RP1_HUMAN
ID RP1_HUMAN Reviewed; 2156 AA.
AC P56715;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Oxygen-regulated protein 1;
DE AltName: Full=Retinitis pigmentosa 1 protein;
DE AltName: Full=Retinitis pigmentosa RP1 protein;
GN Name=RP1; Synonyms=ORP1;
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 [GENOMIC DNA / MRNA], AND VARIANTS HIS-872; TYR-985;
RP THR-1670; PRO-1691 AND TYR-2033.
RC TISSUE=Retina;
RX PubMed=10391212; DOI=10.1038/10314;
RA Sullivan L.S., Heckenlively J.R., Bowne S.J., Zuo J., Hide W.A., Gal A.,
RA Denton M., Inglehearn C.F., Blanton S.H., Daiger S.P.;
RT "Mutations in a novel retina-specific gene cause autosomal dominant
RT retinitis pigmentosa.";
RL Nat. Genet. 22:255-259(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN RP1.
RC TISSUE=Retina;
RX PubMed=10391211; DOI=10.1038/10305;
RA Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.;
RT "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein
RT cause dominant retinitis pigmentosa.";
RL Nat. Genet. 22:248-254(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10401003; DOI=10.1093/hmg/8.8.1541;
RA Guillonneau X., Piriev N.I., Danciger M., Kozak C.A., Cideciyan A.V.,
RA Jacobson S.G., Farber D.B.;
RT "A nonsense mutation in a novel gene is associated with retinitis
RT pigmentosa in a family linked to the RP1 locus.";
RL Hum. Mol. Genet. 8:1541-1546(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11773008;
RA Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E.,
RA Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.;
RT "Identification and subcellular localization of the RP1 protein in human
RT and mouse photoreceptors.";
RL Invest. Ophthalmol. Vis. Sci. 43:22-32(2002).
RN [6]
RP INVOLVEMENT IN RP1.
RX PubMed=22052604; DOI=10.1002/humu.21640;
RA Audo I., Mohand-Said S., Dhaenens C.M., Germain A., Orhan E., Antonio A.,
RA Hamel C., Sahel J.A., Bhattacharya S.S., Zeitz C.;
RT "RP1 and autosomal dominant rod-cone dystrophy: Novel mutations, a review
RT of published variants, and genotype-phenotype correlation.";
RL Hum. Mutat. 33:73-80(2012).
RN [7]
RP VARIANTS RP1 ASN-663 AND PRO-1808, AND VARIANT GLN-1595.
RX PubMed=10484783; DOI=10.1093/hmg/8.11.2121;
RA Bowne S.J., Daiger S.P., Hims M.M., Sohocki M.M., Malone K.A., McKie A.B.,
RA Heckenlively J.R., Birch D.G., Inglehearn C.F., Bhattacharya S.S., Bird A.,
RA Sullivan L.S.;
RT "Mutations in the RP1 gene causing autosomal dominant retinitis
RT pigmentosa.";
RL Hum. Mol. Genet. 8:2121-2128(1999).
RN [8]
RP VARIANTS RP1 ILE-373; ASN-663; ASN-900 AND ASN-2113, AND VARIANTS HIS-872;
RP TYR-985; GLN-1595; THR-1670; PRO-1691 AND SER-1793.
RX PubMed=11095597;
RA Payne A., Vithana E., Khaliq S., Hameed A., Deller J., Abu-Safieh L.,
RA Kermani S., Leroy B.P., Mehdi S.Q., Moore A.T., Bird A.C.,
RA Bhattacharya S.S.;
RT "RP1 protein truncating mutations predominate at the RP1 adRP locus.";
RL Invest. Ophthalmol. Vis. Sci. 41:4069-4073(2000).
RN [9]
RP VARIANTS GLY-168; THR-218; ILE-373; LEU-376; HIS-872; TYR-985; GLY-1072;
RP SER-1356; PRO-1417; PRO-1425; THR-1670; PRO-1691; SER-1793; LEU-1935;
RP TYR-2033 AND ASN-2066.
