ID IMPG2_HUMAN Reviewed; 1241 AA. AC Q9BZV3; A8MWT5; Q9UKD4; Q9UKK5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 25-MAY-2022, entry version 135. DE RecName: Full=Interphotoreceptor matrix proteoglycan 2; DE AltName: Full=Interphotoreceptor matrix proteoglycan of 200 kDa; DE Short=IPM 200; DE AltName: Full=Sialoprotein associated with cones and rods proteoglycan; DE Short=Spacrcan; DE Flags: Precursor; GN Name=IMPG2; Synonyms=IPM200; 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], TISSUE SPECIFICITY, AND VARIANT RP ILE-674. RX PubMed=10542133; DOI=10.1006/mcbr.1999.0161; RA Kuehn M.H., Hageman G.S.; RT "Molecular characterization and genomic mapping of human IPM 200, a second RT member of a novel family of proteoglycans."; RL Mol. Cell Biol. Res. Commun. 2:103-110(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-86; 123-127 AND 582-593, RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, GLYCOSYLATION, AND VARIANT ILE-674. RX PubMed=10702256; DOI=10.1074/jbc.275.10.6945; RA Acharya S., Foletta V.C., Lee J.W., Rayborn M.E., Rodriguez I.R., RA Young W.S. III, Hollyfield J.G.; RT "SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding RT proteoglycan synthesized by photoreceptors and pinealocytes."; RL J. Biol. Chem. 275:6945-6955(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023; RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y., RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C., RA Lako M.; RT "Extracellular matrix component expression in human pluripotent stem cell- RT derived retinal organoids recapitulates retinogenesis in vivo and reveals RT an important role for IMPG1 and CD44 in the development of photoreceptors RT and interphotoreceptor matrix."; RL Acta Biomater. 74:207-221(2018). RN [5] RP VARIANTS ILE-674 AND LEU-1013. RX PubMed=11726612; RA Kuehn M.H., Stone E.M., Hageman G.S.; RT "Organization of the human IMPG2 gene and its evaluation as a candidate RT gene in age-related macular degeneration and other retinal degenerative RT disorders."; RL Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001). RN [6] RP INVOLVEMENT IN RP56, INVOLVEMENT IN VMD5, AND VARIANT VMD5 LEU-124. RX PubMed=20673862; DOI=10.1016/j.ajhg.2010.07.004; RA Bandah-Rozenfeld D., Collin R.W., Banin E., van den Born L.I., Coene K.L., RA Siemiatkowska A.M., Zelinger L., Khan M.I., Lefeber D.J., Erdinest I., RA Testa F., Simonelli F., Voesenek K., Blokland E.A., Strom T.M., RA Klaver C.C., Qamar R., Banfi S., Cremers F.P., Sharon D., RA den Hollander A.I.; RT "Mutations in IMPG2, encoding interphotoreceptor matrix proteoglycan 2, RT cause autosomal-recessive retinitis pigmentosa."; RL Am. J. Hum. Genet. 87:199-208(2010). RN [7] RP VARIANTS RP56 127-ALA--VAL-1241 DEL; 171-LEU--VAL-1241 DEL; RP 212-SER--VAL-1241 DEL; 560-TYR--VAL-1241 DEL; 906-ARG--VAL-1241 DEL; RP 964-ARG--VAL-1241 DEL; 1008-ARG--VAL-1241 DEL AND 296-ARG--ASP-302 DEL, AND RP VARIANT PRO-379. RX PubMed=24876279; DOI=10.1167/iovs.14-14129; RA van Huet R.A., Collin R.W., Siemiatkowska A.M., Klaver C.C., Hoyng C.B., RA Simonelli F., Khan M.I., Qamar R., Banin E., Cremers F.P., Theelen T., RA den Hollander A.I., van den Born L.I., Klevering B.J.; RT "IMPG2-associated retinitis pigmentosa displays relatively early macular RT involvement."; RL Invest. Ophthalmol. Vis. Sci. 55:3939-3953(2014). RN [8] RP INVOLVEMENT IN VMD5, AND VARIANT VMD5 PHE-1077. RX PubMed=25085631; DOI=10.1016/j.ophtha.2014.06.028; RA Meunier I., Manes G., Bocquet B., Marquette V., Baudoin C., Puech B., RA Defoort-Dhellemmes S., Audo I., Verdet R., Arndt C., Zanlonghi X., RA Le Meur G., Dhaenens C.M., Hamel C.P.; RT "Frequency and clinical pattern of vitelliform macular dystrophy caused by RT mutations of interphotoreceptor matrix IMPG1 and IMPG2 genes."; RL Ophthalmology 121:2406-2414(2014). RN [9] RP VARIANTS VMD5 226-GLU--VAL-1241 DEL; 522-SER--VAL-1241 DEL; RP 856-GLN--VAL-1241 DEL AND PHE-1077, AND VARIANTS PRO-243; ASP-1008; RP SER-1016 AND CYS-1042. RX PubMed=28644393; DOI=10.3390/genes8070170; RA Brandl C., Schulz H.L., Charbel Issa P., Birtel J., Bergholz R., Lange C., RA Dahlke C., Zobor D., Weber B.H.F., Stoehr H.; RT "Mutations in the Genes for Interphotoreceptor Matrix Proteoglycans, IMPG1 RT and IMPG2, in Patients with Vitelliform Macular Lesions."; RL Genes (Basel) 8:0-0(2017). CC -!- FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan CC involved in the organization of interphotoreceptor matrix; may CC participate in the maturation and maintenance of the light-sensitive CC photoreceptor outer segment. Binds heparin. CC {ECO:0000269|PubMed:10702256}. CC -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane CC {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein CC {ECO:0000255}. Photoreceptor inner segment membrane CC {ECO:0000250|UniProtKB:Q80XH2}; Single-pass type I membrane protein CC {ECO:0000255}. Secreted, extracellular space, extracellular matrix, CC interphotoreceptor matrix {ECO:0000269|PubMed:10702256}. CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level) CC (PubMed:10702256, PubMed:29777959). Expressed by photoreceptors of the CC interphotoreceptor matrix (IPM) surrounding both rods and cones (at CC protein level) (PubMed:10542133, PubMed:29777959). IPM occupies the CC subretinal space between the apices of the retinal pigment epithelium CC and the neural retina (PubMed:10542133). Expressed in the pineal gland CC (at protein level) (PubMed:10702256). {ECO:0000269|PubMed:10542133, CC ECO:0000269|PubMed:10702256, ECO:0000269|PubMed:29777959}. CC -!- DEVELOPMENTAL STAGE: Expressed in the retina 17 weeks post-conception CC (at protein level) (PubMed:29777959). Expressed in the outer CC neuroblastic zone and retinal pigment epithelium (at protein level) CC (PubMed:29777959). {ECO:0000269|PubMed:29777959}. CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates). CC {ECO:0000269|PubMed:10702256}. CC -!- DISEASE: Retinitis pigmentosa 56 (RP56) [MIM:613581]: 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:20673862, CC ECO:0000269|PubMed:24876279}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A form CC of macular dystrophy, a retinal disease in which various forms of CC deposits, pigmentary changes, and atrophic lesions are observed in the CC macula lutea. Vitelliform macular dystrophies are characterized by CC yellow, lipofuscin-containing deposits, usually localized at the center CC of the macula. VMD5 features include late-onset moderate visual CC impairment and preservation of retinal pigment epithelium reflectivity. CC {ECO:0000269|PubMed:20673862, ECO:0000269|PubMed:25085631, CC ECO:0000269|PubMed:28644393}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AF173155; AAF06999.1; -; mRNA. DR EMBL; AF271379; AAG49889.1; -; Genomic_DNA. DR EMBL; AF271363; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271364; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271365; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271366; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271367; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271368; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271369; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271370; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271371; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271372; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271373; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271374; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271375; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271376; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271377; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF271378; AAG49889.1; JOINED; Genomic_DNA. DR EMBL; AF157624; AAF13154.1; -; mRNA. DR EMBL; AC068764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS2940.1; -. DR RefSeq; NP_057331.2; NM_016247.3. DR AlphaFoldDB; Q9BZV3; -. DR STRING; 9606.ENSP00000193391; -. DR DrugBank; DB08818; Hyaluronic acid. DR GlyGen; Q9BZV3; 10 sites. DR iPTMnet; Q9BZV3; -. DR PhosphoSitePlus; Q9BZV3; -. DR BioMuta; IMPG2; -. DR DMDM; 