M., Dean M.;
RT "Genotype/phenotype analysis of a photoreceptor-specific ATP-binding
RT cassette transporter gene, ABCR, in Stargardt disease.";
RL Am. J. Hum. Genet. 64:422-434(1999).
RN [20]
RP VARIANTS STGD1, AND VARIANTS.
RX PubMed=10090887; DOI=10.1086/302323;
RA Maugeri A., van Driel M.A., van de Pol D.J.R., Klevering B.J.,
RA van Haren F.J.J., Tijmes N., Bergen A.A.B., Rohrschneider K.,
RA Blankenagel A., Pinckers A.J.L.G., Dahl N., Brunner H.G., Deutman A.F.,
RA Hoyng C.B., Cremers F.P.M.;
RT "The 2588G-->C mutation in the ABCR gene is a mild frequent founder
RT mutation in the western European population and allows the classification
RT of ABCR Mutations in patients with Stargardt disease.";
RL Am. J. Hum. Genet. 64:1024-1035(1999).
RN [21]
RP VARIANT STGD1 TYR-54, AND VARIANT ALA-863.
RX PubMed=10612508; DOI=10.1016/s0002-9394(99)00236-6;
RA Zhang K., Garibaldi D.C., Kniazeva M., Albini T., Chiang M.F., Kerrigan M.,
RA Sunness J.S., Han M., Allikmets R.;
RT "A novel mutation in the ABCR gene in four patients with autosomal
RT recessive Stargardt disease.";
RL Am. J. Ophthalmol. 128:720-724(1999).
RN [22]
RP VARIANTS STGD1 VAL-60; ARG-206; ASN-300; PRO-541; ALA-849; PRO-974;
RP VAL-1038; CYS-1108; LEU-1408; ARG-1488; ASP-1652; PRO-1729; GLU-1961;
RP TRP-2038; TRP-2077; HIS-2107; ARG-2128 AND TYR-2150.
RX PubMed=10206579; DOI=10.1001/archopht.117.4.504;
RA Fishman G.A., Stone E.M., Grover S., Derlacki D.J., Haines H.L.,
RA Hockey R.R.;
RT "Variation of clinical expression in patients with Stargardt dystrophy and
RT sequence variations in the ABCR gene.";
RL Arch. Ophthalmol. 117:504-510(1999).
RN [23]
RP VARIANTS GLU-1961 AND ASN-2177.
RX PubMed=10880298; DOI=10.1086/303018;
RA Allikmets R., Tammur J., Hutchinson A., Lewis R.A., Shroyer N.F.,
RA Dalakishvili K., Lupski J.R., Steiner K., Pauleikhoff D., Holz F.G.,
RA Weber B.H.F., Dean M., Atkinson A., Gail M.H., Bernstein P.S., Singh N.,
RA Peiffer A., Zabriskie N.A., Leppert M., Seddon J.M., Zhang K.,
RA Sunness J.S., Udar N.S., Yelchits S., Silva-Garcia R., Small K.W.,
RA Simonelli F., Testa F., D'Urso M., Brancato R., Rinaldi E., Ingvast S.,
RA Taube A., Wadelius C., Souied E., Ducroq D., Kaplan J., Assink J.J.M.,
RA ten Brink J.B., de Jong P.T.V.M., Bergen A.A.B., Maugeri A.,
RA van Driel M.A., Hoyng C.B., Cremers F.P.M., Paloma E., Coco R.,
RA Balcells S., Gonzalez-Duarte R., Kermani S., Stanga P., Bhattacharya S.S.,
RA Bird A.C.;
RT "Further evidence for an association of ABCR alleles with age-related
RT macular degeneration.";
RL Am. J. Hum. Genet. 67:487-491(2000).
RN [24]
RP VARIANTS STGD1 GLU-60; THR-60; GLU-65; LEU-68; ARG-72; CYS-212; SER-230;
RP SER-247; VAL-328; LYS-471; PRO-541; GLN-572; ARG-607; LYS-635; CYS-653;
RP TYR-764; ARG-765; ALA-901; ILE-959; LYS-1036; VAL-1038; PRO-1063; ASP-1087;
RP CYS-1097; CYS-1108; LEU-1380; LYS-1399; PRO-1430; VAL-1440; HIS-1443;
RP LEU-1486; TYR-1488; MET-1537; PRO-1689; LEU-1705; THR-1733; ARG-1748;
RP PRO-1763; LYS-1885; HIS-1898; GLU-1961; ARG-1975; SER-1977; GLY-2077;
RP TRP-2077 AND VAL-2241, AND VARIANTS GLN-152; HIS-212; ARG-423; ILE-552;
RP ARG-914; GLN-943; THR-1562; ILE-1868; MET-1921; LEU-1948; PHE-1970;
RP ALA-2059; ASN-2177 AND VAL-2216.
RX PubMed=10958763; DOI=10.1086/303090;
RA Rivera A., White K., Stoehr H., Steiner K., Hemmrich N., Grimm T.,
RA Jurklies B., Lorenz B., Scholl H.P.N., Apfelstedt-Sylla E., Weber B.H.F.;
RT "A comprehensive survey of sequence variation in the ABCA4 (ABCR) gene in
RT Stargardt disease and age-related macular degeneration.";
RL Am. J. Hum. Genet. 67:800-813(2000).
RN [25]
RP VARIANTS CORD3 GLU-65; CYS-212; PRO-541; ALA-863; GLY-863 DEL; VAL-1038;
RP LYS-1122; TYR-1490 AND ASP-1598.
RX PubMed=10958761; DOI=10.1086/303079;
RA Maugeri A., Klevering B.J., Rohrschneider K., Blankenagel A., Brunner H.G.,
RA Deutman A.F., Hoyng C.B., Cremers F.P.M.;
RT "Mutations in the ABCA4 (ABCR) gene are the major cause of autosomal
RT recessive cone-rod dystrophy.";
RL Am. J. Hum. Genet. 67:960-966(2000).
RN [26]
RP VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 AND
RP HIS-1898, AND VARIANT GLN-943.
RX PubMed=10746567; DOI=10.1007/s004390051034;
RA Shroyer N.F., Lewis R.A., Lupski J.R.;
RT "Complex inheritance of ABCR mutations in Stargardt disease: linkage
RT disequilibrium, complex alleles, and pseudodominance.";
RL Hum. Genet. 106:244-248(2000).
RN [27]
RP VARIANTS GLN-943 AND SER-1948, VARIANTS STGD1 TYR-54; ASP-96; HIS-96;
RP VAL-156; VAL-407; ALA-424; ARG-445; TRP-602; 779-CYS--ASP-2273 DEL;
RP ALA-863; ALA-1429; TRP-1640; GLU-1703; 1779-TYR--ASP-2273 DEL AND ARG-2160,
RP VARIANTS CORD3 VAL-407; 2030-ARG--ASP-2273 DEL AND TYR-2150, AND VARIANT
RP RP19 ALA-424.
RX PubMed=10634594;
RA Papaioannou M., Ocaka L., Bessant D., Lois N., Bird A.C., Payne A.,
RA Bhattacharya S.S.;
RT "An analysis of ABCR mutations in British patients with recessive retinal
RT dystrophies.";
RL Invest. Ophthalmol. Vis. Sci. 41:16-19(2000).
RN [28]
RP VARIANTS STGD1 CYS-212; ASP-767; ILE-897; VAL-1038; LYS-1087; LYS-1399;
RP GLN-1640 AND GLU-1961, AND VARIANT HIS-212.
RX PubMed=10711710;
RA Simonelli F., Testa F., de Crecchio G., Rinaldi E., Hutchinson A.,
RA Atkinson A., Dean M., D'Urso M., Allikmets R.;
RT "New ABCR mutations and clinical phenotype in Italian patients with
RT Stargardt disease.";
RL Invest. Ophthalmol. Vis. Sci. 41:892-897(2000).
RN [29]
RP CHARACTERIZATION OF VARIANTS, AND MUTAGENESIS OF GLY-966; LYS-969; GLY-1975
RP AND LYS-1978.
RX PubMed=11017087; DOI=10.1038/79994;
RA Sun H., Smallwood P.M., Nathans J.;
RT "Biochemical defects in ABCR protein variants associated with human
RT retinopathies.";
RL Nat. Genet. 26:242-246(2000).
RN [30]
RP VARIANT STGD1 ASN-972, AND VARIANTS GLN-943; ILE-1868 AND LEU-1948.
RX PubMed=11594993; DOI=10.1034/j.1600-0420.2001.790520.x;
RA Eksandh L., Ekstroem U., Abrahamson M., Bauer B., Andreasson S.;
RT "Different clinical expressions in two families with Stargardt's macular
RT dystrophy (STGD1).";
RL Acta Ophthalmol. Scand. 79:524-530(2001).
RN [31]
RP VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, AND VARIANTS
RP HIS-212; ARG-423; ILE-1868 AND ILE-2255.
RX PubMed=11384574; DOI=10.1016/s0002-9394(01)00838-8;
RA Shroyer N.F., Lewis R.A., Lupski J.R.;
RT "Analysis of the ABCR (ABCA4) gene in 4-aminoquinoline retinopathy: is
RT retinal toxicity by chloroquine and hydroxychloroquine related to Stargardt
RT disease?";
RL Am. J. Ophthalmol. 131:761-766(2001).
RN [32]
RP VARIANTS GLU-1961 AND ASN-2177.
RX PubMed=11346402; DOI=10.1001/archopht.119.5.745;
RA Guymer R.H., Heon E., Lotery A.J., Munier F.L., Schorderet D.F.,
RA Baird P.N., McNeil R.J., Haines H.L., Sheffield V.C., Stone E.M.;
RT "Variation of codons 1961 and 2177 of the Stargardt disease gene is not
RT associated with age-related macular degeneration.";
RL Arch. Ophthalmol. 119:745-751(2001).
RN [33]
RP VARIANTS FFM GLY-339; ALA-863; TRP-943; ARG-991; VAL-1038; CYS-1108;
RP ARG-1488; THR-1562; GLN-1640; PHE-2027; GLN-2030 AND CYS-2106, AND VARIANTS
RP HIS-212; ARG-423; GLN-943; THR-1148; ILE-1868 AND ILE-2255.
RX PubMed=11379881; DOI=10.1007/s004390100493;
RA Yatsenko A.N., Shroyer N.F., Lewis R.A., Lupski J.R.;
RT "Late-onset Stargardt disease is associated with missense mutations that
RT map outside known functional regions of ABCR (ABCA4).";
RL Hum. Genet. 108:346-355(2001).
RN [34]
RP VARIANTS STGD1 SER-686; TRP-1055; ASP-1799; ASP-1805; PRO-1940 AND
RP HIS-2107, VARIANTS FFM MET-1253 AND PRO-1940, VARIANTS CORD3 CYS-212 AND
RP ARG-2060, AND VARIANTS GLN-943; LEU-1948 AND ILE-2255.
RX PubMed=11385708; DOI=10.1002/humu.1133;
RA Paloma E., Martinez-Mir A., Vilageliu L., Gonzalez-Duarte R., Balcells S.;
RT "Spectrum of ABCA4 (ABCR) gene mutations in Spanish patients with autosomal
RT recessive macular dystrophies.";
RL Hum. Mutat. 17:504-510(2001).
RN [35]
RP VARIANTS STGD1, AND VARIANTS.
RX PubMed=11328725;
RA Webster A.R., Heon E., Lotery A.J., Vandenburgh K., Casavant T.L., Oh K.T.,
RA Beck G., Fishman G.A., Lam B.L., Levin A., Heckenlively J.R.,
RA Jacobson S.G., Weleber R.G., Sheffield V.C., Stone E.M.;
RT "An analysis of allelic variation in the ABCA4 gene.";
RL Invest. Ophthalmol. Vis. Sci. 42:1179-1189(2001).
RN [36]
RP VARIANTS STGD1 13-LYS--TRP-15 DEL; TYR-54; LYS-58; VAL-60; GLU-65; GLU-77;
RP HIS-190; PRO-244; ARG-309; CYS-525; CYS-537; PRO-541; PRO-549; ARG-550;
RP GLN-602; ARG-607; MET-643; ASP-767; PRO-797; ARG-821; THR-824; ALA-863;
RP ALA-935; TRP-943; ALA-989; VAL-1038; CYS-1108; LEU-1108; LYS-1122;
RP ARG-1201; GLN-1300; LEU-1380; PRO-1388; ARG-1408; LEU-1486; ARG-1488;
RP TYR-1490; MET-1526; ASN-1532; THR-1562; TRP-1640; LEU-1776; THR-1846;
RP GLU-1961; SER-1977; PHE-2027; GLN-2030; PRO-2035; LEU-2050; CYS-2107;
RP HIS-2107; TRP-2139; ARG-2150 AND TYR-2150, VARIANTS CORD3 GLN-1640 AND
RP ASP-2146, AND VARIANTS HIS-212; ARG-423; GLN-943; THR-1637; ILE-1868 AND
RP LEU-1948.
RX PubMed=11527935;
RA Briggs C.E., Rucinski D., Rosenfeld P.J., Hirose T., Berson E.L.,
RA Dryja T.P.;
RT "Mutations in ABCR (ABCA4) in patients with Stargardt macular degeneration
RT or cone-rod degeneration.";
RL Invest. Ophthalmol. Vis. Sci. 42:2229-2236(2001).
RN [37]
RP VARIANT ARG-423.
RX PubMed=12111378; DOI=10.1007/s100380200041;
RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
RA Harigae S., Osawa S., Nakamura Y.;
RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8.";
RL J. Hum. Genet. 47:285-310(2002).