RX PubMed=11527933;
RA Berson E.L., Grimsby J.L., Adams S.M., McGee T.L., Sweklo E., Pierce E.A.,
RA Sandberg M.A., Dryja T.P.;
RT "Clinical features and mutations in patients with dominant retinitis
RT pigmentosa-1 (RP1).";
RL Invest. Ophthalmol. Vis. Sci. 42:2217-2224(2001).
RN [10]
RP ASSOCIATION OF VARIANT TYR-985 WITH HYPERTRIGLYCERIDEMIA, AND POLYMORPHISM.
RX PubMed=12764676; DOI=10.1007/s10038-003-0029-z;
RA Fujita Y., Ezura Y., Emi M., Ono S., Takada D., Takahashi K., Uemura K.,
RA Iino Y., Katayama Y., Bujo H., Saito Y.;
RT "Hypertriglyceridemia associated with amino acid variation Asn985Tyr of the
RT RP1 gene.";
RL J. Hum. Genet. 48:305-308(2003).
RN [11]
RP VARIANTS RP1 ILE-373 AND THR-669.
RX PubMed=15863674; DOI=10.1136/jmg.2004.024281;
RA Khaliq S., Abid A., Ismail M., Hameed A., Mohyuddin A., Lall P., Aziz A.,
RA Anwar K., Mehdi S.Q.;
RT "Novel association of RP1 gene mutations with autosomal recessive retinitis
RT pigmentosa.";
RL J. Med. Genet. 42:436-438(2005).
RN [12]
RP VARIANT RP1 GLY-984, AND VARIANTS TRP-727 AND HIS-872.
RX PubMed=15933747; DOI=10.1038/sj.eye.6701944;
RA Chiang S.W., Wang D.Y., Chan W.M., Tam P.O., Chong K.K., Lam D.S.,
RA Pang C.P.;
RT "A novel missense RP1 mutation in retinitis pigmentosa.";
RL Eye 20:602-605(2006).
RN [13]
RP VARIANT RP1 GLU-202.
RX PubMed=19956407;
RA Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H.,
RA Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M.,
RA Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.;
RT "Molecular characterization of retinitis pigmentosa in Saudi Arabia.";
RL Mol. Vis. 15:2464-2469(2009).
RN [14]
RP VARIANTS RP1 GLU-1370 AND LEU-1652, AND VARIANTS LEU-408; ARG-706; HIS-872;
RP TYR-985; THR-1670; PRO-1691 AND TYR-2033.
RX PubMed=20664799;
RA Zhang X., Chen L.J., Law J.P., Lai T.Y., Chiang S.W., Tam P.O., Chu K.Y.,
RA Wang N., Zhang M., Pang C.P.;
RT "Differential pattern of RP1 mutations in retinitis pigmentosa.";
RL Mol. Vis. 16:1353-1360(2010).
RN [15]
RP VARIANT RP1 ARG-172.
RX PubMed=22334370; DOI=10.1002/humu.22045;
RA Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
RA Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
RA Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E.,
RA den Hollander A.I., Hoischen A., Hoyng C., Klevering B.J.,
RA van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.;
RT "Next-generation genetic testing for retinitis pigmentosa.";
RL Hum. Mutat. 33:963-972(2012).
CC -!- FUNCTION: Microtubule-associated protein regulating the stability and
CC length of the microtubule-based axoneme of photoreceptors. Required for
CC the differentiation of photoreceptor cells, it plays a role in the
CC organization of the outer segment of rod and cone photoreceptors
CC ensuring the correct orientation and higher-order stacking of outer
CC segment disks along the photoreceptor axoneme (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the doublecortin domains) with microtubules.
CC Interacts with RP1L1 (By similarity). Interacts with MAK (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:11773008}. Note=Specifically localized in the
CC connecting cilia of rod and cone photoreceptors.
CC -!- TISSUE SPECIFICITY: Expressed in retina. Not expressed in heart, brain,
CC placenta, lung, liver, skeletal muscle, kidney, spleen and pancreas.
CC -!- DOMAIN: The doublecortin domains, which mediate interaction with
CC microtubules, are required for regulation of microtubule polymerization
CC and function in photoreceptor differentiation. {ECO:0000250}.
