TULP1_HUMAN
ID TULP1_HUMAN Reviewed; 542 AA.
AC O00294; O43536; Q5TGM5; Q8N571;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Tubby-related protein 1;
DE AltName: Full=Tubby-like protein 1;
GN Name=TULP1; Synonyms=TUBL1;
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] (ISOFORM 1), AND VARIANTS ARG-67 AND ASN-261.
RC TISSUE=Retina;
RX PubMed=9096357; DOI=10.1073/pnas.94.7.3128;
RA North M.A., Naggert J.K., Yan Y., Noben-Trauth K., Nishina P.M.;
RT "Molecular characterization of TUB, TULP1, and TULP2, members of the novel
RT tubby gene family and their possible relation to ocular diseases.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3128-3133(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-67 AND ASN-261.
RX PubMed=9462751; DOI=10.1038/ng0298-177;
RA Banerjee P., Kleyn P.W., Knowles J.A., Lewis C.A., Ross B.M., Parano E.,
RA Kovats S.G., Lee J.J., Penchaszadeh G.K., Ott J., Jacobson S.G.,
RA Gilliam T.C.;
RT "TULP1 mutation in two extended Dominican kindreds with autosomal recessive
RT retinitis pigmentosa.";
RL Nat. Genet. 18:177-179(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASN-261.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL PHOSPHOLIPIDS, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH F-ACTIN.
RX PubMed=16303976; DOI=10.1167/iovs.05-0693;
RA Xi Q., Pauer G.J.T., Marmorstein A.D., Crabb J.W., Hagstrom S.A.;
RT "Tubby-like protein 1 (TULP1) interacts with F-actin in photoreceptor
RT cells.";
RL Invest. Ophthalmol. Vis. Sci. 46:4754-4761(2005).
RN [6]
RP FUNCTION, AND CHARACTERIZATION OF VARIANTS RP14 PRO-420; LYS-459; ARG-489
RP AND LEU-491.
RX PubMed=19837063; DOI=10.1016/j.yexcr.2009.10.008;
RA Caberoy N.B., Maiguel D., Kim Y., Li W.;
RT "Identification of tubby and tubby-like protein 1 as eat-me signals by
RT phage display.";
RL Exp. Cell Res. 316:245-257(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 291-536 IN COMPLEX WITH IP3.
RG Structural genomics consortium (SGC);
RT "Structure of human TULP1 in complex with IP3.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [8]
RP VARIANTS RP14 120-GLU--ASP-127 DEL; ARG-489 AND THR-496.
RX PubMed=9660588; DOI=10.1016/s0140-6736(05)79384-3;
RA Gu S., Lennon A., Li Y., Lorenz B., Fossarello M., North M., Gal A.,
RA Wright A.;
RT "Tubby-like protein-1 mutations in autosomal recessive retinitis
RT pigmentosa.";
RL Lancet 351:1103-1104(1998).
RN [9]
RP VARIANTS RP14 PRO-420; LYS-459 AND LEU-491.
RX PubMed=9462750; DOI=10.1038/ng0298-174;
RA Hagstrom S.A., North M.A., Nishina P.M., Berson E.L., Dryja T.P.;
RT "Recessive mutations in the gene encoding the tubby-like protein TULP1 in
RT patients with retinitis pigmentosa.";
RL Nat. Genet. 18:174-176(1998).
RN [10]
RP VARIANTS LCA15 TRP-368 AND TRP-400.
RX PubMed=15024725; DOI=10.1002/humu.20010;
RA Hanein S., Perrault I., Gerber S., Tanguy G., Barbet F., Ducroq D.,
RA Calvas P., Dollfus H., Hamel C., Lopponen T., Munier F., Santos L.,
RA Shalev S., Zafeiriou D., Dufier J.-L., Munnich A., Rozet J.-M., Kaplan J.;
RT "Leber congenital amaurosis: comprehensive survey of the genetic
RT heterogeneity, refinement of the clinical definition, and genotype-
RT phenotype correlations as a strategy for molecular diagnosis.";
RL Hum. Mutat. 23:306-317(2004).
RN [11]
RP VARIANT RP14 SER-382.
RX PubMed=15557452; DOI=10.1167/iovs.04-0544;
RA Kondo H., Qin M., Mizota A., Kondo M., Hayashi H., Hayashi K., Oshima K.,
RA Tahira T., Hayashi K.;
RT "A homozygosity-based search for mutations in patients with autosomal
RT recessive retinitis pigmentosa, using microsatellite markers.";
RL Invest. Ophthalmol. Vis. Sci. 45:4433-4439(2004).