RN [38]
RP VARIANTS STGD1 TRP-18; LYS-96; VAL-108; LEU-143; GLN-152; HIS-212; GLN-223;
RP SER-230; 245-TYR--ASP-2273 DEL; THR-246; GLU-498; PRO-541; ARG-550;
RP GLN-572; 639-TYR--ASP-2273 DEL; SER-641; CYS-653; VAL-690;
RP 700-TRP--ASP-2273 DEL; ASP-767; ARG-821; ALA-863; 876-GLN--ASP-2273 DEL;
RP ILE-897; ASP-954; SER-965; ASP-978; LYS-1022; VAL-1038; ASP-1050; LYS-1087;
RP CYS-1098; PRO-1099; CYS-1108; HIS-1108; LEU-1129; ARG-1203; ASP-1203;
RP 1300-ARG--ASP-2273 DEL; GLN-1300; TYR-1490; ARG-1512; MET-1526; ASP-1598;
RP 1652-TYR--ASP-2273 DEL; ASP-1762; ASN-1838; TYR-1838; GLU-1961; PHE-1970;
RP PHE-2027; GLN-2030; LEU-2050; HIS-2107; TRP-2139; LEU-2149; TYR-2150;
RP ASN-2177 AND VAL-2241, AND VARIANTS ARG-423; GLN-943; ASN-1204; LEU-1380;
RP ILE-1868 AND LEU-1948.
RX PubMed=15192030; DOI=10.1373/clinchem.2004.033241;
RA Stenirri S., Fermo I., Battistella S., Galbiati S., Soriani N., Paroni R.,
RA Manitto M.P., Martina E., Brancato R., Allikmets R., Ferrari M.,
RA Cremonesi L.;
RT "Denaturing HPLC profiling of the ABCA4 gene for reliable detection of
RT allelic variations.";
RL Clin. Chem. 50:1336-1343(2004).
RN [39]
RP VARIANT [LARGE SCALE ANALYSIS] MET-224.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [40]
RP VARIANTS ARMD2 GLU-762; LEU-1129; CYS-1724; SER-1977; ASN-2047 AND
RP TYR-2137, AND VARIANT ILE-552.
RX PubMed=19028736; DOI=10.1136/bjo.2008.145193;
RA Aguirre-Lamban J., Riveiro-Alvarez R., Maia-Lopes S., Cantalapiedra D.,
RA Vallespin E., Avila-Fernandez A., Villaverde-Montero C.,
RA Trujillo-Tiebas M.J., Ramos C., Ayuso C.;
RT "Molecular analysis of the ABCA4 gene for reliable detection of allelic
RT variations in Spanish patients: identification of 21 novel variants.";
RL Br. J. Ophthalmol. 93:614-621(2009).
RN [41]
RP VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602;
RP ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965; MET-1019;
RP HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490; GLN-1640;
RP TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977; PHE-2027;
RP ARG-2060; HIS-2107; TYR-2150 AND VAL-2241.
RX PubMed=18977788; DOI=10.1136/bjo.2008.148155;
RA Riveiro-Alvarez R., Aguirre-Lamban J., Lopez-Martinez M.A.,
RA Trujillo-Tiebas M.J., Cantalapiedra D., Vallespin E., Avila-Fernandez A.,
RA Ramos C., Ayuso C.;
RT "Frequency of ABCA4 mutations in 278 Spanish controls: an insight into the
RT prevalence of autosomal recessive Stargardt disease.";
RL Br. J. Ophthalmol. 93:1359-1364(2009).
RN [42]
RP VARIANTS STGD1 21-GLN--ASP-2273 DEL; LEU-68; HIS-96; LYS-96; SER-172;
RP CYS-212; LYS-415; PRO-541; 572-ARG--ASP-2273 DEL; LYS-616; CYS-653;
RP VAL-690; 700-TRP--ASP-2273 DEL; ASP-767; ARG-821; ARG-840; MET-931;
RP SER-965; PRO-970; PRO-977; ASP-978; MET-1019; VAL-1038; TRP-1055; GLU-1078;
RP LYS-1087; CYS-1098; 1099-SER--ASP-2273 DEL; CYS-1108; 1177-CYS--ASP-2273
RP DEL; 1332-GLN--ASP-2273 DEL; LEU-1380; 1408-TRP--ASP-2273 DEL; ILE-1433;
RP 1461-TRP--ASP-2273 DEL; 1479-TRP--ASP-2273 DEL; SER-1484; MET-1526;
RP ASP-1598; ASN-1696; GLU-1961; PHE-1970; SER-1977; 2030-ARG--ASP-2273 DEL;
RP LYS-2096; GLN-2140 AND PRO-2221.
RX PubMed=19265867; DOI=10.1038/eye.2009.35;
RA Passerini I., Sodi A., Giambene B., Mariottini A., Menchini U.,
RA Torricelli F.;
RT "Novel mutations in of the ABCR gene in Italian patients with Stargardt
RT disease.";
RL Eye 24:158-164(2010).
RN [43]
RP VARIANT LEU-2050.
RX PubMed=20335603; DOI=10.1167/iovs.09-4655;
RA Poloschek C.M., Bach M., Lagreze W.A., Glaus E., Lemke J.R., Berger W.,
RA Neidhardt J.;
RT "ABCA4 and ROM1: implications for modification of the PRPH2-associated
RT macular dystrophy phenotype.";
RL Invest. Ophthalmol. Vis. Sci. 51:4253-4265(2010).
RN [44]
RP VARIANTS 219-ARG--ASP-2273 DEL; HIS-576; ARG-1488; MET-1526; CYS-1557;
RP THR-1562; GLU-1773; ASP-1794; 2040-ARG--ASP-2273 DEL AND CYS-2107, AND
RP VARIANTS STGD1 TYR-54; GLN-152; ARG-184; PHE-184; CYS-212; SER-418;
RP LYS-471; MET-643; CYS-653; 782-TRP--ASP-2273 DEL; ALA-863; GLN-943;
RP ALA-989; ARG-991; MET-1019; LYS-1022; SER-1097; CYS-1108; LYS-1122;
RP LEU-1129; ARG-1201; LEU-1380; LYS-1442; LEU-1486; TYR-1490; ASP-1598;
RP ASP-1754; THR-1846; GLU-1961; PHE-2027; GLN-2030; CYS-2106; LYS-2131;
RP TYR-2150 AND PRO-2237.
RX PubMed=23143460; DOI=10.1001/archophthalmol.2012.1697;
RA Downes S.M., Packham E., Cranston T., Clouston P., Seller A., Nemeth A.H.;
RT "Detection rate of pathogenic mutations in ABCA4 using direct sequencing:
RT clinical and research implications.";
RL Arch. Ophthalmol. 130:1486-1490(2012).
RN [45]
RP VARIANTS STGD1 TRP-18; HIS-24; 89-GLU--ASP-2273 DEL; CYS-212; ASP-241;
RP TRP-290; TRP-602; GLU-818; SER-965; ARG-1014; LEU-1129; LEU-1380; PHE-1416
RP DEL; HIS-1443; TRP-1551 DEL; THR-1556; 1681-VAL--VAL-1685 DEL; GLN-1705;
RP VAL-1773; ASN-1775; HIS-1779; ILE-1868; GLN-1942; VAL-2074 AND ARG-2128,
RP AND VARIANTS GLN-943 AND ILE-2255.
RX PubMed=23419329; DOI=10.1016/j.exer.2013.02.006;
RA Chacon-Camacho O.F., Granillo-Alvarez M., Ayala-Ramirez R., Zenteno J.C.;
RT "ABCA4 mutational spectrum in Mexican patients with Stargardt disease:
RT Identification of 12 novel mutations and evidence of a founder effect for
RT the common p.A1773V mutation.";
RL Exp. Eye Res. 109:77-82(2013).
RN [46]
RP VARIANT STGD1 TRP-602.
RX PubMed=24444108; DOI=10.1186/1471-2350-15-11;
RA Ortube M.C., Strom S.P., Nelson S.F., Nusinowitz S., Martinez A.,
RA Gorin M.B.;
RT "Whole exome sequencing detects homozygosity for ABCA4 p.Arg602Trp missense
RT mutation in a pediatric patient with rapidly progressive retinal
RT dystrophy.";
RL BMC Med. Genet. 15:11-11(2014).
RN [47]
RP VARIANTS STGD1 CYS-212; PRO-541; LEU-640; ASP-767; VAL-1038; CYS-1108;
RP ARG-1408; GLN-1640; TRP-1640; ASP-1838; GLU-1961 AND HIS-2107.
RX PubMed=24457364; DOI=10.1136/bjophthalmol-2013-304270;
RA Miraldi Utz V., Coussa R.G., Marino M.J., Chappelow A.V., Pauer G.J.,
RA Hagstrom S.A., Traboulsi E.I.;
RT "Predictors of visual acuity and genotype-phenotype correlates in a cohort
RT of patients with Stargardt disease.";
RL Br. J. Ophthalmol. 98:513-518(2014).
RN [48]
RP VARIANTS CORD3 CYS-440; GLY-643; HIS-1145; GLU-1203; LEU-2050 AND ASN-2177,
RP VARIANTS STGD1 HIS-24; GLU-65; SER-247; 431-TRP--ASP-2273 DEL; PRO-541;
RP ARG-607; HIS-653; ALA-863; 1029-GLN--ASP-2273 DEL; VAL-1038; GLN-1300;
RP MET-1537; TRP-1640; PRO-1763; HIS-1898; GLU-1961; PHE-1970; PHE-2027;
RP GLN-2030 AND ARG-2033, VARIANTS RP19 MET-455 AND ILE-552, VARIANTS
RP 681-ARG--ASP-2273 DEL; ASP-767 AND ARG-1591, AND VARIANT CORD3 GLU-1961.
RX PubMed=25346251; DOI=10.1002/humu.22716;
RA Bauwens M., De Zaeytijd J., Weisschuh N., Kohl S., Meire F., Dahan K.,
RA Depasse F., De Jaegere S., De Ravel T., De Rademaeker M., Loeys B.,
RA Coppieters F., Leroy B.P., De Baere E.;
RT "An augmented ABCA4 screen targeting noncoding regions reveals a deep
RT intronic founder variant in Belgian Stargardt patients.";
RL Hum. Mutat. 36:39-42(2015).
RN [49]
RP VARIANTS STGD1 LYS-14; PRO-18; HIS-24; VAL-72; CYS-97; 185-GLN--ASP-2273
RP DEL; ARG-240; LEU-291; 326-TYR--ASP-2273 DEL; VAL-328; SER-345; THR-410;
RP CYS-508; CYS-511; ARG-519; 533-GLN--ASP-2273 DEL; CYS-537; ARG-548;
RP ARG-550; LEU-593; TRP-602; CYS-603; ARG-607; ASN-645; HIS-653; SER-754;
RP 808-TYR--ASP-2273 DEL; VAL-816; SER-965; TYR-965; SER-973; MET-1019;
RP GLY-1022; LYS-1036; LEU-1074; THR-1094; HIS-1108; LYS-1122; THR-1130;
RP TRP-1140; SER-1159; HIS-1161; 1300-ARG--ASP-2273 DEL; ASN-1371;
RP 1453-TYR--ASP-2273 DEL; LEU-1503; HIS-1511; MET-1526; ARG-1591;
RP 1724-TRP--ASP-2273 DEL; VAL-1773; LEU-1776; TRP-1843; ILE-1868; LYS-1885;
RP GLY-1921; MET-1921; ARG-1961; SER-1977; TYR-2017; THR-2023;
RP 2030-ARG--ASP-2273 DEL; ARG-2032; TRP-2038; 2040-ARG--ASP-2273 DEL;
RP GLN-2040; GLY-2042; THR-2064; GLU-2078; SER-2097; ARG-2150 AND SER-2188,
RP VARIANTS ARG-423; TYR-1102; THR-1209; MET-1428; MET-1572;
RP 1618-TRP--ASP-2273 DEL; VAL-1623; GLN-1640; 1652-TYR--ASP-2273 DEL AND
RP ILE-2255, AND VARIANTS CORD3 53-GLU--ASP-2273 DEL; ARG-55; PRO-63;
RP 107-ARG--ASP-2273 DEL; 218-GLN--ASP-2273 DEL; CYS-320; 339-TRP--ASP-2273
RP DEL; 605-TRP--ASP-2273 DEL; LYS-636; ARG-661; CYS-1183; CYS-1368;
RP 1479-TRP--ASP-2273 DEL; 1650-GLU--ASP-2273 DEL; ILE-1882; SER-2043;
RP HIS-2107 AND ASP-2146.
RX PubMed=26780318; DOI=10.1167/iovs.15-18190;
RA Jiang F., Pan Z., Xu K., Tian L., Xie Y., Zhang X., Chen J., Dong B.,
RA Li Y.;
RT "Screening of ABCA4 Gene in a Chinese Cohort With Stargardt Disease or
RT Cone-Rod Dystrophy With a Report on 85 Novel Mutations.";
RL Invest. Ophthalmol. Vis. Sci. 57:145-152(2016).
RN [50]
RP VARIANTS STGD1 ARG-72; PRO-541; VAL-1038; GLU-1091; PRO-1794 AND TRP-2077,
RP CHARACTERIZATION OF VARIANTS STGD1 ARG-72; PRO-541; VAL-1038; GLU-1091;
RP PRO-1794 AND TRP-2077, MUTAGENESIS OF ALA-1357, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29847635; DOI=10.1167/iovs.17-23364;
RA Garces F., Jiang K., Molday L.L., Stoehr H., Weber B.H., Lyons C.J.,
RA Maberley D., Molday R.S.;
RT "Correlating the Expression and Functional Activity of ABCA4 Disease
RT Variants With the Phenotype of Patients With Stargardt Disease.";
RL Invest. Ophthalmol. Vis. Sci. 59:2305-2315(2018).
RN [51]
RP VARIANTS ALA-863; GLY-863 DEL AND ILE-1868.
RX PubMed=30120214; DOI=10.1136/jmedgenet-2018-105364;
RA de Bruijn S.E., Verbakel S.K., de Vrieze E., Kremer H., Cremers F.P.M.,
RA Hoyng C.B., van den Born L.I., Roosing S.;
RT "Homozygous variants in KIAA1549, encoding a ciliary protein, are
RT associated with autosomal recessive retinitis pigmentosa.";
RL J. Med. Genet. 55:705-712(2018).