CC -!- POLYMORPHISM: Tyr-985 is associated with susceptibility to
CC hypertriglyceridemia [MIM:145750] in the homozygous state.
CC {ECO:0000269|PubMed:12764676}.
CC -!- DISEASE: Retinitis pigmentosa 1 (RP1) [MIM:180100]: A retinal dystrophy
CC 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:10391211,
CC ECO:0000269|PubMed:10484783, ECO:0000269|PubMed:11095597,
CC ECO:0000269|PubMed:15863674, ECO:0000269|PubMed:15933747,
CC ECO:0000269|PubMed:19956407, ECO:0000269|PubMed:20664799,
CC ECO:0000269|PubMed:22052604, ECO:0000269|PubMed:22334370}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=RetNet; Note=Retinal information network;
CC URL="https://sph.uth.tmc.edu/retnet/";
CC -!- WEB RESOURCE: Name=Mutations of the RP1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/rp1mut.htm";
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DR EMBL; AF143226; AAD44197.1; -; Genomic_DNA.
DR EMBL; AF143224; AAD44197.1; JOINED; Genomic_DNA.
DR EMBL; AF143225; AAD44197.1; JOINED; Genomic_DNA.
DR EMBL; AF143222; AAD44198.1; -; mRNA.
DR EMBL; AF141021; AAD42072.1; -; mRNA.
DR EMBL; AF152242; AAD46774.1; -; Genomic_DNA.
DR EMBL; AF152240; AAD46774.1; JOINED; Genomic_DNA.
DR EMBL; AF152241; AAD46774.1; JOINED; Genomic_DNA.
DR EMBL; AF146592; AAD46769.1; -; mRNA.
DR EMBL; AF128525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS6160.1; -.
DR RefSeq; NP_006260.1; NM_006269.1.
DR RefSeq; XP_016869211.1; XM_017013722.1.
DR AlphaFoldDB; P56715; -.
DR SMR; P56715; -.
DR BioGRID; 112028; 4.
DR IntAct; P56715; 3.
DR STRING; 9606.ENSP00000220676; -.
DR iPTMnet; P56715; -.
DR PhosphoSitePlus; P56715; -.
DR BioMuta; RP1; -.
DR DMDM; 6225804; -.
DR EPD; P56715; -.
DR MassIVE; P56715; -.
DR MaxQB; P56715; -.
DR PaxDb; P56715; -.
DR PeptideAtlas; P56715; -.
DR PRIDE; P56715; -.
DR ProteomicsDB; 56940; -.
DR Antibodypedia; 50968; 58 antibodies from 10 providers.
DR DNASU; 6101; -.
DR Ensembl; ENST00000220676.2; ENSP00000220676.1; ENSG00000104237.11.
DR GeneID; 6101; -.
DR KEGG; hsa:6101; -.
DR MANE-Select; ENST00000220676.2; ENSP00000220676.1; NM_006269.2; NP_006260.1.
DR UCSC; uc003xsd.1; human.
DR CTD; 6101; -.
DR DisGeNET; 6101; -.
DR GeneCards; RP1; -.
DR GeneReviews; RP1; -.
DR HGNC; HGNC:10263; RP1.
DR HPA; ENSG00000104237; Tissue enriched (retina).
DR MalaCards; RP1; -.
DR MIM; 145750; phenotype.
DR MIM; 180100; phenotype.
DR MIM; 603937; gene.
DR neXtProt; NX_P56715; -.
DR OpenTargets; ENSG00000104237; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA34635; -.
DR VEuPathDB; HostDB:ENSG00000104237; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000154242; -.
DR HOGENOM; CLU_232270_0_0_1; -.
DR InParanoid; P56715; -.
DR PhylomeDB; P56715; -.
DR TreeFam; TF318770; -.
DR PathwayCommons; P56715; -.
DR SignaLink; P56715; -.
DR BioGRID-ORCS; 6101; 5 hits in 1067 CRISPR screens.
DR ChiTaRS; RP1; human.
DR GeneWiki; RP1; -.
DR GenomeRNAi; 6101; -.
DR Pharos; P56715; Tdark.
DR PRO; PR:P56715; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P56715; protein.