RN [12]
RP VARIANT RP14 TRP-482.
RX PubMed=17620573; DOI=10.1001/archopht.125.7.932;
RA den Hollander A.I., van Lith-Verhoeven J.J., Arends M.L., Strom T.M.,
RA Cremers F.P., Hoyng C.B.;
RT "Novel compound heterozygous TULP1 mutations in a family with severe early-
RT onset retinitis pigmentosa.";
RL Arch. Ophthalmol. 125:932-935(2007).
RN [13]
RP VARIANT LCA15 PHE-ALA-529 INS, AND VARIANTS THR-259; ASN-261 AND THR-496.
RX PubMed=17962469; DOI=10.1167/iovs.06-1013;
RA Mataftsi A., Schorderet D.F., Chachoua L., Boussalah M., Nouri M.T.,
RA Barthelmes D., Borruat F.X., Munier F.L.;
RT "Novel TULP1 mutation causing Leber congenital amaurosis or early onset
RT retinal degeneration.";
RL Invest. Ophthalmol. Vis. Sci. 48:5160-5167(2007).
CC -!- FUNCTION: Required for normal development of photoreceptor synapses.
CC Required for normal photoreceptor function and for long-term survival
CC of photoreceptor cells. Interacts with cytoskeleton proteins and may
CC play a role in protein transport in photoreceptor cells (By
CC similarity). Binds lipids, especially phosphatidylinositol 3-phosphate,
CC phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate,
CC phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-
CC bisphosphate, phosphatidylinositol 3,4,5-bisphosphate,
CC phosphatidylserine and phosphatidic acid (in vitro). Contribute to
CC stimulation of phagocytosis of apoptotic retinal pigment epithelium
CC (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:16303976,
CC ECO:0000269|PubMed:19837063}.
CC -!- SUBUNIT: Homodimer (Probable). May interact with ABCF1, PSIP1, ZEB1 and
CC HMGB2 (Potential). Interacts with DNM1 (By similarity). Interacts with
CC F-actin. Interacts with TUB (By similarity). Interacts with TYRO3 (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC O00294; P16333: NCK1; NbExp=2; IntAct=EBI-1756778, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16303976}. Cell
CC membrane {ECO:0000269|PubMed:16303976}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16303976}; Cytoplasmic side
CC {ECO:0000269|PubMed:16303976}. Secreted {ECO:0000250}. Synapse
CC {ECO:0000250}. Note=Detected at synapses between photoreceptor cells
CC and second-order neurons. Does not have a cleavable signal peptide and
CC is secreted by an alternative pathway (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00294-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00294-2; Sequence=VSP_023031;
CC -!- TISSUE SPECIFICITY: Retina-specific.
CC -!- DISEASE: Retinitis pigmentosa 14 (RP14) [MIM:600132]: 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. {ECO:0000269|PubMed:15557452,
CC ECO:0000269|PubMed:17620573, ECO:0000269|PubMed:19837063,
CC ECO:0000269|PubMed:9462750, ECO:0000269|PubMed:9660588}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Leber congenital amaurosis 15 (LCA15) [MIM:613843]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:15024725,
CC ECO:0000269|PubMed:17962469}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the TULP1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/tulpmut.htm";
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DR EMBL; U82468; AAB53700.1; -; mRNA.
DR EMBL; AF034923; AAB97966.1; -; Genomic_DNA.
DR EMBL; AF034919; AAB97966.1; JOINED; Genomic_DNA.
DR EMBL; AF034920; AAB97966.1; JOINED; Genomic_DNA.
DR EMBL; AF034921; AAB97966.1; JOINED; Genomic_DNA.
DR EMBL; AF034922; AAB97966.1; JOINED; Genomic_DNA.
DR EMBL; AL033519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032714; AAH32714.1; -; mRNA.
DR EMBL; BC065261; AAH65261.1; -; mRNA.
DR CCDS; CCDS4807.1; -. [O00294-1]
DR CCDS; CCDS75436.1; -. [O00294-2]
DR RefSeq; NP_001276324.1; NM_001289395.1. [O00294-2]
DR RefSeq; NP_003313.3; NM_003322.5. [O00294-1]
DR PDB; 2FIM; X-ray; 1.90 A; A/B=290-542.
DR PDB; 3C5N; X-ray; 1.80 A; A/B=291-536.
DR PDBsum; 2FIM; -.
DR PDBsum; 3C5N; -.