RN [52]
RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS STGD1 CYS-653;
RP HIS-653; ARG-661; SER-686; VAL-690; MET-716; TYR-764; ARG-765; ASN-765;
RP ASP-767; PRO-797; GLU-818; ARG-821; THR-824; ARG-840; ALA-849; ASP-851;
RP THR-854; LEU-1380; LYS-1399; ASN-1696; GLU-1703; LYS-1703; LEU-1705;
RP VAL-1773; ASP-1794; PRO-1794; ASP-1805; ASN-1838; ASP-1838; TYR-1838;
RP TRP-1843; ILE-1868 AND HIS-1898, CHARACTERIZATION OF VARIANTS HIS-846;
RP GLU-1773 AND CYS-1898, AND MUTAGENESIS OF HIS-1838.
RX PubMed=33375396; DOI=10.3390/ijms22010185;
RA Garces F.A., Scortecci J.F., Molday R.S.;
RT "Functional Characterization of ABCA4 Missense Variants Linked to Stargardt
RT Macular Degeneration.";
RL Int. J. Mol. Sci. 22:0-0(2020).
CC -!- FUNCTION: Flippase that catalyzes in an ATP-dependent manner the
CC transport of retinal-phosphatidylethanolamine conjugates like the 11-
CC cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine
CC from the lumen to the cytoplasmic leaflet of photoreceptor outer
CC segment disk membranes, where N-cis-retinylidene-
CC phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-
CC trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-
CC retinol (all-trans-rol) and therefore prevents the accumulation of
CC excess of 11-cis-retinal and its schiff-base conjugate and the
CC formation of toxic bisretinoid (PubMed:24097981, PubMed:22735453,
CC PubMed:23144455, PubMed:20404325, PubMed:10075733, PubMed:29847635,
CC PubMed:33375396). May display both ATPase and GTPase activity that is
CC strongly influenced by the lipid environment and the presence of
CC retinoid compounds (PubMed:22735453). Binds the unprotonated form of N-
CC retinylidene-phosphatidylethanolamine with high affinity in the absence
CC of ATP, and ATP binding and hydrolysis induce a protein conformational
CC change that causes the dissociation of N-retinylidene-
CC phosphatidylethanolamine (By similarity).
CC {ECO:0000250|UniProtKB:F1MWM0, ECO:0000269|PubMed:10075733,
CC ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:22735453,
CC ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:24097981,
CC ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-all-trans-
CC retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-
CC retinylidenephosphatidylethanolamine(in) + phosphate;
CC Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189;
CC Evidence={ECO:0000305|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:24097981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24097981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:24097981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out)
CC = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) +
CC phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167887, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F1MWM0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193;
CC Evidence={ECO:0000250|UniProtKB:F1MWM0};
CC -!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and
CC ceramide. ATPase activity is stimulated by phosphatidylethanolamine.
CC Phospholipids translocase activity is highly reduced by berylium
CC fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid
CC translocase activity. {ECO:0000269|PubMed:24097981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for ATP {ECO:0000269|PubMed:33605212};
CC Vmax=112.5 nmol/min/mg enzyme (for ATP hydrolysis)
CC {ECO:0000269|PubMed:33605212};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10075733}; Multi-
CC pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:24097981}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000250|UniProtKB:F1MWM0}. Note=Localized to the rim and incisures
CC of rod outer segments disks. {ECO:0000250|UniProtKB:F1MWM0}.
CC -!- TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively found in
CC the rims of rod photoreceptor cells.
CC -!- DOMAIN: The second extracellular domain (ECD2, aa 1395-1680) undergoes
CC conformational change in response to its specific interaction with its
CC substrate all-trans-retinal (PubMed:20404325). Nucleotide binding
CC domain 1 (NBD1, aa 854-1375) binds preferentially and with high
CC affinity with the 11-cis retinal (PubMed:23144455).
CC {ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23144455}.
CC -!- PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal
CC fragment and a 115-kDa C-terminal fragment that are linked through
CC disulfide bonds. {ECO:0000269|PubMed:11320094}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11320094}.
CC -!- PTM: Phosphorylation is independent of light exposure and modulates
CC ATPase activity. {ECO:0000250|UniProtKB:F1MWM0}.
CC -!- DISEASE: Stargardt disease 1 (STGD1) [MIM:248200]: A common hereditary
CC macular degeneration. It is characterized by decreased central vision,
CC atrophy of the macula and underlying retinal pigment epithelium, and
CC frequent presence of prominent flecks in the posterior pole of the
CC retina. {ECO:0000269|PubMed:10090887, ECO:0000269|PubMed:10206579,
CC ECO:0000269|PubMed:10612508, ECO:0000269|PubMed:10634594,
CC ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10746567,
CC ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11328725,
CC ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935,
CC ECO:0000269|PubMed:11594993, ECO:0000269|PubMed:15192030,
CC ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867,
CC ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:22735453,
CC ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23144455,
CC ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24097981,
CC ECO:0000269|PubMed:24444108, ECO:0000269|PubMed:24457364,
CC ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318,
CC ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396,
CC ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9490294,
CC ECO:0000269|PubMed:9503029, ECO:0000269|PubMed:9781034,
CC ECO:0000269|PubMed:9973280}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal recessive
CC retinal disorder very similar to Stargardt disease. In contrast to
CC Stargardt disease, FFM is characterized by later onset and slowly
CC progressive course. {ECO:0000269|PubMed:10634594,
CC ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11385708,
CC ECO:0000269|PubMed:9781034}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Macular degeneration, age-related, 2 (ARMD2) [MIM:153800]: A
CC form of age-related macular degeneration, a multifactorial eye disease
CC and the most common cause of irreversible vision loss in the developed
CC world. In most patients, the disease is manifest as ophthalmoscopically
CC visible yellowish accumulations of protein and lipid that lie beneath
CC the retinal pigment epithelium and within an elastin-containing
CC structure known as Bruch membrane. {ECO:0000269|PubMed:19028736,
CC ECO:0000269|PubMed:9295268}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited
CC retinal dystrophy characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10958761,
CC ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935,
CC ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Retinitis pigmentosa 19 (RP19) [MIM:601718]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. RP19 is characterized by choroidal
CC atrophy. {ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10958763,
CC ECO:0000269|PubMed:25346251}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the ABCA4 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/abcrmut.htm";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U88667; AAC51144.1; -; mRNA.
DR EMBL; AF000148; AAC23915.1; -; mRNA.
DR EMBL; Y15635; CAA75729.1; -; Genomic_DNA.
DR EMBL; Y15636; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15637; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15638; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15639; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15640; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15641; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15642; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15643; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15644; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15645; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15646; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15647; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15648; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15649; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15650; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15651; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15652; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15653; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15654; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15655; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15656; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15657; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15658; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15659; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15660; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15661; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15662; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15663; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15664; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15665; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15666; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15667; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15668; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15669; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15670; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15671; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15672; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15673; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15674; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15675; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15676; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15677; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15678; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15679; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15680; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15681; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15682; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15683; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; Y15684; CAA75729.1; JOINED; Genomic_DNA.
DR EMBL; AF001945; AAC05632.1; -; mRNA.
DR EMBL; AB210040; BAE06122.1; ALT_INIT; mRNA.
DR EMBL; AC093579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ426859; ABD90529.1; -; mRNA.
DR CCDS; CCDS747.1; -.
DR RefSeq; NP_000341.2; NM_000350.2.
DR PDB; 7E7I; EM; 3.30 A; A=1-2273.
DR PDB; 7E7O; EM; 3.40 A; A=1-2273.
DR PDB; 7E7Q; EM; 3.30 A; A=1-2273.
DR PDB; 7LKP; EM; 3.27 A; A=1-2273.
DR PDB; 7LKZ; EM; 3.27 A; A=1-2273.
DR PDB; 7M1P; EM; 3.60 A; A=1-2273.
DR PDB; 7M1Q; EM; 2.92 A; A=1-2273.
DR PDBsum; 7E7I; -.
DR PDBsum; 7E7O; -.
DR PDBsum; 7E7Q; -.
DR PDBsum; 7LKP; -.
DR PDBsum; 7LKZ; -.
DR PDBsum; 7M1P; -.
DR PDBsum; 7M1Q; -.
DR AlphaFoldDB; P78363; -.
DR SMR; P78363; -.
DR BioGRID; 106542; 3.
DR ELM; P78363; -.
DR IntAct; P78363; 2.
DR STRING; 9606.ENSP00000359245; -.
DR SwissLipids; SLP:000000347; -.
DR TCDB; 3.A.1.211.2; the atp-binding cassette (abc) superfamily.
DR GlyGen; P78363; 8 sites.
DR iPTMnet; P78363; -.
DR PhosphoSitePlus; P78363; -.
DR BioMuta; ABCA4; -.
DR DMDM; 6707663; -.
DR EPD; P78363; -.
DR MassIVE; P78363; -.
DR PaxDb; P78363; -.
DR PeptideAtlas; P78363; -.
DR PRIDE; P78363; -.
DR ProteomicsDB; 57593; -.
DR Antibodypedia; 33661; 192 antibodies from 32 providers.
DR DNASU; 24; -.
DR Ensembl; ENST00000370225.4; ENSP00000359245.3; ENSG00000198691.14.
DR GeneID; 24; -.
DR KEGG; hsa:24; -.
DR MANE-Select; ENST00000370225.4; ENSP00000359245.3; NM_000350.3; NP_000341.2.
DR UCSC; uc001dqh.4; human.
DR CTD; 24; -.
DR DisGeNET; 24; -.
DR GeneCards; ABCA4; -.
DR GeneReviews; ABCA4; -.
DR HGNC; HGNC:34; ABCA4.
DR HPA; ENSG00000198691; Group enriched (choroid plexus, retina).
DR MalaCards; ABCA4; -.
DR MIM; 153800; phenotype.
DR MIM; 248200; phenotype.
DR MIM; 601691; gene.
DR MIM; 601718; phenotype.
DR MIM; 604116; phenotype.
DR neXtProt; NX_P78363; -.
DR OpenTargets; ENSG00000198691; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR Orphanet; 791; Retinitis pigmentosa.
DR Orphanet; 827; Stargardt disease.
DR PharmGKB; PA24379; -.
DR VEuPathDB; HostDB:ENSG00000198691; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000155624; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; P78363; -.
DR OMA; DPVYSYD; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; P78363; -.
DR TreeFam; TF105191; -.
DR PathwayCommons; P78363; -.
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR SignaLink; P78363; -.
DR BioGRID-ORCS; 24; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; ABCA4; human.
DR GeneWiki; ABCA4; -.
DR GenomeRNAi; 24; -.
DR Pharos; P78363; Tbio.
DR PRO; PR:P78363; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P78363; protein.
DR Bgee; ENSG00000198691; Expressed in pigmented layer of retina and 102 other tissues.
DR ExpressionAtlas; P78363; baseline and differential.
