RET3_HUMAN
ID RET3_HUMAN Reviewed; 1247 AA.
AC P10745; Q0QD34; Q5VSR0; Q8IXN0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Retinol-binding protein 3;
DE AltName: Full=Interphotoreceptor retinoid-binding protein;
DE Short=IRBP;
DE AltName: Full=Interstitial retinol-binding protein;
DE Flags: Precursor;
GN Name=RBP3;
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].
RX PubMed=2542268; DOI=10.1016/s0021-9258(18)83169-6;
RA Liou G.I., Ma D.-P., Yang Y.-W., Geng L., Zhu C., Baehr W.;
RT "Human interstitial retinoid-binding protein. Gene structure and primary
RT structure.";
RL J. Biol. Chem. 264:8200-8206(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2303470; DOI=10.1016/s0021-9258(19)39642-5;
RA Fong S.-L., Fong W.B., Morris T.A., Kedzie K.M., Bridges C.D.B.;
RT "Characterization and comparative structural features of the gene for human
RT interstitial retinol-binding protein.";
RL J. Biol. Chem. 265:3648-3653(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2792773; DOI=10.1016/0378-1119(89)90254-0;
RA Si J.S., Borst D.E., Redmond T.M., Nickerson J.M.;
RT "Cloning of cDNAs encoding human interphotoreceptor retinoid-binding
RT protein (IRBP) and comparison with bovine IRBP sequences.";
RL Gene 80:99-108(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=3170584; DOI=10.1016/s0021-9258(19)37592-1;
RA Fong S.-L., Bridges C.D.B.;
RT "Internal quadruplication in the structure of human interstitial retinol-
RT binding protein deduced from its cloned cDNA.";
RL J. Biol. Chem. 263:15330-15334(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma;
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1247.
RX PubMed=3455009; DOI=10.1007/bf01534925;
RA Liou G.I., Fong S.-L., Gosden J., van Tuinen P., Ledbetter D.H.,
RA Christie S., Rout D., Bhattacharya S., Cook R.G., Li Y., Wang C.,
RA Bridges C.D.B.;
RT "Human interstitial retinol-binding protein (IRBP): cloning, partial
RT sequence, and chromosomal localization.";
RL Somat. Cell Mol. Genet. 13:315-323(1987).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-382.
RX PubMed=2402443; DOI=10.1093/nar/18.17.5181;
RA Albini A., Toffenetti J., Zhen Z., Chader G.J., Noonan D.M.;
RT "Hypomethylation of the interphotoreceptor retinoid-binding protein (IRBP)
RT promotor and first exon is linked to expression of the gene.";
RL Nucleic Acids Res. 18:5181-5187(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-10.
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 [12]
RP PROTEIN SEQUENCE OF 18-42.
RX PubMed=3827838; DOI=10.1042/bj2400019;
RA Redmond T.M., Wiggert B., Robey F.A., Chader G.J.;
RT "Interspecies conservation of structure of interphotoreceptor retinoid-
RT binding protein. Similarities and differences as adjudged by peptide
RT mapping and N-terminal sequencing.";
RL Biochem. J. 240:19-26(1986).
RN [13]
RP PROTEIN SEQUENCE OF 23-39.
RX PubMed=3743780; DOI=10.1016/0014-5793(86)80918-8;
RA Fong S.-L., Cook R.G., Alvarez R.A., Liou G.I., Landers R.A.,
RA Bridges C.D.B.;
RT "N-terminal sequence homologies in interstitial retinol-binding proteins
RT from 10 vertebrate species.";
RL FEBS Lett. 205:309-312(1986).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-530.
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 [15]
RP VARIANT RP66 ASN-1080, AND VARIANTS VAL-18; HIS-122; MET-155; PRO-163;
RP MET-196; GLN-267; MET-282; ILE-321; THR-325; HIS-346; THR-379; LEU-433;
RP SER-443; LEU-505; ARG-518; GLN-523; CYS-535; HIS-544; ALA-593; VAL-599;
RP ASN-614; VAL-615; ILE-675; VAL-688; MET-693; LEU-723; SER-741; CYS-747;
RP LYS-785; CYS-833; SER-835; MET-884; ARG-903; ARG-921; LYS-956; ILE-963;
RP TYR-1021; ILE-1059 AND MET-1194.
RX PubMed=19074801; DOI=10.1167/iovs.08-2497;
RA den Hollander A.I., McGee T.L., Ziviello C., Banfi S., Dryja T.P.,
RA Gonzalez-Fernandez F., Ghosh D., Berson E.L.;
RT "A homozygous missense mutation in the IRBP gene (RBP3) associated with
RT autosomal recessive retinitis pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 50:1864-1872(2009).
RN [16]
RP CHARACTERIZATION OF VARIANT RP66 ASN-1080.