DR Bgee; ENSG00000104237; Expressed in right uterine tube and 70 other tissues.
DR ExpressionAtlas; P56715; baseline and differential.
DR Genevisible; P56715; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:UniProtKB.
DR GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
DR GO; GO:0046548; P:retinal rod cell development; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR040163; RP1/RP1L1/DCX.
DR PANTHER; PTHR23005; PTHR23005; 1.
DR Pfam; PF03607; DCX; 2.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disease variant; Microtubule; Reference proteome; Repeat;
KW Retinitis pigmentosa; Sensory transduction; Vision.
FT CHAIN 1..2156
FT /note="Oxygen-regulated protein 1"
FT /id="PRO_0000097410"
FT DOMAIN 36..118
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 154..233
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1590..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 168
FT /note="R -> G (in dbSNP:rs1422215201)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066948"
FT VARIANT 172
FT /note="L -> R (in RP1; dbSNP:rs180729424)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068351"
FT VARIANT 202
FT /note="D -> E (in RP1)"
FT /evidence="ECO:0000269|PubMed:19956407"
FT /id="VAR_064182"
FT VARIANT 218
FT /note="A -> T (in dbSNP:rs145691085)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066949"
FT VARIANT 251
FT /note="Y -> C (in dbSNP:rs16920614)"
FT /id="VAR_051323"
FT VARIANT 373
FT /note="T -> I (in RP1; unknown pathological significance;
FT dbSNP:rs77775126)"
FT /evidence="ECO:0000269|PubMed:11095597,
FT ECO:0000269|PubMed:11527933, ECO:0000269|PubMed:15863674"
FT /id="VAR_064183"
FT VARIANT 376
FT /note="R -> L (in dbSNP:rs1166678265)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066950"
FT VARIANT 408
FT /note="I -> L"
FT /evidence="ECO:0000269|PubMed:20664799"
FT /id="VAR_064466"
FT VARIANT 663
FT /note="K -> N (in RP1; unknown pathological significance;
FT dbSNP:rs372551375)"
FT /evidence="ECO:0000269|PubMed:10484783,
FT ECO:0000269|PubMed:11095597"
FT /id="VAR_064467"
FT VARIANT 669
FT /note="A -> T (in RP1; dbSNP:rs201725231)"
FT /evidence="ECO:0000269|PubMed:15863674"
FT /id="VAR_064468"
FT VARIANT 706
FT /note="G -> R (in dbSNP:rs199879316)"
FT /evidence="ECO:0000269|PubMed:20664799"
FT /id="VAR_064469"
FT VARIANT 727
FT /note="C -> W"
FT /evidence="ECO:0000269|PubMed:15933747"
FT /id="VAR_064470"
FT VARIANT 752
FT /note="T -> M (in dbSNP:rs28399531)"
FT /id="VAR_051324"
FT VARIANT 872
FT /note="R -> H (in dbSNP:rs444772)"
FT /evidence="ECO:0000269|PubMed:10391212,
FT ECO:0000269|PubMed:11095597, ECO:0000269|PubMed:11527933,