DR Genevisible; P78363; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0120202; C:rod photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140327; F:flippase activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0140347; F:N-retinylidene-phosphatidylethanolamine flippase activity; ISS:UniProtKB.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IDA:BHF-UCL.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0005501; F:retinoid binding; ISS:UniProtKB.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
DR GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
DR GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR005951; ABCA4/ABCR.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01257; rim_protein; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Age-related macular degeneration; ATP-binding;
KW Cell projection; Cone-rod dystrophy; Cytoplasmic vesicle; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Retinitis pigmentosa; Sensory transduction; Stargardt disease; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..2273
FT /note="Retinal-specific phospholipid-transporting ATPase
FT ABCA4"
FT /id="PRO_0000093301"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..646
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:11320094"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..730
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..835
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..1376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1377..1397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1398..1727
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:11320094"
FT TRANSMEM 1728..1748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1749..1759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1760..1780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1781..1792
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1793..1813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1814..1831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1832..1852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1853..1873
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1874..1894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1895..2273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 929..1160
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1938..2170
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 891..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2244..2249
FT /note="Essential for ATP binding and ATPase activity"
FT /evidence="ECO:0000269|PubMed:31481235"
FT COMPBIAS 1327..1341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 963..970
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKZ"
FT BINDING 1054
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKZ"
FT BINDING 1972..1980
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKZ"
FT BINDING 2073..2074
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKZ"
FT SITE 1309
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 901
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 1313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP"
FT CARBOHYD 1469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 1529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 1588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT CARBOHYD 1662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11320094,
FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP,
FT ECO:0007744|PDB:7LKZ"
FT DISULFID 54..81
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT DISULFID 75..324
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT DISULFID 370..519
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT DISULFID 641..1490
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT DISULFID 1444..1455
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT DISULFID 1488..1502
FT /evidence="ECO:0000269|PubMed:33605212,
FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ"
FT VARIANT 11
FT /note="L -> P (in FFM; dbSNP:rs62645946)"
FT /evidence="ECO:0000269|PubMed:9781034"
FT /id="VAR_012493"
FT VARIANT 13..15
FT /note="Missing (in STGD1)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012494"
FT VARIANT 14
FT /note="N -> K (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084833"
FT VARIANT 18
FT /note="R -> P (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084834"
FT VARIANT 18
FT /note="R -> W (in STGD1; dbSNP:rs121909205)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:9503029,
FT ECO:0000269|PubMed:9781034"
FT /id="VAR_008398"
FT VARIANT 21..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084835"
FT VARIANT 24
FT /note="R -> H (in STGD1; unknown pathological significance;
FT dbSNP:rs62645958)"
FT /evidence="ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318"
FT /id="VAR_008399"
FT VARIANT 53..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance; dbSNP:rs764744217)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084836"
FT VARIANT 54
FT /note="C -> Y (in STGD1; dbSNP:rs150774447)"
FT /evidence="ECO:0000269|PubMed:10612508,
FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_008400"
FT VARIANT 55
FT /note="H -> R (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084837"
FT VARIANT 58
FT /note="N -> K (in STGD1; dbSNP:rs61748524)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012495"
FT VARIANT 60
FT /note="A -> E (in STGD1)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012496"
FT VARIANT 60
FT /note="A -> T (in STGD1; dbSNP:rs61751411)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012497"
FT VARIANT 60
FT /note="A -> V (in STGD1; dbSNP:rs55732384)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:11527935"
FT /id="VAR_008492"
FT VARIANT 63
FT /note="S -> P (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084838"
FT VARIANT 65
FT /note="G -> E (in STGD1 and CORD3; dbSNP:rs62654395)"
FT /evidence="ECO:0000269|PubMed:10958761,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:25346251"
FT /id="VAR_008401"
FT VARIANT 68
FT /note="P -> L (in STGD1; dbSNP:rs62654397)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_012498"
FT VARIANT 68
FT /note="P -> R (in STGD1; dbSNP:rs62654397)"
FT /id="VAR_012499"
FT VARIANT 72
FT /note="G -> R (in STGD1; does not affect intracellular
FT vesicle localization; does not affect solubility;
FT significantly reduces N-Ret-PE binding; drastically reduces
FT basal ATPase activity with little or no all trans retinal
FT stimulation; dbSNP:rs61751412)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:29847635"
FT /id="VAR_012500"
FT VARIANT 72
FT /note="G -> V (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084839"
FT VARIANT 75
FT /note="C -> G (in STGD1; dbSNP:rs61748526)"
FT /id="VAR_008402"
FT VARIANT 77
FT /note="V -> E (in STGD1; dbSNP:rs61748527)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012501"
FT VARIANT 89..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085009"
FT VARIANT 96
FT /note="N -> D (in STGD1; dbSNP:rs61748529)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_008403"
FT VARIANT 96
FT /note="N -> H (in STGD1; unknown pathological significance;
FT dbSNP:rs61748529)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_008404"
FT VARIANT 96
FT /note="N -> K (in STGD1; unknown pathological significance;
FT dbSNP:rs886039297)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_084840"
FT VARIANT 97
FT /note="Y -> C (in STGD1; unknown pathological significance;
FT dbSNP:rs755691060)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084841"
FT VARIANT 100
FT /note="S -> P (in STGD1; highly decreased protein
FT abundance; highly decreased ATPase activity; highly
FT decreased phospholipid translocase activity;
FT dbSNP:rs61748530)"
FT /evidence="ECO:0000269|PubMed:24097981"
FT /id="VAR_012502"
FT VARIANT 107..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance; dbSNP:rs765429911)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084842"
FT VARIANT 108
FT /note="D -> V (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084843"
FT VARIANT 143
FT /note="P -> L (in STGD1; unknown pathological significance;
FT dbSNP:rs62646860)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084844"
FT VARIANT 152
FT /note="R -> Q (in STGD1; dbSNP:rs62646862)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23143460"
FT /id="VAR_012503"
FT VARIANT 156
FT /note="I -> V (in STGD1; dbSNP:rs62646863)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_012504"
FT VARIANT 172
FT /note="G -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs61748532)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084845"
FT VARIANT 184
FT /note="S -> F (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084846"
FT VARIANT 184
FT /note="S -> R (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084847"
FT VARIANT 185..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084848"
FT VARIANT 190
FT /note="Q -> H (in STGD1; dbSNP:rs281865397)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012505"
FT VARIANT 192
FT /note="A -> T (in STGD1; dbSNP:rs61748535)"
FT /id="VAR_008405"
FT VARIANT 206
FT /note="S -> R (in STGD1; reduced basal and retinal-
FT stimulated ATP-hydrolysis; dbSNP:rs61748536)"
FT /evidence="ECO:0000269|PubMed:10206579"
FT /id="VAR_012506"
FT VARIANT 212
FT /note="R -> C (in STGD1 and CORD3; common mutation in
FT southern Europe; reduced ATP-binding capacity;
FT dbSNP:rs61750200)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:9503029, ECO:0000269|PubMed:9781034"
FT /id="VAR_008406"
FT VARIANT 212
FT /note="R -> H (in STGD1; dbSNP:rs6657239)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030"
FT /id="VAR_012507"
FT VARIANT 218..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084849"
FT VARIANT 219..2273
FT /note="Missing (found in a patient with chorioretinal
FT atrophy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084850"
FT VARIANT 220
FT /note="R -> C (in STGD1; dbSNP:rs61748538)"
FT /id="VAR_012508"
FT VARIANT 223
FT /note="K -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs147619585)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084851"
FT VARIANT 224
FT /note="T -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs373540612)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035736"
FT VARIANT 230
FT /note="C -> S (in STGD1; dbSNP:rs1057518767)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:15192030"
FT /id="VAR_012509"
FT VARIANT 240
FT /note="I -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs1553195472)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084852"
FT VARIANT 241
FT /note="E -> D (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085010"
FT VARIANT 244
FT /note="L -> P (in STGD1; dbSNP:rs62646864)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012510"
FT VARIANT 245..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084853"
FT VARIANT 246
FT /note="A -> T (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084854"
FT VARIANT 247
FT /note="N -> S (in STGD1; dbSNP:rs62645950)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:25346251"
FT /id="VAR_012511"
FT VARIANT 249
FT /note="D -> G (in STGD1; dbSNP:rs62646865)"
FT /id="VAR_008407"
FT VARIANT 290
FT /note="R -> W (in STGD1; unknown pathological significance;
FT dbSNP:rs781716640)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085011"
FT VARIANT 291
FT /note="P -> L (in STGD1; unknown pathological significance;
FT dbSNP:rs190540405)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084855"
FT VARIANT 300
FT /note="T -> N (in STGD1; dbSNP:rs61748544)"
FT /evidence="ECO:0000269|PubMed:10206579"
FT /id="VAR_008408"
FT VARIANT 309
FT /note="P -> R (in STGD1; dbSNP:rs61748545)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012512"
FT VARIANT 320
FT /note="S -> C (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084856"
FT VARIANT 326..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance; dbSNP:rs747540967)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084857"
FT VARIANT 328
FT /note="E -> V (in STGD1; dbSNP:rs61751419)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012513"
FT VARIANT 333
FT /note="R -> W (in STGD1; dbSNP:rs61748546)"
FT /id="VAR_012514"
FT VARIANT 336
FT /note="S -> C (in STGD1; dbSNP:rs61748547)"
FT /id="VAR_008409"
FT VARIANT 339..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084858"
FT VARIANT 339
FT /note="W -> G (in FFM; dbSNP:rs61751420)"
FT /evidence="ECO:0000269|PubMed:11379881"
FT /id="VAR_012515"
FT VARIANT 340
FT /note="Y -> D (in STGD1; dbSNP:rs61748548)"
FT /evidence="ECO:0000269|PubMed:10746567"
FT /id="VAR_008410"
FT VARIANT 345
FT /note="Y -> S (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084859"
FT VARIANT 380
FT /note="N -> K (in STGD1; dbSNP:rs61748549)"
FT /evidence="ECO:0000269|PubMed:18977788"
FT /id="VAR_012516"
FT VARIANT 407
FT /note="A -> V (in STGD1 and CORD3; dbSNP:rs61751264)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_008411"
FT VARIANT 410
FT /note="I -> T (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084860"
FT VARIANT 415
FT /note="N -> K (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084861"
FT VARIANT 418
FT /note="F -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs794726979)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084862"
FT VARIANT 423
FT /note="H -> R (benign variant; dbSNP:rs3112831)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11384574,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:12111378,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:26780318"
FT /id="VAR_012517"
FT VARIANT 424
FT /note="V -> A (in STGD1 and RP19; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_085012"
FT VARIANT 431..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084863"
FT VARIANT 440
FT /note="Y -> C (in CORD3; unknown pathological significance;
FT dbSNP:rs770439859)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084864"
FT VARIANT 445
FT /note="S -> R (in STGD1; dbSNP:rs61748552)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_008412"
FT VARIANT 455
FT /note="L -> M (in RP19; unknown pathological significance;
FT dbSNP:rs764170051)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084865"
FT VARIANT 471
FT /note="E -> K (in ARMD2 and STGD1; unknown pathological
FT significance; ATP-binding capacity and retinal stimulation
FT as in wild-type; dbSNP:rs1800548)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:9295268"
FT /id="VAR_008413"
FT VARIANT 498
FT /note="D -> E (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084866"
FT VARIANT 508
FT /note="R -> C (in STGD1; unknown pathological significance;
FT dbSNP:rs138157885)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084867"
FT VARIANT 511
FT /note="R -> C (in STGD1; unknown pathological significance;
FT dbSNP:rs752786160)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084868"
FT VARIANT 519
FT /note="C -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs1224959251)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084869"
FT VARIANT 523
FT /note="D -> E (in STGD1; dbSNP:rs62646868)"
FT /id="VAR_008414"
FT VARIANT 525
FT /note="F -> C (in STGD1)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012518"
FT VARIANT 533..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084870"
FT VARIANT 537
FT /note="R -> C (in STGD1; dbSNP:rs61748556)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012519"
FT VARIANT 541
FT /note="L -> P (in STGD1, FFM and CORD3; reduced ATP-binding
FT capacity; abolishes retinal-stimulated ATP hydrolysis; does
FT not affect solubility; does not affect intracellular
FT vesicle localization; significantly reduces substrate
FT binding; drastically reduces basal ATPase activity with
FT little or no substrate stimulation; dbSNP:rs61751392)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:29847635,
FT ECO:0000269|PubMed:9781034"
FT /id="VAR_008415"
FT VARIANT 548
FT /note="W -> R (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084871"
FT VARIANT 549
FT /note="A -> P (in STGD1; dbSNP:rs61748557)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012520"
FT VARIANT 550
FT /note="G -> R (in STGD1; dbSNP:rs61748558)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012521"
FT VARIANT 552
FT /note="V -> I (in RP19; unknown pathological significance;
FT dbSNP:rs145525174)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:19028736, ECO:0000269|PubMed:25346251"
FT /id="VAR_012522"
FT VARIANT 572..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084872"
FT VARIANT 572
FT /note="R -> P (in STGD1; dbSNP:rs61748559)"
FT /evidence="ECO:0000269|PubMed:18977788"
FT /id="VAR_008416"
FT VARIANT 572
FT /note="R -> Q (in STGD1; dbSNP:rs61748559)"
FT /evidence="ECO:0000269|PubMed:10746567,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:15192030"