DR AlphaFoldDB; O00294; -.
DR SMR; O00294; -.
DR BioGRID; 113138; 3.
DR IntAct; O00294; 5.
DR STRING; 9606.ENSP00000229771; -.
DR iPTMnet; O00294; -.
DR PhosphoSitePlus; O00294; -.
DR BioMuta; TULP1; -.
DR MassIVE; O00294; -.
DR PaxDb; O00294; -.
DR PeptideAtlas; O00294; -.
DR PRIDE; O00294; -.
DR ProteomicsDB; 47825; -. [O00294-1]
DR ProteomicsDB; 47826; -. [O00294-2]
DR Antibodypedia; 45745; 99 antibodies from 21 providers.
DR DNASU; 7287; -.
DR Ensembl; ENST00000229771.11; ENSP00000229771.6; ENSG00000112041.13. [O00294-1]
DR Ensembl; ENST00000322263.8; ENSP00000319414.4; ENSG00000112041.13. [O00294-2]
DR GeneID; 7287; -.
DR KEGG; hsa:7287; -.
DR MANE-Select; ENST00000229771.11; ENSP00000229771.6; NM_003322.6; NP_003313.3.
DR UCSC; uc003okv.6; human. [O00294-1]
DR CTD; 7287; -.
DR DisGeNET; 7287; -.
DR GeneCards; TULP1; -.
DR GeneReviews; TULP1; -.
DR HGNC; HGNC:12423; TULP1.
DR HPA; ENSG00000112041; Tissue enriched (retina).
DR MalaCards; TULP1; -.
DR MIM; 600132; phenotype.
DR MIM; 602280; gene.
DR MIM; 613843; phenotype.
DR neXtProt; NX_O00294; -.
DR OpenTargets; ENSG00000112041; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA37085; -.
DR VEuPathDB; HostDB:ENSG00000112041; -.
DR eggNOG; KOG2502; Eukaryota.
DR GeneTree; ENSGT00940000158771; -.
DR HOGENOM; CLU_028236_5_1_1; -.
DR InParanoid; O00294; -.
DR OMA; MRWQNKN; -.
DR PhylomeDB; O00294; -.
DR TreeFam; TF314076; -.
DR PathwayCommons; O00294; -.
DR SignaLink; O00294; -.
DR BioGRID-ORCS; 7287; 40 hits in 1087 CRISPR screens.
DR EvolutionaryTrace; O00294; -.
DR GeneWiki; TULP1; -.
DR GenomeRNAi; 7287; -.
DR Pharos; O00294; Tbio.
DR PRO; PR:O00294; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00294; protein.
DR Bgee; ENSG00000112041; Expressed in pigmented layer of retina and 95 other tissues.
DR ExpressionAtlas; O00294; baseline and differential.
DR Genevisible; O00294; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISS:UniProtKB.
DR GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 3.20.90.10; -; 1.
DR InterPro; IPR025659; Tubby-like_C.
DR InterPro; IPR000007; Tubby_C.
DR InterPro; IPR018066; Tubby_C_CS.
DR Pfam; PF01167; Tub; 1.
DR PRINTS; PR01573; SUPERTUBBY.
DR SUPFAM; SSF54518; SSF54518; 1.
DR PROSITE; PS01200; TUB_1; 1.
DR PROSITE; PS01201; TUB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Disease variant; Leber congenital amaurosis; Membrane; Phagocytosis;
KW Reference proteome; Retinitis pigmentosa; Secreted; Sensory transduction;
KW Synapse; Vision.