FT ECO:0000269|PubMed:15933747, ECO:0000269|PubMed:20664799"
FT /id="VAR_007810"
FT VARIANT 900
FT /note="K -> N (in RP1)"
FT /evidence="ECO:0000269|PubMed:11095597"
FT /id="VAR_066951"
FT VARIANT 945
FT /note="V -> L (in dbSNP:rs16920621)"
FT /id="VAR_051325"
FT VARIANT 984
FT /note="D -> G (in RP1; dbSNP:rs200135800)"
FT /evidence="ECO:0000269|PubMed:15933747"
FT /id="VAR_064471"
FT VARIANT 985
FT /note="N -> Y (associated with susceptibility to
FT hypertriglyceridemia; dbSNP:rs2293869)"
FT /evidence="ECO:0000269|PubMed:10391212,
FT ECO:0000269|PubMed:11095597, ECO:0000269|PubMed:11527933,
FT ECO:0000269|PubMed:20664799"
FT /id="VAR_007811"
FT VARIANT 1072
FT /note="D -> G (in dbSNP:rs756775228)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066952"
FT VARIANT 1356
FT /note="L -> S"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066953"
FT VARIANT 1370
FT /note="K -> E (in RP1; unknown pathological significance;
FT dbSNP:rs186594858)"
FT /evidence="ECO:0000269|PubMed:20664799"
FT /id="VAR_064472"
FT VARIANT 1417
FT /note="L -> P (in dbSNP:rs139294220)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066954"
FT VARIANT 1425
FT /note="L -> P (in dbSNP:rs1338252422)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066955"
FT VARIANT 1595
FT /note="R -> Q (in dbSNP:rs35084330)"
FT /evidence="ECO:0000269|PubMed:10484783,
FT ECO:0000269|PubMed:11095597"
FT /id="VAR_051326"
FT VARIANT 1652
FT /note="R -> L (in RP1; unknown pathological significance;
FT dbSNP:rs760740229)"
FT /evidence="ECO:0000269|PubMed:20664799"
FT /id="VAR_064473"
FT VARIANT 1670
FT /note="A -> T (in dbSNP:rs446227)"
FT /evidence="ECO:0000269|PubMed:10391212,
FT ECO:0000269|PubMed:11095597, ECO:0000269|PubMed:11527933,
FT ECO:0000269|PubMed:20664799"
FT /id="VAR_007812"
FT VARIANT 1691
FT /note="S -> P (in dbSNP:rs414352)"
FT /evidence="ECO:0000269|PubMed:10391212,
FT ECO:0000269|PubMed:11095597, ECO:0000269|PubMed:11527933,
FT ECO:0000269|PubMed:20664799"
FT /id="VAR_007813"
FT VARIANT 1793
FT /note="P -> S (in dbSNP:rs143088423)"
FT /evidence="ECO:0000269|PubMed:11095597,
FT ECO:0000269|PubMed:11527933"
FT /id="VAR_066956"
FT VARIANT 1808
FT /note="L -> P (in RP1; unknown pathological significance;
FT dbSNP:rs371969576)"
FT /evidence="ECO:0000269|PubMed:10484783"
FT /id="VAR_064474"
FT VARIANT 1935
FT /note="F -> L (in dbSNP:rs140137224)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066957"
FT VARIANT 2033
FT /note="C -> Y (in dbSNP:rs61739567)"
FT /evidence="ECO:0000269|PubMed:10391212,
FT ECO:0000269|PubMed:11527933, ECO:0000269|PubMed:20664799"
FT /id="VAR_007814"
FT VARIANT 2066
FT /note="D -> N (in dbSNP:rs149282954)"