FT /id="VAR_008417"
FT VARIANT 576
FT /note="D -> H (found in a patient with pattern dystrophy;
FT unknown pathological significance; dbSNP:rs374224955)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084873"
FT VARIANT 593
FT /note="P -> L (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084874"
FT VARIANT 602
FT /note="R -> Q (in STGD1; dbSNP:rs61749410)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012523"
FT VARIANT 602
FT /note="R -> W (in STGD1; dbSNP:rs61749409)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:24444108, ECO:0000269|PubMed:26780318"
FT /id="VAR_008418"
FT VARIANT 603
FT /note="Y -> C (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084875"
FT VARIANT 605..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084876"
FT VARIANT 607
FT /note="G -> R (in STGD1; dbSNP:rs61749412)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318"
FT /id="VAR_012524"
FT VARIANT 607
FT /note="G -> W (in STGD1; dbSNP:rs61749412)"
FT /id="VAR_012525"
FT VARIANT 608
FT /note="F -> I (in STGD1; moderately decreased protein
FT abundance; highly decreased ATPase activity; highly
FT decreased phospholipid translocase activity;
FT dbSNP:rs61752398)"
FT /evidence="ECO:0000269|PubMed:24097981"
FT /id="VAR_008419"
FT VARIANT 616
FT /note="E -> K (in STGD1; unknown pathological significance;
FT dbSNP:rs1557787473)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084877"
FT VARIANT 635
FT /note="Q -> K (in STGD1; dbSNP:rs61749414)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012526"
FT VARIANT 636
FT /note="Q -> H (in STGD1; dbSNP:rs61752400)"
FT /evidence="ECO:0000269|PubMed:9781034"
FT /id="VAR_012527"
FT VARIANT 636
FT /note="Q -> K (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084878"
FT VARIANT 639..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084879"
FT VARIANT 640
FT /note="P -> L (in STGD1; unknown pathological significance;
FT dbSNP:rs760790294)"
FT /evidence="ECO:0000269|PubMed:24457364"
FT /id="VAR_085013"
FT VARIANT 641
FT /note="C -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs61749416)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084880"
FT VARIANT 643
FT /note="V -> G (in CORD3; unknown pathological significance;
FT dbSNP:rs61754024)"
FT /evidence="ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:9295268"
FT /id="VAR_008420"
FT VARIANT 643
FT /note="V -> M (in STGD1; dbSNP:rs61749417)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012528"
FT VARIANT 645
FT /note="D -> N (in STGD1; dbSNP:rs61749418)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_008421"
FT VARIANT 653
FT /note="R -> C (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity; very
FT low substrate binding; dbSNP:rs61749420)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012529"
FT VARIANT 653
FT /note="R -> H (in STGD1; unknown pathological significance;
FT does not affect solubility; does not affect location in
FT cytoplasmic vesicle; does not affect both basal and N-Ret-
FT PE-stimulated ATPase activity; very low substrate binding;
FT dbSNP:rs141823837)"
FT /evidence="ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:33375396"
FT /id="VAR_084881"
FT VARIANT 661
FT /note="L -> R (in CORD3; unknown pathological significance;
FT severely decreases solubility; loss of cytoplasmic vesicle
FT localization;decreases basal ATPase activity below 50%;
FT loss of N-Ret-PE-induced stimulation in ATPase activity;
FT very low substrate binding)"
FT /evidence="ECO:0000269|PubMed:26780318,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_084882"
FT VARIANT 681..2273
FT /note="Missing (found in a patient with macular dystrophy;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084883"
FT VARIANT 686
FT /note="L -> S (in STGD1; severely decreases solubility;
FT loss of cytoplasmic vesicle localization;decreases basal
FT ATPase activity below 50%; loss of N-Ret-PE-induced
FT stimulation in ATPase activity; very low substrate binding;
FT dbSNP:rs61752402)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012530"
FT VARIANT 690
FT /note="G -> V (in STGD1; unknown pathological significance;
FT severely decreases solubility; loss of cytoplasmic vesicle
FT localization; very low substrate binding)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:33375396"
FT /id="VAR_084884"
FT VARIANT 700..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_084885"
FT VARIANT 716
FT /note="T -> M (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity;
FT decreases N-Ret-PE binding in the range of 40-70%;
FT dbSNP:rs61749426)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_012531"
FT VARIANT 752
FT /note="S -> I (in dbSNP:rs1801369)"
FT /id="VAR_014703"
FT VARIANT 754
FT /note="F -> S (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084886"
FT VARIANT 762
FT /note="A -> E (in ARMD2)"
FT /evidence="ECO:0000269|PubMed:19028736"
FT /id="VAR_067427"
FT VARIANT 764
FT /note="C -> Y (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity;
FT decreases N-Ret-PE binding in the range of 40-70%;
FT dbSNP:rs61749428)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012532"
FT VARIANT 765
FT /note="S -> N (in STGD1; severely decreases solubility;
FT loss of cytoplasmic vesicle localization;decreases basal
FT ATPase activity below 50%; loss of N-Ret-PE-induced
FT stimulation in ATPase activity; very low substrate binding;
FT dbSNP:rs61749429)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_012534"
FT VARIANT 765
FT /note="S -> R (in STGD1; severely decreases solubility;
FT loss of cytoplasmic vesicle localization;decreases basal
FT ATPase activity below 50%; loss of N-Ret-PE-induced
FT stimulation in ATPase activity; very low substrate binding;
FT dbSNP:rs61752404)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012533"
FT VARIANT 767
FT /note="V -> D (in STGD1; also found in a patient with
FT macular dystrophy; severely decreases solubility; loss of
FT cytoplasmic vesicle localization; decreases basal ATPase
FT activity below 50%; severely decreases N-Ret-PE-stimulated
FT ATPase activity; very low substrate binding;
FT dbSNP:rs61751395)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012535"
FT VARIANT 779..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_085014"
FT VARIANT 782..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084887"
FT VARIANT 797
FT /note="L -> P (in STGD1; severely decreases solubility;
FT loss of cytoplasmic vesicle localization;decreases basal
FT ATPase activity below 50%; loss of N-Ret-PE-induced
FT stimulation in ATPase activity; very low substrate binding;
FT dbSNP:rs61749432)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012536"
FT VARIANT 808..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084888"
FT VARIANT 816
FT /note="G -> V (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084889"
FT VARIANT 818
FT /note="G -> E (in ARMD2 and STGD1; reduced ATP-binding
FT capacity; moderately decreases solubility; loss of
FT cytoplasmic vesicle localization; decreases ATPase activity
FT between 50% and 80%; decreases modestly N-Ret-PE-stimulated
FT ATPase; very low substrate binding; dbSNP:rs61750202)"
FT /evidence="ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008422"
FT VARIANT 821
FT /note="W -> R (in STGD1; moderately decreases solubility;
FT loss of cytoplasmic vesicle localization; decreases ATPase
FT activity between 50% and 80%; decreases modestly N-Ret-PE-
FT stimulated ATPase; very low substrate binding;
FT dbSNP:rs61749433)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008423"
FT VARIANT 824
FT /note="I -> T (in STGD1; moderately decreases solubility;
FT loss of cytoplasmic vesicle localization; decreases ATPase
FT activity between 50% and 80%; decreases modestly N-Ret-PE-
FT stimulated ATPase; very low substrate binding)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012537"
FT VARIANT 840
FT /note="M -> R (in STGD1; unknown pathological significance;
FT severely decreases solubility; loss of cytoplasmic vesicle
FT localization;decreases basal ATPase activity below 50%;
FT loss of N-Ret-PE-induced stimulation in ATPase activity;
FT very low substrate binding)"
FT /evidence="ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_084890"
FT VARIANT 846
FT /note="D -> H (severely decreases solubility; loss of
FT cytoplasmic vesicle localization; decreases basal ATPase
FT activity below 50%; severely decreases N-Ret-PE-stimulated
FT ATPase activity; very low substrate binding;
FT dbSNP:rs61754027)"
FT /evidence="ECO:0000269|PubMed:33375396,
FT ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9295268"
FT /id="VAR_008493"
FT VARIANT 849
FT /note="V -> A (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity;
FT decreases N-Ret-PE binding in the range of 40-70%;
FT dbSNP:rs61749435)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012538"
FT VARIANT 851
FT /note="G -> D (in STGD1; highly reduced ATP-binding
FT capacity; severely decreases solubility; loss of
FT cytoplasmic vesicle localization;decreases basal ATPase
FT activity below 50%; loss of N-Ret-PE-induced stimulation in
FT ATPase activity; very low substrate binding;
FT dbSNP:rs61749436)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_008424"
FT VARIANT 854
FT /note="A -> T (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; decreases
FT ATPase activity between 50% and 80%; decreases modestly N-
FT Ret-PE-stimulated ATPase; decreases N-Ret-PE binding in the
FT range of 40-70%; dbSNP:rs61749437)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_012539"
FT VARIANT 863
FT /note="G -> A (in STGD1, FFM and CORD3; also found in a
FT patient with bull's eye maculopathy; mild alteration
FT probably leading to disease phenotype only in combination
FT with a more severe allele; frequent mutation in northern
FT Europe in linkage disequilibrium with the polymorphic
FT variant Q-943; reduced ATP-binding capacity and retinal-
FT stimulated ATP hydrolysis; significantly attenuates 11-cis-
FT retinal binding; decreases about 80% the N-retinylidene-
FT phosphatidylethanolamine transport activity; stimulates
FT modestely the retinal-stimulated ATPase activity; does not
FT affect ATP-independent N-retinylidene-
FT phosphatidylethanolamine binding. Does not affect ATP-
FT dependent release of N-retinylidene-
FT phosphatidylethanolamine; significantly reduces
FT phosphatidylethanolamine flippase activity;
FT dbSNP:rs76157638)"
FT /evidence="ECO:0000269|PubMed:10612508,
FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10746567,
FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:30120214, ECO:0000269|PubMed:9295268"
FT /id="VAR_008425"
FT VARIANT 863
FT /note="Missing (in STGD1 and CORD3; reduced ATP-binding
FT capacity and retinal-stimulated ATP hydrolysis)"
FT /evidence="ECO:0000269|PubMed:10958761,
FT ECO:0000269|PubMed:30120214"
FT /id="VAR_012540"
FT VARIANT 873
FT /note="F -> L (in STGD1; dbSNP:rs62642570)"
FT /id="VAR_012541"
FT VARIANT 876..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084891"
FT VARIANT 897
FT /note="T -> I (in STGD1; dbSNP:rs61749440)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788"
FT /id="VAR_012542"
FT VARIANT 901
FT /note="T -> A (in dbSNP:rs61754030)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_008426"
FT VARIANT 914
FT /note="H -> R"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012543"
FT VARIANT 931
FT /note="V -> M (in STGD1; dbSNP:rs58331765)"
FT /evidence="ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_008427"
FT VARIANT 935
FT /note="V -> A (in STGD1; dbSNP:rs61749444)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012544"
FT VARIANT 943
FT /note="R -> Q (in linkage disequilibrium with A-863 in the
FT European population and STGD1; found in a patient with
FT macular dystrophy; unknown pathological significance;
FT decreases 11-cis-Retinal binding affinity by 100-fold;
FT dbSNP:rs1801581)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:10746567, ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:11594993,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9295268,
FT ECO:0000269|Ref.5"
FT /id="VAR_008428"
FT VARIANT 943
FT /note="R -> W (in STGD1 and FFM; dbSNP:rs61749446)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11527935"
FT /id="VAR_012545"
FT VARIANT 954
FT /note="Y -> D (in STGD1; unknown pathological significance;
FT dbSNP:rs61749447)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084892"
FT VARIANT 957
FT /note="Q -> R (in STGD1; dbSNP:rs61749448)"
FT /id="VAR_008429"
FT VARIANT 959
FT /note="T -> I (in STGD1; moderately decreased protein
FT abundance; highly decreased ATPase activity; highly
FT decreased phospholipid translocase activity;
FT dbSNP:rs61752409)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:24097981"
FT /id="VAR_012546"
FT VARIANT 965
FT /note="N -> S (in STGD1; reduced retinal-stimulated ATP
FT hydrolysis; moderately decreased protein abundance; highly
FT decreased ATPase activity; highly decreased phospholipid
FT translocase activity; decreases about 60% the N-
FT retinylidene-phosphatidylethanolamine transfer activity;
FT stimulates modestly the retinal-stimulated ATPase activity;
FT does not affect ATP-independent N-retinylidene-
FT phosphatidylethanolamine binding; does not affect ATP-
FT dependent release of N-retinylidene-
FT phosphatidylethanolamine; significantly reduces
FT phosphatidylethanolamine flippase activity;
FT dbSNP:rs201471607)"
FT /evidence="ECO:0000269|PubMed:10746567,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:22735453,
FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24097981,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_008430"
FT VARIANT 965
FT /note="N -> Y (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084893"
FT VARIANT 970
FT /note="T -> P (in STGD1; unknown pathological significance;
FT dbSNP:rs1570377849)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084894"
FT VARIANT 971
FT /note="T -> N (in STGD1; highly reduced ATP-binding
FT capacity; abolishes retinal-stimulated ATP hydrolysis;
FT dbSNP:rs61749450)"
FT /id="VAR_012547"
FT VARIANT 972
FT /note="T -> N (in STGD1; unknown pathological significance;
FT dbSNP:rs61749451)"
FT /evidence="ECO:0000269|PubMed:11594993"
FT /id="VAR_012548"
FT VARIANT 973
FT /note="L -> S (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084895"
FT VARIANT 974
FT /note="S -> P (in STGD1; dbSNP:rs281865400)"
FT /evidence="ECO:0000269|PubMed:10206579"
FT /id="VAR_012549"
FT VARIANT 977
FT /note="T -> P (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084896"
FT VARIANT 978
FT /note="G -> C (in STGD1; dbSNP:rs61749452)"
FT /id="VAR_008431"
FT VARIANT 978
FT /note="G -> D (in STGD1; unknown pathological significance;
FT dbSNP:rs61749453)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_084897"
FT VARIANT 989
FT /note="V -> A (in STGD1; dbSNP:rs61749454)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012550"
FT VARIANT 991
FT /note="G -> R (in FFM and STGD1; dbSNP:rs61749455)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012551"
FT VARIANT 1014
FT /note="L -> R (in STGD1; dbSNP:rs61749456)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_012552"
FT VARIANT 1019
FT /note="T -> A (in STGD1; dbSNP:rs61749457)"
FT /id="VAR_012553"
FT VARIANT 1019
FT /note="T -> M (in STGD1; dbSNP:rs201855602)"
FT /evidence="ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034"
FT /id="VAR_012554"
FT VARIANT 1022
FT /note="E -> G (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084898"
FT VARIANT 1022
FT /note="E -> K (in STGD1; unknown pathological significance;
FT dbSNP:rs61749459)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012555"
FT VARIANT 1029..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084899"
FT VARIANT 1031
FT /note="K -> E (in STGD1; dbSNP:rs61750060)"
FT /id="VAR_012556"
FT VARIANT 1036
FT /note="E -> K (in STGD1; dbSNP:rs61750061)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_008432"
FT VARIANT 1038
FT /note="A -> V (in STGD1, FFM and CORD3; frequent mutation;
FT reduced ATP-binding and retinal-stimulated ATP hydrolysis;
FT decreases solubility at 70%; does not affect intracellular
FT vesicle localization; significantly reduces substrate
FT binding in the absence of ATP; reduces basal ATPase
FT activity; dbSNP:rs61751374)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10746567,
FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:9781034"
FT /id="VAR_008433"
FT VARIANT 1050
FT /note="G -> D (in STGD1; unknown pathological significance;
FT dbSNP:rs61750062)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084900"
FT VARIANT 1055
FT /note="R -> W (in STGD1; dbSNP:rs61752412)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_012557"
FT VARIANT 1063
FT /note="S -> P (in STGD1; dbSNP:rs61752413)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012558"