FT CHAIN 1..542
FT /note="Tubby-related protein 1"
FT /id="PRO_0000186466"
FT REGION 1..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 64..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023031"
FT VARIANT 67
FT /note="T -> R (in dbSNP:rs7764472)"
FT /evidence="ECO:0000269|PubMed:9096357,
FT ECO:0000269|PubMed:9462751"
FT /id="VAR_008274"
FT VARIANT 120..127
FT /note="Missing (in RP14)"
FT /evidence="ECO:0000269|PubMed:9660588"
FT /id="VAR_013310"
FT VARIANT 245
FT /note="A -> V (in RP14; dbSNP:rs62636707)"
FT /id="VAR_008275"
FT VARIANT 259
FT /note="I -> T (in dbSNP:rs2064317)"
FT /evidence="ECO:0000269|PubMed:17962469"
FT /id="VAR_008276"
FT VARIANT 261
FT /note="K -> N (in dbSNP:rs2064318)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17962469, ECO:0000269|PubMed:9096357,
FT ECO:0000269|PubMed:9462751"
FT /id="VAR_034575"
FT VARIANT 261
FT /note="K -> T (in RP14)"
FT /id="VAR_008277"
FT VARIANT 368
FT /note="G -> W (in LCA15; dbSNP:rs387906837)"
FT /evidence="ECO:0000269|PubMed:15024725"
FT /id="VAR_065500"
FT VARIANT 378
FT /note="R -> H (in RP14; dbSNP:rs148749577)"
FT /id="VAR_008278"
FT VARIANT 382
FT /note="F -> S (in RP14; dbSNP:rs121909076)"
FT /evidence="ECO:0000269|PubMed:15557452"
FT /id="VAR_037584"
FT VARIANT 400
FT /note="R -> W (in LCA15; dbSNP:rs387906836)"
FT /evidence="ECO:0000269|PubMed:15024725"
FT /id="VAR_065501"
FT VARIANT 420
FT /note="R -> P (in RP14; no effect on RPE phagocytosis;
FT dbSNP:rs121909073)"
FT /evidence="ECO:0000269|PubMed:19837063,
FT ECO:0000269|PubMed:9462750"
FT /id="VAR_007941"
FT VARIANT 454
FT /note="T -> M (in RP14; dbSNP:rs138200747)"
FT /id="VAR_008279"
FT VARIANT 459
FT /note="I -> K (in RP14; no effect on RPE phagocytosis;
FT dbSNP:rs121909075)"
FT /evidence="ECO:0000269|PubMed:19837063,
FT ECO:0000269|PubMed:9462750"
FT /id="VAR_007942"
FT VARIANT 482
FT /note="R -> W (in RP14; dbSNP:rs121909077)"
FT /evidence="ECO:0000269|PubMed:17620573"
FT /id="VAR_065502"
FT VARIANT 489
FT /note="K -> R (in RP14; abolishes RPE phagocytosis;
FT dbSNP:rs62636511)"
FT /evidence="ECO:0000269|PubMed:19837063,
FT ECO:0000269|PubMed:9660588"
FT /id="VAR_008280"
FT VARIANT 491
FT /note="F -> L (in RP14; abolishes RPE phagocytosis;
FT dbSNP:rs121909074)"
FT /evidence="ECO:0000269|PubMed:19837063,
FT ECO:0000269|PubMed:9462750"
FT /id="VAR_007943"
FT VARIANT 496
FT /note="A -> T (in RP14; unknown pathological significance;
FT dbSNP:rs141980901)"
FT /evidence="ECO:0000269|PubMed:17962469,
FT ECO:0000269|PubMed:9660588"
FT /id="VAR_008281"
FT VARIANT 529
FT /note="A -> AFA (in LCA15)"
FT /evidence="ECO:0000269|PubMed:17962469"
FT /id="VAR_065503"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2FIM"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:3C5N"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:3C5N"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3C5N"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 503..510
FT /evidence="ECO:0007829|PDB:3C5N"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:3C5N"
FT HELIX 524..533
FT /evidence="ECO:0007829|PDB:3C5N"
SQ SEQUENCE 542 AA; 60609 MW; 65320103E2674B60 CRC64;
MPLRDETLRE VWASDSGHEE ESLSPEAPRR PKQRPAPAQR LRKKRTEAPE SPCPTGSKPR
KPGAGRTGRP REEPSPDPAQ ARAPQTVYAR FLRDPEAKKR DPRETFLVAR APDAEDEEEE
EEEDEEDEEE EAEEKKEKIL LPPKKPLREK SSADLKERRA KAQGPRGDLG SPDPPPKPLR
VRNKEAPAGE GTKMRKTKKK GSGEADKDPS GSPASARKSP AAMFLVGEGS PDKKALKKKG
TPKGARKEEE EEEEAATVIK KSNQKGKAKG KGKKKAKEER APSPPVEVDE PREFVLRPAP
QGRTVRCRLT RDKKGMDRGM YPSYFLHLDT EKKVFLLAGR KRKRSKTANY LISIDPTNLS
RGGENFIGKL RSNLLGNRFT VFDNGQNPQR GYSTNVASLR QELAAVIYET NVLGFRGPRR
MTVIIPGMSA ENERVPIRPR NASDGLLVRW QNKTLESLIE LHNKPPVWND DSGSYTLNFQ
GRVTQASVKN FQIVHADDPD YIVLQFGRVA EDAFTLDYRY PLCALQAFAI ALSSFDGKLA
CE