RX PubMed=23486466; DOI=10.1074/jbc.m112.418251;
RA Li S., Yang Z., Hu J., Gordon W.C., Bazan N.G., Haas A.L., Bok D., Jin M.;
RT "Secretory defect and cytotoxicity: the potential disease mechanisms for
RT the retinitis pigmentosa (RP)-associated interphotoreceptor retinoid-
RT binding protein (IRBP).";
RL J. Biol. Chem. 288:11395-11406(2013).
CC -!- FUNCTION: IRBP shuttles 11-cis and all trans retinoids between the
CC retinol isomerase in the pigment epithelium and the visual pigments in
CC the photoreceptor cells of the retina.
CC -!- INTERACTION:
CC P10745; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-12806054, EBI-396137;
CC P10745; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12806054, EBI-10192698;
CC P10745; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12806054, EBI-3867333;
CC P10745; O95967: EFEMP2; NbExp=3; IntAct=EBI-12806054, EBI-743414;
CC P10745; P49639: HOXA1; NbExp=3; IntAct=EBI-12806054, EBI-740785;
CC P10745; O43593: HR; NbExp=3; IntAct=EBI-12806054, EBI-2880706;
CC P10745; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-12806054, EBI-3918847;
CC P10745; Q5T749: KPRP; NbExp=3; IntAct=EBI-12806054, EBI-10981970;
CC P10745; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-12806054, EBI-10172150;
CC P10745; Q8IV28: NID2; NbExp=3; IntAct=EBI-12806054, EBI-10261509;
CC P10745; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-12806054, EBI-769257;
CC P10745; Q12837: POU4F2; NbExp=3; IntAct=EBI-12806054, EBI-17236143;
CC P10745; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-12806054, EBI-11959123;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, interphotoreceptor matrix. Note=Interphotoreceptor matrix that
CC permeates the space between the retina and the contiguous layer of
CC pigment epithelium cells.
CC -!- DISEASE: Retinitis pigmentosa 66 (RP66) [MIM:615233]: 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:19074801,
CC ECO:0000269|PubMed:23486466}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M33875; AAA59453.1; -; Genomic_DNA.
DR EMBL; M33864; AAA59453.1; JOINED; Genomic_DNA.
DR EMBL; M33865; AAA59453.1; JOINED; Genomic_DNA.
DR EMBL; M33866; AAA59453.1; JOINED; Genomic_DNA.
DR EMBL; M22453; AAA36126.1; -; mRNA.
DR EMBL; J05253; AAC18875.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB593121; BAJ84061.1; -; mRNA.
DR EMBL; AL731561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471251; EAW50659.1; -; Genomic_DNA.
DR EMBL; BC039844; AAH39844.1; -; mRNA.
DR EMBL; J03912; AAA59188.1; -; mRNA.
DR EMBL; X53044; CAA37213.1; -; Genomic_DNA.
DR EMBL; DQ426897; ABD90548.1; -; mRNA.
DR CCDS; CCDS73119.1; -.
DR PIR; A33812; A33812.
DR RefSeq; NP_002891.1; NM_002900.2.
DR AlphaFoldDB; P10745; -.
DR SMR; P10745; -.
DR BioGRID; 111883; 16.
DR IntAct; P10745; 13.
DR STRING; 9606.ENSP00000463151; -.
DR DrugBank; DB06755; Beta carotene.
DR DrugBank; DB11948; Lapachone.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; P10745; -.
DR MEROPS; S41.950; -.
DR MEROPS; S41.951; -.
DR GlyGen; P10745; 2 sites.
DR iPTMnet; P10745; -.
DR PhosphoSitePlus; P10745; -.
DR BioMuta; RBP3; -.
DR DMDM; 124894; -.
DR EPD; P10745; -.
DR jPOST; P10745; -.
DR MassIVE; P10745; -.
DR PaxDb; P10745; -.
DR PeptideAtlas; P10745; -.
DR PRIDE; P10745; -.
DR ProteomicsDB; 52643; -.
DR Antibodypedia; 72614; 228 antibodies from 25 providers.
DR DNASU; 5949; -.
DR Ensembl; ENST00000584701.2; ENSP00000463151.1; ENSG00000265203.2.
DR GeneID; 5949; -.
DR KEGG; hsa:5949; -.
DR MANE-Select; ENST00000584701.2; ENSP00000463151.1; NM_002900.3; NP_002891.1.
DR UCSC; uc001jez.3; human.
DR CTD; 5949; -.
DR DisGeNET; 5949; -.
DR GeneCards; RBP3; -.
DR GeneReviews; RBP3; -.
DR HGNC; HGNC:9921; RBP3.
DR HPA; ENSG00000265203; Tissue enriched (retina).
DR MalaCards; RBP3; -.
DR MIM; 180290; gene.
DR MIM; 615233; phenotype.