FT VARIANT 1071
FT /note="S -> L (in STGD1; reduced ATP-binding capacity;
FT dbSNP:rs61750065)"
FT /id="VAR_008434"
FT VARIANT 1072
FT /note="V -> A (in STGD1)"
FT /id="VAR_008435"
FT VARIANT 1074
FT /note="I -> L (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084901"
FT VARIANT 1078
FT /note="G -> E (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084902"
FT VARIANT 1087
FT /note="E -> D (in STGD1; dbSNP:rs61752416)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012559"
FT VARIANT 1087
FT /note="E -> K (in STGD1; dbSNP:rs61751398)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867"
FT /id="VAR_008436"
FT VARIANT 1091
FT /note="G -> E (in FFM and STGD1; decreases solubilized at
FT 70%; does not affect intracellular vesicle localization;
FT does not affect substrate binding; drastically reduces
FT basal ATPase activity with little or no substrate
FT stimulation; dbSNP:rs61752417)"
FT /evidence="ECO:0000269|PubMed:29847635,
FT ECO:0000269|PubMed:9781034"
FT /id="VAR_012560"
FT VARIANT 1094
FT /note="P -> T (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084903"
FT VARIANT 1097
FT /note="R -> C (in STGD1)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012561"
FT VARIANT 1097
FT /note="R -> S (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084904"
FT VARIANT 1098
FT /note="R -> C (in STGD1; unknown pathological significance;
FT dbSNP:rs756840095)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_084905"
FT VARIANT 1099..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084906"
FT VARIANT 1099
FT /note="S -> P (in STGD1; unknown pathological significance;
FT dbSNP:rs61750119)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084907"
FT VARIANT 1102
FT /note="D -> Y (in dbSNP:rs138641544)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084908"
FT VARIANT 1108
FT /note="R -> C (in STGD1 and FFM; reduced ATP-binding
FT capacity; dbSNP:rs61750120)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:9781034"
FT /id="VAR_012562"
FT VARIANT 1108
FT /note="R -> H (in STGD1; dbSNP:rs61750121)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:26780318"
FT /id="VAR_012563"
FT VARIANT 1108
FT /note="R -> L (in STGD1; dbSNP:rs61750121)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012564"
FT VARIANT 1112
FT /note="T -> N (in STGD1; dbSNP:rs61750122)"
FT /id="VAR_008437"
FT VARIANT 1122
FT /note="E -> K (in STGD1 and CORD3; dbSNP:rs61751399)"
FT /evidence="ECO:0000269|PubMed:10958761,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_008438"
FT VARIANT 1129
FT /note="R -> C (in STGD1; may predispose to develop retinal
FT toxicity after treatment with chloroquine and
FT hydroxychloroquine; dbSNP:rs779426136)"
FT /evidence="ECO:0000269|PubMed:11384574"
FT /id="VAR_012565"
FT VARIANT 1129
FT /note="R -> L (in ARMD2 and STGD1; also found in patients
FT with fundus flavimaculatus; reduced ATP-binding capacity;
FT dbSNP:rs1801269)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19028736,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:9295268"
FT /id="VAR_008439"
FT VARIANT 1130
FT /note="I -> T (in STGD1; unknown pathological significance;
FT dbSNP:rs1064793010)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084909"
FT VARIANT 1140
FT /note="C -> W (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084910"
FT VARIANT 1145
FT /note="L -> H (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084911"
FT VARIANT 1148
FT /note="K -> T"
FT /evidence="ECO:0000269|PubMed:11379881"
FT /id="VAR_012566"
FT VARIANT 1159
FT /note="L -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs1340749727)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084912"
FT VARIANT 1161
FT /note="R -> H (in STGD1; unknown pathological significance;
FT dbSNP:rs768278935)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084913"
FT VARIANT 1177..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084914"
FT VARIANT 1183
FT /note="G -> C (in CORD3; unknown pathological significance;
FT dbSNP:rs75267647)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084915"
FT VARIANT 1201
FT /note="L -> R (in STGD1; may predispose to develop retinal
FT toxicity after treatment with chloroquine and
FT hydroxychloroquine; dbSNP:rs61750126)"
FT /evidence="ECO:0000269|PubMed:11384574,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:23143460"
FT /id="VAR_008440"
FT VARIANT 1203
FT /note="G -> D (in STGD1)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084916"
FT VARIANT 1203
FT /note="G -> E (in CORD3; unknown pathological significance;
FT dbSNP:rs146786552)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084917"
FT VARIANT 1203
FT /note="G -> R (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084918"
FT VARIANT 1204
FT /note="D -> N (in STGD1; found in a patient with age-
FT related macular degeneration; unknown pathological
FT significance; dbSNP:rs61750127)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_008441"
FT VARIANT 1209
FT /note="M -> T (in dbSNP:rs76258939)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084919"
FT VARIANT 1250
FT /note="L -> P (in STGD1; dbSNP:rs61750128)"
FT /id="VAR_012567"
FT VARIANT 1253
FT /note="T -> M (in FFM; unknown pathological significance;
FT dbSNP:rs61752424)"
FT /evidence="ECO:0000269|PubMed:11385708"
FT /id="VAR_012568"
FT VARIANT 1300..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance; dbSNP:rs61752427)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_084920"
FT VARIANT 1300
FT /note="R -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs61750129)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:25346251"
FT /id="VAR_012569"
FT VARIANT 1314
FT /note="P -> T (in dbSNP:rs61754041)"
FT /id="VAR_008442"
FT VARIANT 1332..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084921"
FT VARIANT 1368
FT /note="R -> C (in CORD3; unknown pathological significance;
FT dbSNP:rs1183074086)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084922"
FT VARIANT 1371
FT /note="K -> N (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084923"
FT VARIANT 1380
FT /note="P -> L (in STGD1; also found in a patient with
FT chorioretinal atrophy; reduced ATP-binding capacity;
FT moderately decreases solubility; loss of cytoplasmic
FT vesicle localization; decreases ATPase activity between 50%
FT and 80%; decreases modestly N-Ret-PE-stimulated ATPase;
FT dbSNP:rs61750130)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008443"
FT VARIANT 1388
FT /note="L -> P (in STGD1; dbSNP:rs61750131)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012570"
FT VARIANT 1399
FT /note="E -> K (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity;
FT increases N-Ret-PE binding; dbSNP:rs62642573)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:33375396"
FT /id="VAR_012571"
FT VARIANT 1406
FT /note="H -> Y (in STGD1; dbSNP:rs61750133)"
FT /id="VAR_008444"
FT VARIANT 1408..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084924"
FT VARIANT 1408
FT /note="W -> L (in STGD1; does not affect secondary
FT structure; decreases structural flexibility; significantly
FT decreases all-trans-retinal binding; dbSNP:rs61750134)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:20404325"
FT /id="VAR_008445"
FT VARIANT 1408
FT /note="W -> R (in STGD1; reduced retinal-stimulated ATP
FT hydrolysis; dbSNP:rs61750135)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:24457364"
FT /id="VAR_008446"
FT VARIANT 1416
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085015"
FT VARIANT 1428
FT /note="T -> M (in dbSNP:rs1800549)"
FT /evidence="ECO:0000269|PubMed:26780318,
FT ECO:0000269|PubMed:9295268"
FT /id="VAR_008447"
FT VARIANT 1429
FT /note="V -> A (in STGD1; dbSNP:rs61752432)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_008448"
FT VARIANT 1430
FT /note="L -> P (in STGD1)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012572"
FT VARIANT 1433
FT /note="V -> I (in STGD1; dbSNP:rs56357060)"
FT /evidence="ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19265867"
FT /id="VAR_008449"
FT VARIANT 1439
FT /note="G -> D (in STGD1; dbSNP:rs61750140)"
FT /id="VAR_008450"
FT VARIANT 1440
FT /note="F -> S (in STGD1; dbSNP:rs61750141)"
FT /id="VAR_008451"
FT VARIANT 1440
FT /note="F -> V (in STGD1; dbSNP:rs61752433)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012573"
FT VARIANT 1442
FT /note="N -> K (in STGD1; unknown pathological significance;
FT dbSNP:rs762150575)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084925"
FT VARIANT 1443
FT /note="R -> H (in STGD1; loss of the majority of alpha-
FT helical secondary structure; does not bind all-trans-
FT retinal; does not affect conformational change;
FT dbSNP:rs61750142)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23419329"
FT /id="VAR_012574"
FT VARIANT 1453..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084926"
FT VARIANT 1461..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084927"
FT VARIANT 1479..2273
FT /note="Missing (in STGD1 and CORD3; unknown pathological
FT significance; dbSNP:rs61752434)"
FT /evidence="ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_084928"
FT VARIANT 1484
FT /note="P -> S (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084929"
FT VARIANT 1486
FT /note="P -> L (in STGD1; dbSNP:rs61750145)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_008452"
FT VARIANT 1488
FT /note="C -> F (in STGD1; dbSNP:rs61750147)"
FT /id="VAR_012575"
FT VARIANT 1488
FT /note="C -> R (in STGD1 and FFM; also found in a patient
FT with chorioretinal atrophy; reduced retinal-stimulated ATP
FT hydrolysis; does not affect secondary structure; oss of
FT structural flexibility; significantly decreases all-trans-
FT retinal binding; dbSNP:rs61750146)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23143460"
FT /id="VAR_008453"
FT VARIANT 1488
FT /note="C -> Y (in STGD1; dbSNP:rs61750147)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012576"
FT VARIANT 1490
FT /note="C -> Y (in STGD1 and CORD3; reduced retinal-
FT stimulated ATP hydrolysis; dbSNP:rs61751402)"
FT /evidence="ECO:0000269|PubMed:10958761,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23143460"
FT /id="VAR_008454"
FT VARIANT 1503
FT /note="P -> L (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084930"
FT VARIANT 1508
FT /note="G -> C (in FFM)"
FT /evidence="ECO:0000269|PubMed:9781034"
FT /id="VAR_012577"
FT VARIANT 1511
FT /note="P -> H (in STGD1; unknown pathological significance;
FT dbSNP:rs886046564)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084931"
FT VARIANT 1512
FT /note="P -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs61750150)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084932"
FT VARIANT 1513
FT /note="Q -> R (in STGD1; dbSNP:rs281865402)"
FT /id="VAR_012578"
FT VARIANT 1517
FT /note="R -> S (in ARMD2; dbSNP:rs1800550)"
FT /evidence="ECO:0000269|PubMed:9295268"
FT /id="VAR_008455"
FT VARIANT 1525
FT /note="L -> P (in STGD1; dbSNP:rs61750151)"
FT /id="VAR_012579"
FT VARIANT 1526
FT /note="T -> M (in STGD1; also found in a patient with
FT chorioretinal atrophy; reduced retinal-stimulated ATP
FT hydrolysis; dbSNP:rs61750152)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:26780318"
FT /id="VAR_008456"
FT VARIANT 1532
FT /note="D -> N (in STGD1; dbSNP:rs62642574)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_008457"
FT VARIANT 1537
FT /note="T -> M (in STGD1; moderately decreased protein
FT abundance; moderately decreased ATPase activity; moderately
FT decreased phospholipid translocase activity;
FT dbSNP:rs62642575)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:25346251"
FT /id="VAR_012580"
FT VARIANT 1551
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085016"
FT VARIANT 1556
FT /note="R -> T (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085017"
FT VARIANT 1557
FT /note="Y -> C (found in a patient with chorioretinal
FT atrophy; unknown pathological significance;
FT dbSNP:rs1401716074)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084933"
FT VARIANT 1562
FT /note="I -> T (in STGD1, FFM, ARMD2 and CORD3; found in a
FT patient with bull's eye maculopathy; unknown pathological
FT significance; dbSNP:rs1762111)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:9295268"
FT /id="VAR_008458"
FT VARIANT 1572
FT /note="T -> M (in dbSNP:rs185093512)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084934"
FT VARIANT 1578
FT /note="G -> R (in ARMD2; dbSNP:rs1800551)"
FT /evidence="ECO:0000269|PubMed:9295268"
FT /id="VAR_008459"
FT VARIANT 1591
FT /note="G -> R (in STGD1; also found in a patient with
FT macular dystrophy; unknown pathological significance;
FT dbSNP:rs113106943)"
FT /evidence="ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_084935"
FT VARIANT 1598
FT /note="A -> D (in CORD3 and STGD1; unknown pathological
FT significance; dbSNP:rs61750155)"
FT /evidence="ECO:0000269|PubMed:10958761,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012581"
FT VARIANT 1618..2273
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084936"
FT VARIANT 1623
FT /note="G -> V (unknown pathological significance;
FT dbSNP:rs1571257969)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084937"
FT VARIANT 1631
FT /note="L -> P (in STGD1; dbSNP:rs61750158)"
FT /id="VAR_008460"
FT VARIANT 1637
FT /note="A -> T (in dbSNP:rs61754056)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012582"
FT VARIANT 1640
FT /note="R -> Q (in STGD1, FFM and CORD3; dbSNP:rs61751403)"
FT /evidence="ECO:0000269|PubMed:10711710,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012583"
FT VARIANT 1640
FT /note="R -> W (in STGD1 and CORD3; dbSNP:rs61751404)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:9781034"
FT /id="VAR_008461"
FT VARIANT 1650..2273
FT /note="Missing (in CORD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084938"
FT VARIANT 1652..2273
FT /note="Missing (in STGD1 and FFM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_084939"
FT VARIANT 1652
FT /note="Y -> D (in STGD1; dbSNP:rs61750560)"
FT /evidence="ECO:0000269|PubMed:10206579"
FT /id="VAR_008462"
FT VARIANT 1681..1685
FT /note="Missing (in STGD1; highly reduced ATP-binding
FT capacity)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_012584"
FT VARIANT 1689
FT /note="S -> P (in STGD1; dbSNP:rs61753020)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012585"
FT VARIANT 1693
FT /note="V -> I (in STGD1; dbSNP:rs61750563)"
FT /id="VAR_012586"
FT VARIANT 1696
FT /note="S -> N (in STGD1; unknown pathological significance;
FT does not affect solubility; does not affect location in
FT cytoplasmic vesicle; does not affect both basal and N-Ret-
FT PE-stimulated ATPase activity; increases N-Ret-PE binding;
FT dbSNP:rs61750564)"
FT /evidence="ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008463"
FT VARIANT 1703
FT /note="Q -> E (in STGD1; unknown pathological significance;
FT does not affect solubility; does not affect location in
FT cytoplasmic vesicle;decreases basal ATPase activity below
FT 50%; loss of N-Ret-PE-induced stimulation in ATPase
FT activity; dbSNP:rs61750565)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_085018"
FT VARIANT 1703
FT /note="Q -> K (in STGD1; moderately decreases solubility;
FT loss of cytoplasmic vesicle localization;decreases basal
FT ATPase activity below 50%; loss of N-Ret-PE-induced
FT stimulation in ATPase activity)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_008464"
FT VARIANT 1705
FT /note="R -> L (in STGD1; moderately decreases solubility;
FT loss of cytoplasmic vesicle localization; decreases ATPase
FT activity between 50% and 80%; decreases modestly N-Ret-PE-
FT stimulated ATPase; dbSNP:rs61753021)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012587"
FT VARIANT 1705
FT /note="R -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs61753021)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085019"
FT VARIANT 1724..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084940"
FT VARIANT 1724
FT /note="W -> C (in ARMD2)"
FT /evidence="ECO:0000269|PubMed:19028736"
FT /id="VAR_067428"
FT VARIANT 1729
FT /note="L -> P (in STGD1; dbSNP:rs61750567)"
FT /evidence="ECO:0000269|PubMed:10206579"
FT /id="VAR_008465"
FT VARIANT 1733
FT /note="M -> T (in STGD1; dbSNP:rs765563320)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012588"
FT VARIANT 1736
FT /note="S -> P (in STGD1; dbSNP:rs61750568)"
FT /id="VAR_012589"
FT VARIANT 1748
FT /note="G -> R (in STGD1; dbSNP:rs61753025)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_012590"
FT VARIANT 1754
FT /note="Y -> D (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084941"
FT VARIANT 1761..1763
FT /note="Missing (in STGD1; highly reduced ATP-binding
FT capacity)"
FT /id="VAR_012591"
FT VARIANT 1762
FT /note="A -> D (in STGD1; unknown pathological significance;