296439325; -. DR jPOST; Q9BZV3; -. DR MassIVE; Q9BZV3; -. DR PaxDb; Q9BZV3; -. DR PeptideAtlas; Q9BZV3; -. DR PRIDE; Q9BZV3; -. DR ProteomicsDB; 79907; -. DR Antibodypedia; 32271; 50 antibodies from 19 providers. DR DNASU; 50939; -. DR Ensembl; ENST00000193391.8; ENSP00000193391.6; ENSG00000081148.12. DR GeneID; 50939; -. DR KEGG; hsa:50939; -. DR MANE-Select; ENST00000193391.8; ENSP00000193391.6; NM_016247.4; NP_057331.2. DR UCSC; uc003duq.3; human. DR CTD; 50939; -. DR DisGeNET; 50939; -. DR GeneCards; IMPG2; -. DR GeneReviews; IMPG2; -. DR HGNC; HGNC:18362; IMPG2. DR HPA; ENSG00000081148; Tissue enriched (retina). DR MalaCards; IMPG2; -. DR MIM; 607056; gene. DR MIM; 613581; phenotype. DR MIM; 616152; phenotype. DR neXtProt; NX_Q9BZV3; -. DR OpenTargets; ENSG00000081148; -. DR Orphanet; 99000; Adult-onset foveomacular vitelliform dystrophy. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA29866; -. DR VEuPathDB; HostDB:ENSG00000081148; -. DR eggNOG; ENOG502QT6W; Eukaryota. DR GeneTree; ENSGT00530000063503; -. DR HOGENOM; CLU_005111_0_0_1; -. DR InParanoid; Q9BZV3; -. DR OMA; ESSIWPW; -. DR OrthoDB; 112459at2759; -. DR PhylomeDB; Q9BZV3; -. DR TreeFam; TF331340; -. DR PathwayCommons; Q9BZV3; -. DR BioGRID-ORCS; 50939; 9 hits in 1068 CRISPR screens. DR ChiTaRS; IMPG2; human. DR GenomeRNAi; 50939; -. DR Pharos; Q9BZV3; Tbio. DR PRO; PR:Q9BZV3; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9BZV3; protein. DR Bgee; ENSG00000081148; Expressed in oviduct epithelium and 55 other tissues. DR ExpressionAtlas; Q9BZV3; baseline and differential. DR Genevisible; Q9BZV3; HS. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:UniProtKB. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; TAS:UniProtKB. DR Gene3D; 3.30.70.960; -; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR039861; IMPG. DR InterPro; IPR032975; IMPG2. DR InterPro; IPR000082; SEA_dom. DR InterPro; IPR036364; SEA_dom_sf. DR PANTHER; PTHR12199; PTHR12199; 1. DR PANTHER; PTHR12199:SF4; PTHR12199:SF4; 1. DR Pfam; PF01390; SEA; 2. DR SMART; SM00200; SEA; 2. DR SUPFAM; SSF82671; SSF82671; 2. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS50024; SEA; 2. PE 1: Evidence at protein level; KW Cell projection; Direct protein sequencing; Disease variant; KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; KW Heparin-binding; Membrane; Receptor; Reference proteome; Repeat; KW Retinitis pigmentosa; Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..1241 FT /note="Interphotoreceptor matrix proteoglycan 2" FT /id="PRO_0000320149" FT TOPO_DOM 23..1099 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1100..1120 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1121..1241 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 239..353 FT /note="SEA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT DOMAIN 897..1010 FT /note="SEA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT DOMAIN 1010..1051 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1052..1093 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 180..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 259..267 FT /note="Hyaluronan-binding motif involved in chondroitin FT sulfate A-binding" FT /evidence="ECO:0000250" FT REGION 660..684 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1080..1088 FT /note="Hyaluronan-binding motif involved in chondroitin FT sulfate C-binding" FT /evidence="ECO:0000250" FT REGION 1125..1133 FT /note="Hyaluronan-binding motif involved in chondroitin FT sulfate A- and C-binding" FT /evidence="ECO:0000250" FT REGION 1136..1145 FT /note="Hyaluronan-binding motif involved in chondroitin FT sulfate C-binding" FT /evidence="ECO:0000250" FT REGION 1210..1218 FT /note="Hyaluronan-binding motif involved in chondroitin FT sulfate A- and C-binding motif" FT /evidence="ECO:0000250" FT COMPBIAS 180..198 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 660..678 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 154 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 190 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 