DR neXtProt; NX_P10745; -.
DR OpenTargets; ENSG00000265203; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA34288; -.
DR VEuPathDB; HostDB:ENSG00000265203; -.
DR eggNOG; ENOG502QW81; Eukaryota.
DR GeneTree; ENSGT00390000014726; -.
DR HOGENOM; CLU_279077_0_0_1; -.
DR InParanoid; P10745; -.
DR OMA; RFDMMAE; -.
DR OrthoDB; 116338at2759; -.
DR PhylomeDB; P10745; -.
DR TreeFam; TF332253; -.
DR BioCyc; MetaCyc:ENSG00000107618-MON; -.
DR PathwayCommons; P10745; -.
DR Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR SignaLink; P10745; -.
DR SIGNOR; P10745; -.
DR BioGRID-ORCS; 5949; 24 hits in 1061 CRISPR screens.
DR ChiTaRS; RBP3; human.
DR GeneWiki; RBP3; -.
DR GenomeRNAi; 5949; -.
DR Pharos; P10745; Tbio.
DR PRO; PR:P10745; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P10745; protein.
DR Bgee; ENSG00000265203; Expressed in pigmented layer of retina and 29 other tissues.
DR Genevisible; P10745; HS.
DR GO; GO:0090658; C:cone matrix sheath; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; TAS:Reactome.
DR GO; GO:0019841; F:retinol binding; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR Pfam; PF03572; Peptidase_S41; 4.
DR SMART; SM00245; TSPc; 4.
DR SUPFAM; SSF52096; SSF52096; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disease variant; Extracellular matrix;
KW Glycoprotein; Reference proteome; Repeat; Retinitis pigmentosa; Secreted;
KW Signal; Transport; Vitamin A.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3827838"
FT CHAIN 18..1247
FT /note="Retinol-binding protein 3"
FT /id="PRO_0000021523"
FT REPEAT 18..320
FT /note="1"
FT REPEAT 321..630
FT /note="2"
FT REPEAT 631..931
FT /note="3"
FT REPEAT 932..1230
FT /note="4"
FT REGION 18..1230
FT /note="4 X approximate tandem repeats"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 18
FT /note="G -> V (in dbSNP:rs864621997)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069669"
FT VARIANT 122
FT /note="R -> H (in dbSNP:rs41302693)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069670"
FT VARIANT 155
FT /note="V -> M (in dbSNP:rs782157576)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069671"
FT VARIANT 163
FT /note="S -> P (in dbSNP:rs35686775)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069672"
FT VARIANT 196
FT /note="V -> M (in dbSNP:rs782398712)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069673"
FT VARIANT 267
FT /note="R -> Q (in dbSNP:rs200239015)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069674"
FT VARIANT 282
FT /note="V -> M (in dbSNP:rs782095820)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069675"
FT VARIANT 321
FT /note="T -> I (in dbSNP:rs376854254)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069676"
FT VARIANT 325
FT /note="A -> T (in dbSNP:rs368898051)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069677"
FT VARIANT 346
FT /note="R -> H (in dbSNP:rs111245635)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069678"
FT VARIANT 379
FT /note="A -> T (in dbSNP:rs781840247)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069679"
FT VARIANT 433
FT /note="S -> L (in dbSNP:rs375761633)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069680"
FT VARIANT 443
FT /note="R -> S (in dbSNP:rs864621999)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069681"
FT VARIANT 505
FT /note="H -> L (in dbSNP:rs201808774)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069682"
FT VARIANT 518
FT /note="Q -> R (in dbSNP:rs563600593)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069683"
FT VARIANT 523
FT /note="H -> Q (in dbSNP:rs148093336)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069684"
FT VARIANT 530
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1354470616)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035929"
FT VARIANT 535
FT /note="R -> C (in dbSNP:rs143632019)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069685"
FT VARIANT 544
FT /note="R -> H (in dbSNP:rs41284962)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069686"
FT VARIANT 593
FT /note="V -> A (in dbSNP:rs782233167)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069687"
FT VARIANT 599