FT dbSNP:rs121909206)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_084942"
FT VARIANT 1763
FT /note="L -> P (in STGD1; dbSNP:rs61753028)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:25346251"
FT /id="VAR_012592"
FT VARIANT 1773
FT /note="A -> E (found in a patient with chorioretinal
FT atrophy; unknown pathological significance; severely
FT decreases solubility; loss of cytoplasmic vesicle
FT localization; decreases basal ATPase activity below 50%;
FT loss of N-Ret-PE-induced stimulation in ATPase activity)"
FT /evidence="ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_084943"
FT VARIANT 1773
FT /note="A -> V (in STGD1; unknown pathological significance;
FT severely decreases solubility; loss of cytoplasmic vesicle
FT localization; decreases basal ATPase activity below 50%;
FT loss of N-Ret-PE-induced stimulation in ATPase activity;
FT dbSNP:rs760549861)"
FT /evidence="ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:33375396"
FT /id="VAR_084944"
FT VARIANT 1775
FT /note="I -> N (in STGD1; unknown pathological significance;
FT dbSNP:rs771742619)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085020"
FT VARIANT 1776
FT /note="P -> L (in STGD1; dbSNP:rs281865404)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012593"
FT VARIANT 1779..2273
FT /note="Missing (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_085021"
FT VARIANT 1779
FT /note="Y -> H (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085022"
FT VARIANT 1780
FT /note="P -> A (in STGD1; dbSNP:rs121909207)"
FT /evidence="ECO:0000269|PubMed:10746567"
FT /id="VAR_012594"
FT VARIANT 1794
FT /note="A -> D (in STGD1; also found in a patient with
FT bull's eye maculopathy; unknown pathological significance;
FT moderately decreases solubility; loss of cytoplasmic
FT vesicle localization; decreases basal ATPase activity below
FT 50%; severely decreases N-Ret-PE-stimulated ATPase
FT activity; dbSNP:rs61751406)"
FT /evidence="ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008466"
FT VARIANT 1794
FT /note="A -> P (in STGD1; unknown pathological significance;
FT loss of cytoplasmic vesicle localization; decreases ATPase
FT activity between 50% and 80%; decreases modestly N-Ret-PE-
FT stimulated ATPase; decreases solubility below 50%;
FT significantly reduces N-Ret-PE binding in the absence of
FT ATP; dbSNP:rs1571252997)"
FT /evidence="ECO:0000269|PubMed:29847635,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_085023"
FT VARIANT 1799
FT /note="N -> D (in STGD1; dbSNP:rs61750574)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_012595"
FT VARIANT 1805
FT /note="N -> D (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; decreases
FT ATPase activity between 50% and 80%; decreases modestly N-
FT Ret-PE-stimulated ATPase; dbSNP:rs61753029)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_012596"
FT VARIANT 1817
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:9054934,
FT ECO:0000269|PubMed:9503029"
FT /id="VAR_012597"
FT VARIANT 1820
FT /note="R -> P (in STGD1; dbSNP:rs62646875)"
FT /id="VAR_008467"
FT VARIANT 1838
FT /note="H -> D (in STGD1; unknown pathological significance;
FT moderately decreases solubility; loss of cytoplasmic
FT vesicle localization; decreases basal ATPase activity below
FT 50%; decreases modestly N-Ret-PE-stimulated ATPase;
FT dbSNP:rs62642562)"
FT /evidence="ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_085024"
FT VARIANT 1838
FT /note="H -> N (in STGD1; unknown pathological significance;
FT does not affect solubility; does not affect location in
FT cytoplasmic vesicle; decreases basal ATPase activity
FT between 50% and 80%; decreases modestly N-Ret-PE-stimulated
FT ATPase; dbSNP:rs62642562)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_084945"
FT VARIANT 1838
FT /note="H -> Y (in STGD1; moderately decreases solubility;
FT loss of cytoplasmic vesicle localization; decreases basal
FT ATPase activity below 50%; severely decreases N-Ret-PE-
FT stimulated ATPase activity; dbSNP:rs62642562)"
FT /evidence="ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008468"
FT VARIANT 1843
FT /note="R -> W (in STGD1; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; decreases
FT ATPase activity between 50% and 80%; decreases modestly N-
FT Ret-PE-stimulated ATPase; does not affect N-Ret-PE binding;
FT dbSNP:rs62642576)"
FT /evidence="ECO:0000269|PubMed:26780318,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008469"
FT VARIANT 1846
FT /note="I -> T (in STGD1; dbSNP:rs61750575)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_008494"
FT VARIANT 1868
FT /note="N -> I (in STGD1; slightly reduced retinal-
FT stimulated ATP hydrolysis; does not affect solubility; does
FT not affect location in cytoplasmic vesicle; does not affect
FT both basal and N-Ret-PE-stimulated ATPase activity; does
FT not affect N-Ret-PE binding; dbSNP:rs1801466)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11384574,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:11594993,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23419329,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:30120214,
FT ECO:0000269|PubMed:33375396"
FT /id="VAR_008470"
FT VARIANT 1882
FT /note="M -> I (in CORD3; unknown pathological significance;
FT dbSNP:rs752160946)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084946"
FT VARIANT 1884
FT /note="V -> E (in STGD1; dbSNP:rs62642578)"
FT /id="VAR_012598"
FT VARIANT 1885
FT /note="E -> K (in STGD1; dbSNP:rs62642563)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012599"
FT VARIANT 1886
FT /note="G -> E (in STGD1; highly reduced ATP-binding
FT capacity; dbSNP:rs62642579)"
FT /id="VAR_008471"
FT VARIANT 1890
FT /note="Missing (in STGD1; dbSNP:rs61750635)"
FT /id="VAR_008472"
FT VARIANT 1896
FT /note="V -> D (in STGD1; dbSNP:rs61750636)"
FT /id="VAR_012600"
FT VARIANT 1898
FT /note="R -> C (does not affect solubility; does not affect
FT location in cytoplasmic vesicle; does not affect both basal
FT and N-Ret-PE-stimulated ATPase activity;
FT dbSNP:rs201357151)"
FT /evidence="ECO:0000269|PubMed:33375396"
FT /id="VAR_085025"
FT VARIANT 1898
FT /note="R -> H (in STGD1 and ARMD2; does not affect
FT solubility; does not affect location in cytoplasmic
FT vesicle; does not affect both basal and N-Ret-PE-stimulated
FT ATPase activity; Increases N-Ret-PE binding;
FT dbSNP:rs1800552)"
FT /evidence="ECO:0000269|PubMed:10746567,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:33375396, ECO:0000269|PubMed:9295268"
FT /id="VAR_008473"
FT VARIANT 1921
FT /note="V -> G (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084947"
FT VARIANT 1921
FT /note="V -> M (in STGD1; dbSNP:rs61753032)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012601"
FT VARIANT 1940
FT /note="L -> P (in STGD1 and FFM; dbSNP:rs61753033)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_012602"
FT VARIANT 1942
FT /note="E -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs760353830)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085026"
FT VARIANT 1948
FT /note="P -> L (in dbSNP:rs56142141)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:11594993, ECO:0000269|PubMed:15192030"
FT /id="VAR_008474"
FT VARIANT 1948
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_085027"
FT VARIANT 1961
FT /note="G -> E (in STGD1, FFM and CORD3; also found patients
FT with cone dystrophy and with macular dystrophy; frequent
FT mutation; may be associated with ARMD2; inhibition of ATP
FT hydrolysis by retinal; dbSNP:rs1800553)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10880298,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11346402,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:9295268"
FT /id="VAR_008475"
FT VARIANT 1961
FT /note="G -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs142253670)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084948"
FT VARIANT 1970
FT /note="L -> F (in ARMD2, FFM and STGD1; also found in a
FT patient with cone dystrophy; dbSNP:rs28938473)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:9295268,
FT ECO:0000269|PubMed:9781034"
FT /id="VAR_008476"
FT VARIANT 1971
FT /note="L -> R (in FFM; highly reduced ATP-binding capacity;
FT abolishes basal and retinal-stimulated ATP hydrolysis;
FT dbSNP:rs61753034)"
FT /evidence="ECO:0000269|PubMed:9781034"
FT /id="VAR_012603"
FT VARIANT 1975
FT /note="G -> R (in STGD1; dbSNP:rs61753036)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012604"
FT VARIANT 1977
FT /note="G -> S (in STGD1 and ARMD2; highly reduced ATP-
FT binding capacity; inhibition of ATP hydrolysis by retinal;
FT dbSNP:rs61750639)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:19028736, ECO:0000269|PubMed:19265867,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034"
FT /id="VAR_008477"
FT VARIANT 2017
FT /note="C -> Y (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084949"
FT VARIANT 2023
FT /note="I -> T (in STGD1; unknown pathological significance;
FT dbSNP:rs150633517)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084950"
FT VARIANT 2027
FT /note="L -> F (in STGD1 and FFM; also found in a patient
FT with chorioretinal atrophy; highly reduced ATP-binding
FT capacity; dbSNP:rs61751408)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:25346251"
FT /id="VAR_008478"
FT VARIANT 2030..2273
FT /note="Missing (in STGD1 and CORD3; unknown pathological
FT significance; dbSNP:rs61751383)"
FT /evidence="ECO:0000269|PubMed:10634594,
FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:26780318"
FT /id="VAR_084951"
FT VARIANT 2030
FT /note="R -> Q (in STGD1 and FFM; dbSNP:rs61750641)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:25346251"
FT /id="VAR_008480"
FT VARIANT 2032
FT /note="H -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs1242866408)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084952"
FT VARIANT 2033
FT /note="L -> R (in STGD1; unknown pathological significance;
FT dbSNP:rs1553186896)"
FT /evidence="ECO:0000269|PubMed:25346251"
FT /id="VAR_084953"
FT VARIANT 2035
FT /note="L -> P (in STGD1; dbSNP:rs61750642)"
FT /evidence="ECO:0000269|PubMed:11527935"
FT /id="VAR_012605"
FT VARIANT 2038
FT /note="R -> W (in STGD1; highly reduced ATP-binding
FT capacity; dbSNP:rs61750643)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_008495"
FT VARIANT 2040..2273
FT /note="Missing (in STGD1; found in a patient with
FT chorioretinal atrophy; unknown pathological significance;
FT dbSNP:rs61753038)"
FT /evidence="ECO:0000269|PubMed:23143460,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_084954"
FT VARIANT 2040
FT /note="R -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs148460146)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084955"
FT VARIANT 2042
FT /note="V -> G (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084956"
FT VARIANT 2043
FT /note="P -> S (in CORD3; unknown pathological significance;
FT dbSNP:rs763230559)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084957"
FT VARIANT 2047
FT /note="I -> N (in ARMD2)"
FT /evidence="ECO:0000269|PubMed:19028736"
FT /id="VAR_067429"
FT VARIANT 2050
FT /note="V -> L (in STGD1 and CORD3; may act as a modifier of
FT macular dystrophy in patients who also have a TRP-172
FT mutation in PRPH2; dbSNP:rs41292677)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:20335603,
FT ECO:0000269|PubMed:25346251"
FT /id="VAR_008481"
FT VARIANT 2059
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012606"
FT VARIANT 2060
FT /note="L -> R (in CORD3; dbSNP:rs61753039)"
FT /evidence="ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:18977788"
FT /id="VAR_012607"
FT VARIANT 2064
FT /note="A -> T (in STGD1; unknown pathological significance;
FT dbSNP:rs61753040)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084958"
FT VARIANT 2071
FT /note="Y -> F (in STGD1)"
FT /id="VAR_012608"
FT VARIANT 2074
FT /note="G -> V (in STGD1; unknown pathological significance;
FT dbSNP:rs367839100)"
FT /evidence="ECO:0000269|PubMed:23419329"
FT /id="VAR_085028"
FT VARIANT 2077
FT /note="R -> G (in STGD1; dbSNP:rs61750645)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012609"
FT VARIANT 2077
FT /note="R -> W (in STGD1; highly reduced ATP-binding
FT capacity; decreases solubility at 50 %; loss of
FT intracellular vesicle localization; drastically reduced
FT basal activity with little or no substrate stimulation;
FT dbSNP:rs61750645)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:29847635"
FT /id="VAR_008482"
FT VARIANT 2078
FT /note="K -> E (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084959"
FT VARIANT 2096
FT /note="E -> K (in STGD1; inhibition of ATP hydrolysis by
FT retinal; dbSNP:rs61750646)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_008483"
FT VARIANT 2097
FT /note="P -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs1166357291)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084960"
FT VARIANT 2106
FT /note="R -> C (in STGD1 and FFM; reduced ATP-binding
FT capacity; dbSNP:rs61750648)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_008484"
FT VARIANT 2107
FT /note="R -> C (in STGD1; found in a patient with bull's eye
FT maculopathy; unknown pathological significance;
FT dbSNP:rs2297669)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_012610"
FT VARIANT 2107
FT /note="R -> H (in STGD1 and CORD3; may predispose to
FT develop retinal toxicity after treatment with chloroquine
FT and hydroxychloroquine; dbSNP:rs62642564)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030,
FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:24457364,
FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034"
FT /id="VAR_008485"
FT VARIANT 2128
FT /note="H -> R (in STGD1; dbSNP:rs61750651)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:23419329"
FT /id="VAR_008486"
FT VARIANT 2131
FT /note="E -> K (in STGD1; unknown pathological significance;
FT dbSNP:rs61750652)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_008487"
FT VARIANT 2137
FT /note="C -> Y (in ARMD2)"
FT /evidence="ECO:0000269|PubMed:19028736"
FT /id="VAR_067430"
FT VARIANT 2139
FT /note="R -> W (in STGD1; dbSNP:rs61750653)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030"
FT /id="VAR_008488"
FT VARIANT 2140
FT /note="L -> Q (in STGD1; unknown pathological significance;
FT dbSNP:rs774475956)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084961"
FT VARIANT 2146
FT /note="G -> D (in CORD3; dbSNP:rs61753044)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012611"
FT VARIANT 2149
FT /note="R -> L (in STGD1; dbSNP:rs61750655)"
FT /evidence="ECO:0000269|PubMed:15192030"
FT /id="VAR_012612"
FT VARIANT 2150
FT /note="C -> R (in STGD1; dbSNP:rs61750656)"
FT /evidence="ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:26780318"
FT /id="VAR_012613"
FT VARIANT 2150
FT /note="C -> Y (in STGD1 and CORD3; dbSNP:rs61751384)"
FT /evidence="ECO:0000269|PubMed:10206579,
FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:11527935,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788,
FT ECO:0000269|PubMed:23143460"
FT /id="VAR_008489"
FT VARIANT 2160
FT /note="K -> R (in STGD1; dbSNP:rs281865405)"
FT /evidence="ECO:0000269|PubMed:10634594"
FT /id="VAR_008490"
FT VARIANT 2177
FT /note="D -> N (in CORD3, ARMD2 and STGD1; unknown
FT pathological significance; increased retinal-stimulated ATP
FT hydrolysis; dbSNP:rs1800555)"
FT /evidence="ECO:0000269|PubMed:10880298,
FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11346402,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:25346251,
FT ECO:0000269|PubMed:9295268"
FT /id="VAR_008491"
FT VARIANT 2188
FT /note="F -> S (in STGD1; unknown pathological significance;
FT dbSNP:rs61750658)"
FT /evidence="ECO:0000269|PubMed:26780318"
FT /id="VAR_084962"
FT VARIANT 2216
FT /note="A -> V (in dbSNP:rs886044763)"
FT /evidence="ECO:0000269|PubMed:10958763"
FT /id="VAR_012614"
FT VARIANT 2221
FT /note="L -> P (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19265867"
FT /id="VAR_084963"
FT VARIANT 2229
FT /note="L -> P (in STGD1; dbSNP:rs61750659)"
FT /id="VAR_012615"
FT VARIANT 2237
FT /note="T -> P (in STGD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23143460"
FT /id="VAR_084964"
FT VARIANT 2241
FT /note="L -> V (in STGD1; dbSNP:rs61748521)"
FT /evidence="ECO:0000269|PubMed:10958763,
FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788"
FT /id="VAR_012616"
FT VARIANT 2255
FT /note="S -> I (benign variant; dbSNP:rs6666652)"
FT /evidence="ECO:0000269|PubMed:11379881,
FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11385708,
FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:26780318,
FT ECO:0000269|PubMed:9295268"
FT /id="VAR_009157"
FT VARIANT 2263
FT /note="R -> L (in STGD1; dbSNP:rs281865407)"
FT /id="VAR_012617"
FT MUTAGEN 940
FT /note="P->R: Decreases 11-cis-Retinal binding affinity by
FT 50%."