FT /evidence="ECO:0000269|PubMed:11527933"
FT /id="VAR_066958"
FT VARIANT 2113
FT /note="T -> N (in RP1; dbSNP:rs137887415)"
FT /evidence="ECO:0000269|PubMed:11095597"
FT /id="VAR_066959"
SQ SEQUENCE 2156 AA; 240661 MW; 55AEDBEC43D6A507 CRC64;
MSDTPSTGFS IIHPTSSEGQ VPPPRHLSLT HPVVAKRISF YKSGDPQFGG VRVVVNPRSF
KSFDALLDNL SRKVPLPFGV RNISTPRGRH SITRLEELED GESYLCSHGR KVQPVDLDKA
RRRPRPWLSS RAISAHSPPH PVAVAAPGMP RPPRSLVVFR NGDPKTRRAV LLSRRVTQSF
EAFLQHLTEV MQRPVVKLYA TDGRRVPSLQ AVILSSGAVV AAGREPFKPG NYDIQKYLLP
ARLPGISQRV YPKGNAKSES RKISTHMSSS SRSQIYSVSS EKTHNNDCYL DYSFVPEKYL
ALEKNDSQNL PIYPSEDDIE KSIIFNQDGT MTVEMKVRFR IKEEETIKWT TTVSKTGPSN
NDEKSEMSFP GRTESRSSGL KLAACSFSAD VSPMERSSNQ EGSLAEEINI QMTDQVAETC
SSASWENATV DTDIIQGTQD QAKHRFYRPP TPGLRRVRQK KSVIGSVTLV SETEVQEKMI
GQFSYSEERE SGENKSEYHM FTHSCSKMSS VSNKPVLVQI NNNDQMEESS LERKKENSLL
KSSAISAGVI EITSQKMLEM SHNNGLPSTI SNNSIVEEDV VDCVVLDNKT GIKNFKTYGN
TNDRFSPISA DATHFSSNNS GTDKNISEAP ASEASSTVTA RIDRLINEFA QCGLTKLPKN
EKKILSSVAS KKKKKSRQQA INSRYQDGQL ATKGILNKNE RINTKGRITK EMIVQDSDSP
LKGGILCEED LQKSDTVIES NTFCSKSNLN STISKNFHRN KLNTTQNSKV QGLLTKRKSR
SLNKISLGAP KKREIGQRDK VFPHNESKYC KSTFENKSLF HVFNILEQKP KDFYAPQSQA
EVASGYLRGM AKKSLVSKVT DSHITLKSQK KRKGDKVKAS AILSKQHATT RANSLASLKK
PDFPEAIAHH SIQNYIQSWL QNINPYPTLK PIKSAPVCRN ETSVVNCSNN SFSGNDPHTN
SGKISNFVME SNKHITKIAG LTGDNLCKEG DKSFIANDTG EEDLHETQVG SLNDAYLVPL
HEHCTLSQSA INDHNTKSHI AAEKSGPEKK LVYQEINLAR KRQSVEAAIQ VDPIEEETPK
DLLPVLMLHQ LQASVPGIHK TQNGVVQMPG SLAGVPFHSA ICNSSTNLLL AWLLVLNLKG
SMNSFCQVDA HKATNKSSET LALLEILKHI AITEEADDLK AAVANLVEST TSHFGLSEKE
QDMVPIDLSA NCSTVNIQSV PKCSENERTQ GISSLDGGCS ASEACAPEVC VLEVTCSPCE
MCTVNKAYSP KETCNPSDTF FPSDGYGVDQ TSMNKACFLG EVCSLTDTVF SDKACAQKEN
HTYEGACPID ETYVPVNVCN TIDFLNSKEN TYTDNLDSTE ELERGDDIQK DLNILTDPEY
KNGFNTLVSH QNVSNLSSCG LCLSEKEAEL DKKHSSLDDF ENCSLRKFQD ENAYTSFDME
EPRTSEEPGS ITNSMTSSER NISELESFEE LENHDTDIFN TVVNGGEQAT EELIQEEVEA
SKTLELIDIS SKNIMEEKRM NGIIYEIISK RLATPPSLDF CYDSKQNSEK ETNEGETKMV
KMMVKTMETG SYSESSPDLK KCIKSPVTSD WSDYRPDSDS EQPYKTSSDD PNDSGELTQE
KEYNIGFVKR AIEKLYGKAD IIKPSFFPGS TRKSQVCPYN SVEFQCSRKA SLYDSEGQSF
GSSEQVSSSS SMLQEFQEER QDKCDVSAVR DNYCRGDIVE PGTKQNDDSR ILTDIEEGVL
IDKGKWLLKE NHLLRMSSEN PGMCGNADTT SVDTLLDNNS SEVPYSHFGN LAPGPTMDEL
SSSELEELTQ PLELKCNYFN MPHGSDSEPF HEDLLDVRNE TCAKERIANH HTEEKGSHQS
ERVCTSVTHS FISAGNKVYP VSDDAIKNQP LPGSNMIHGT LQEADSLDKL YALCGQHCPI
LTVIIQPMNE EDRGFAYRKE SDIENFLGFY LWMKIHPYLL QTDKNVFREE NNKASMRQNL
IDNAIGDIFD QFYFSNTFDL MGKRRKQKRI NFLGLEEEGN LKKFQPDLKE RFCMNFLHTS
LLVVGNVDSN TQDLSGQTNE IFKAVDENNN LLNNRFQGSR TNLNQVVREN INCHYFFEML
GQACLLDICQ VETSLNISNR NILELCMFEG ENLFIWEEED ILNLTDLESS REQEDL