FT /note="I -> V (in dbSNP:rs144289912)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069688"
FT VARIANT 614
FT /note="D -> N (in dbSNP:rs149642039)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069689"
FT VARIANT 615
FT /note="A -> V (in dbSNP:rs368920246)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069690"
FT VARIANT 675
FT /note="T -> I (in dbSNP:rs864622000)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069691"
FT VARIANT 688
FT /note="A -> V (in dbSNP:rs200168559)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069692"
FT VARIANT 693
FT /note="V -> M (in dbSNP:rs112888313)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069693"
FT VARIANT 723
FT /note="P -> L (in dbSNP:rs148247227)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069694"
FT VARIANT 741
FT /note="G -> S (in dbSNP:rs143110000)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069695"
FT VARIANT 747
FT /note="R -> C (in dbSNP:rs782664364)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069696"
FT VARIANT 785
FT /note="N -> K (in dbSNP:rs864622001)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069697"
FT VARIANT 833
FT /note="R -> C (in dbSNP:rs142945423)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069698"
FT VARIANT 835
FT /note="G -> S (in dbSNP:rs782480179)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069699"
FT VARIANT 884
FT /note="V -> M (in dbSNP:rs11204213)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_051315"
FT VARIANT 903
FT /note="T -> R (in dbSNP:rs373766942)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069700"
FT VARIANT 921
FT /note="S -> R (in dbSNP:rs548622709)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069701"
FT VARIANT 956
FT /note="E -> K (in dbSNP:rs781847641)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069702"
FT VARIANT 963
FT /note="T -> I (in dbSNP:rs200706310)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069703"
FT VARIANT 1021
FT /note="S -> Y (in dbSNP:rs148591757)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069704"
FT VARIANT 1059
FT /note="V -> I (in dbSNP:rs864622002)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069705"
FT VARIANT 1080
FT /note="D -> N (in RP66; abolishes secretion; results in
FT mis-folded insoluble complexes degraded via the ER-
FT associated protein catabolic process; dbSNP:rs146150511)"
FT /evidence="ECO:0000269|PubMed:19074801,
FT ECO:0000269|PubMed:23486466"
FT /id="VAR_069706"
FT VARIANT 1194
FT /note="T -> M (in dbSNP:rs782099994)"
FT /evidence="ECO:0000269|PubMed:19074801"
FT /id="VAR_069707"
FT CONFLICT 757
FT /note="V -> G (in Ref. 5; BAJ84061 and 8; AAH39844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1247 AA; 135363 MW; 6C1841411E012E0F CRC64;
MMREWVLLMS VLLCGLAGPT HLFQPSLVLD MAKVLLDNYC FPENLLGMQE AIQQAIKSHE
ILSISDPQTL ASVLTAGVQS SLNDPRLVIS YEPSTPEPPP QVPALTSLSE EELLAWLQRG
LRHEVLEGNV GYLRVDSVPG QEVLSMMGEF LVAHVWGNLM GTSALVLDLR HCTGGQVSGI
PYIISYLHPG NTILHVDTIY NRPSNTTTEI WTLPQVLGER YGADKDVVVL TSSQTRGVAE
DIAHILKQMR RAIVVGERTG GGALDLRKLR IGESDFFFTV PVSRSLGPLG GGSQTWEGSG
VLPCVGTPAE QALEKALAIL TLRSALPGVV HCLQEVLKDY YTLVDRVPTL LQHLASMDFS
TVVSEEDLVT KLNAGLQAAS EDPRLLVRAI GPTETPSWPA PDAAAEDSPG VAPELPEDEA
IRQALVDSVF QVSVLPGNVG YLRFDSFADA SVLGVLAPYV LRQVWEPLQD TEHLIMDLRH
NPGGPSSAVP LLLSYFQGPE AGPVHLFTTY DRRTNITQEH FSHMELPGPR YSTQRGVYLL
TSHRTATAAE EFAFLMQSLG WATLVGEITA GNLLHTRTVP LLDTPEGSLA LTVPVLTFID
NHGEAWLGGG VVPDAIVLAE EALDKAQEVL EFHQSLGALV EGTGHLLEAH YARPEVVGQT
SALLRAKLAQ GAYRTAVDLE SLASQLTADL QEVSGDHRLL VFHSPGELVV EEAPPPPPAV
PSPEELTYLI EALFKTEVLP GQLGYLRFDA MAELETVKAV GPQLVRLVWQ QLVDTAALVI
DLRYNPGSYS TAIPLLCSYF FEAEPRQHLY SVFDRATSKV TEVWTLPQVA GQRYGSHKDL
YILMSHTSGS AAEAFAHTMQ DLQRATVIGE PTAGGALSVG IYQVGSSPLY ASMPTQMAMS
ATTGKAWDLA GVEPDITVPM SEALSIAQDI VALRAKVPTV LQTAGKLVAD NYASAELGAK
MATKLSGLQS RYSRVTSEVA LAEILGADLQ MLSGDPHLKA AHIPENAKDR IPGIVPMQIP
SPEVFEELIK FSFHTNVLED NIGYLRFDMF GDGELLTQVS RLLVEHIWKK IMHTDAMIID
MRFNIGGPTS SIPILCSYFF DEGPPVLLDK IYSRPDDSVS ELWTHAQVVG ERYGSKKSMV
ILTSSVTAGT AEEFTYIMKR LGRALVIGEV TSGGCQPPQT YHVDDTNLYL TIPTARSVGA
SDGSSWEGVG VTPHVVVPAE EALARAKEML QHNQLRVKRS PGLQDHL