FT /evidence="ECO:0000269|PubMed:23144455"
FT MUTAGEN 966
FT /note="G->D: Abolishes basal and retinal-stimulated ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:11017087"
FT MUTAGEN 969
FT /note="K->M: Abolishes basal and retinal-stimulated ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:11017087"
FT MUTAGEN 969
FT /note="K->M: Inhibits ATPase activity; when associated with
FT M-1978. Decreases translocase activity; when associated
FT with M-1978. Does not affect protein subcellular
FT localization in endoplasmic reticulum; when associated with
FT M-1978. Loss of ATP-dependent all-trans-retinal transport;
FT when associated with M-1978. Loss in N-retinylidene-PE
FT transfer activity. Inhibits ATPase activity with increasing
FT retinal concentration. Does not affect N-retinylidene-PE
FT binding. Impairs ATP-dependent release of N-retinylidene-
FT PE. Significantly reduces PE flippase activity."
FT /evidence="ECO:0000269|PubMed:22735453,
FT ECO:0000269|PubMed:24097981"
FT MUTAGEN 1087
FT /note="E->Q: Does not affect protein folding; when
FT associated with Q-2096. Loss of ATPase activity; when
FT associated with Q-2096."
FT /evidence="ECO:0000269|PubMed:33605212"
FT MUTAGEN 1357
FT /note="A->T: Decreases solubility at 50%. Loss of
FT intracellular vesicle localization. Does not affect
FT substrate binding. Reduces basal ATPase activity."
FT /evidence="ECO:0000269|PubMed:29847635"
FT MUTAGEN 1502
FT /note="C->R: Moderately decreased protein abundance.
FT Moderately decreased ATPase activity. Moderately decreased
FT phospholipid translocase activity."
FT /evidence="ECO:0000269|PubMed:24097981"
FT MUTAGEN 1838
FT /note="H->R: Severely decreases solubility. Loss of
FT cytoplasmic vesicle localization. Decreases basal ATPase
FT activity below 50%. Loss of N-Ret-PE-induced stimulation in
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:33375396"
FT MUTAGEN 1975
FT /note="G->D: Inhibition of retinal-stimulated ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:11017087"
FT MUTAGEN 1978
FT /note="K->M: Inhibits ATPase activity; when associated with
FT M-969. Decreases translocase activity; when associated with
FT M-969. Does not affect protein subcellular localization in
FT endoplasmic reticulum; when associated with M-969. Loss of
FT ATP-dependent all-trans-retinal transport; when associated
FT with M-1978. Loss in N-retinylidene-PE transfer activity.
FT Inhibits ATPase activity with increasing retinal
FT concentration. Does not affect ATP-independent N-
FT retinylidene-PE binding. Does not affect ATP-dependent of
FT N-retinylidene-PE release. Significantly reduces PE
FT flippase activity. Inhibition of retinal-stimulated ATP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:11017087,
FT ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24097981"
FT MUTAGEN 2096
FT /note="E->Q: Does not affect protein folding; when
FT associated with Q-1087. Loss of ATPase activity; when
FT associated with Q-1087."
FT /evidence="ECO:0000269|PubMed:33605212"
FT MUTAGEN 2107
FT /note="R->P: Highly decreased protein abundance. Highly
FT decreased ATPase activity. Highly decreased phospholipid
FT translocase activity."
FT /evidence="ECO:0000269|PubMed:24097981"
FT MUTAGEN 2180
FT /note="P->L: Does not affect protein abundance. Does not
FT affect ATPase activity. Moderately decreased phospholipid
FT translocase activity."
FT /evidence="ECO:0000269|PubMed:24097981"
FT CONFLICT 722
FT /note="G -> V (in Ref. 2; AAC23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="V -> C (in Ref. 1; AAC51144)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="G -> S (in Ref. 1; AAC51144 and 3; CAA75729)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="C -> S (in Ref. 2; AAC23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116
FT /note="S -> P (in Ref. 1; AAC51144)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125..1126
FT /note="LL -> HQ (in Ref. 1; AAC51144)"
FT /evidence="ECO:0000305"
FT CONFLICT 1395
FT /note="P -> L (in Ref. 1; AAC51144 and 3; CAA75729)"
FT /evidence="ECO:0000305"
FT CONFLICT 1465
FT /note="S -> C (in Ref. 4; AAC05632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1518
FT /note="S -> T (in Ref. 4; AAC05632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1733
FT /note="M -> V (in Ref. 2; AAC23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 1989
FT /note="T -> N (in Ref. 2; AAC23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 2119
FT /note="E -> K (in Ref. 1; AAC51144)"
FT /evidence="ECO:0000305"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 24..44
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:7E7I"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:7E7I"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:7E7I"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:7E7I"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7E7I"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:7E7Q"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 405..414
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 462..467
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:7E7O"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 499..517
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 531..536
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 537..543
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 565..572
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 608..624
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:7E7I"
FT HELIX 647..679
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 683..689
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 695..721
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 730..754
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 758..781
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 790..794
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 798..814
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 821..825
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:7LKZ"
FT HELIX 837..860
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 872..876
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 923..925
FT /evidence="ECO:0007829|PDB:7E7Q"
FT STRAND 927..934
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 939..941
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 945..949
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 956..960
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 965..968
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 969..977
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 986..989
FT /evidence="ECO:0007829|PDB:7LKP"
FT TURN 993..995
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1001..1004
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1005..1008
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 1016..1018
FT /evidence="ECO:0007829|PDB:7LKZ"
FT HELIX 1020..1030
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1035..1043
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1049..1054
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1055..1058
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1059..1061
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1064..1073
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1074..1076
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1077..1079
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1081..1084
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1086..1091
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 1094..1106
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1121..1123
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1134..1137
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1144..1148
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1156..1158
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1159..1161
FT /evidence="ECO:0007829|PDB:7E7I"
FT STRAND 1201..1203
FT /evidence="ECO:0007829|PDB:7LKZ"
FT HELIX 1205..1215
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1223..1225
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1228..1230
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1231..1233
FT /evidence="ECO:0007829|PDB:7E7Q"
FT STRAND 1236..1238
FT /evidence="ECO:0007829|PDB:7E7O"
FT HELIX 1240..1254
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1255..1258
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 1259..1262
FT /evidence="ECO:0007829|PDB:7E7Q"
FT STRAND 1263..1265
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1269..1276
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1349..1368
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1371..1374
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1375..1378
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1379..1393
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1407..1409
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1410..1412
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1414..1419
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1425..1435
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1436..1438
FT /evidence="ECO:0007829|PDB:7E7O"
FT STRAND 1440..1442
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1451..1453
FT /evidence="ECO:0007829|PDB:7E7O"
FT HELIX 1468..1476
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1481..1483
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1493..1495
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1504..1507
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1513..1515
FT /evidence="ECO:0007829|PDB:7LKZ"
FT TURN 1517..1519
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1520..1524
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 1530..1545
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1548..1551
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1558..1562
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1570..1573
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1574..1586
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1593..1599
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1602..1609
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1612..1619
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1627..1641
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1645..1647
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1649..1651
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1653..1658
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1665..1690
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1692..1706
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1709..1716
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1720..1747
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1748..1750
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1752..1755
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1757..1759
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1760..1778
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1781..1784
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1788..1813
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1817..1820
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1821..1829
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 1830..1832
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1833..1835
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1837..1860
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1870..1875
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1876..1896
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1919..1929
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1931..1933
FT /evidence="ECO:0007829|PDB:7E7O"
FT STRAND 1937..1946
FT /evidence="ECO:0007829|PDB:7LKP"
FT TURN 1948..1950
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1952..1958
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 1967..1969
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 1974..1976
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 1978..1985
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1986..1988
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 1993..1998
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 2003..2005
FT /evidence="ECO:0007829|PDB:7LKP"
FT TURN 2009..2011
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2013..2020
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2025..2028
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 2034..2040
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2044..2046
FT /evidence="ECO:0007829|PDB:7LKP"
FT TURN 2050..2053
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2055..2058
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 2062..2065
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 2068..2070
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2073..2084
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 2085..2087
FT /evidence="ECO:0007829|PDB:7LKZ"
FT STRAND 2090..2097
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2103..2119
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2122..2126
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2131..2133
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 2134..2136
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2138..2152
FT /evidence="ECO:0007829|PDB:7LKP"
FT HELIX 2154..2160
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2166..2169
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2179..2192
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2197..2202
FT /evidence="ECO:0007829|PDB:7LKP"
FT STRAND 2205..2209
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2217..2224
FT /evidence="ECO:0007829|PDB:7M1Q"
FT TURN 2225..2228
FT /evidence="ECO:0007829|PDB:7M1Q"
FT STRAND 2235..2237
FT /evidence="ECO:0007829|PDB:7M1Q"
FT HELIX 2241..2252
FT /evidence="ECO:0007829|PDB:7LKP"
SQ SEQUENCE 2273 AA; 255944 MW; 6E7012D3041CD043 CRC64;
MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS HHECHFPNKA
MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS ILARVYRDFQ ELLMNAPESQ
HLGRIWTELH ILSQFMDTLR THPERIAGRG IRIRDILKDE ETLTLFLIKN IGLSDSVVYL
LINSQVRPEQ FAHGVPDLAL KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI
EDTLYANVDF FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT
RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG IDSTRKDPIY
SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY TPDSPAARRI LKNANSTFEE
LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM IRDTLGNPTV KDFLNRQLGE EGITAEAILN
FLYKGPRESQ ADDMANFDWR DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS
LLEENMFWAG VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED
FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV
LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM
HGRILHYSDP FILFLFLLAF STATIMLCFL LSTFFSKASL AAACSGVIYF TLYLPHILCF
AWQDRMTAEL KKAVSLLSPV AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM
QMMLLDAAVY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL
TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN ITFYENQITA
FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA VRQSLGMCPQ HNILFHHLTV
AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA
KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC
SGTPLFLKNC FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV
LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL EETLADLGLS
SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR HPCLGPREKA GQTPQDSNVC
SPGAPAAHPE GQPPPEPECP GPQLNTGTQL VLQHVQALLV KRFQHTIRSH KDFLAQIVLP
ATFVFLALML SIVIPPFGEY PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF
GNRCLKEGWL PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP
ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF WVNEQRYGGI
SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK EIPDFLKHLE TEDNIKVWFN
NKGWHALVSF LNVAHNAILR ASLPKDRSPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA
VVAICVIFSM SFVPASFVLY LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG
LVVGIFIGFQ KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL
FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL SQAVTDVYAR
FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF FLSQWIAEPT KEPIVDEDDD
VAEERQRIIT GGNKTDILRL HELTKIYPGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT
TFKMLTGDTT VTSGDATVAG KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR
GVPAEEIEKV ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG
MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC MGTIQHLKSK
FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFQ
LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK QQTESHDLPL HPRAAGASRQ AQD