192 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 320 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 544 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 556 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 942 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 956 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1014..1025 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1019..1036 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1038..1050 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1054..1067 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1061..1077 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1079..1092 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VARIANT 124 FT /note="F -> L (in VMD5; dbSNP:rs201893545)" FT /evidence="ECO:0000269|PubMed:20673862" FT /id="VAR_064336" FT VARIANT 127..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082176" FT VARIANT 171..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082177" FT VARIANT 212..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082178" FT VARIANT 226..1241 FT /note="Missing (in VMD5)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082179" FT VARIANT 243 FT /note="A -> P (found in a patient with vitelliform macular FT dystrophy; unknown pathological significance)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082180" FT VARIANT 296..302 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082181" FT VARIANT 344 FT /note="K -> N (in dbSNP:rs34375459)" FT /id="VAR_039144" FT VARIANT 379 FT /note="S -> P (found in a patient with retinitis FT pigmentosa; unknown pathological significance)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082182" FT VARIANT 522..1241 FT /note="Missing (in VMD5)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082183" FT VARIANT 560..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082184" FT VARIANT 674 FT /note="T -> I (in dbSNP:rs571391)" FT /evidence="ECO:0000269|PubMed:10542133, FT ECO:0000269|PubMed:10702256, ECO:0000269|PubMed:11726612" FT /id="VAR_039145" FT VARIANT 856..1241 FT /note="Missing (in VMD5)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082185" FT VARIANT 906..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082186" FT VARIANT 964..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082187" FT VARIANT 1008 FT /note="G -> D (found in a patient with vitelliform macular FT dystrophy; unknown pathological significance)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082188" FT VARIANT 1013 FT /note="P -> L (in dbSNP:rs116450347)" FT /evidence="ECO:0000269|PubMed:11726612" FT /id="VAR_039146" FT VARIANT 1016 FT /note="F -> S (found in a patient with VMD5; unknown FT pathological significance)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082189" FT VARIANT 1042 FT /note="Y -> C (found in a patient with vitelliform macular FT dystophy; unknown pathological significance)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082190" FT VARIANT 1077 FT /note="C -> F (in VMD5; dbSNP:rs713993049)" FT /evidence="ECO:0000269|PubMed:25085631, FT ECO:0000269|PubMed:28644393" FT /id="VAR_072671" FT VARIANT 1088..1241 FT /note="Missing (in RP56)" FT /evidence="ECO:0000269|PubMed:24876279" FT /id="VAR_082191" FT CONFLICT 5 FT /note="P -> L (in Ref. 2; AAF13154)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="I -> T (in Ref. 2; AAF13154)" FT /evidence="ECO:0000305" FT CONFLICT 668 FT /note="E -> V (in Ref. 2; AAF13154)" FT /evidence="ECO:0000305" FT CONFLICT 715 FT /note="Y -> C (in Ref. 1; AAF06999)" FT /evidence="ECO:0000305" FT CONFLICT 1012 FT /note="N -> T (in Ref. 1; AAG49889)" FT /evidence="ECO:0000305" SQ SEQUENCE 1241 AA; 138621 MW; E72D7BFB84824078 CRC64; MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP EESTDLSLAT KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA VANHVKYFKV RVCQEAVWEA FRTFWDRLPG REEYHYWMNL CEDGVTSIFE MGTNFSESVE HRSLIMKKLT YAKETVSSSE LSSPVPVGDT STLGDTTLSV PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE QIAEFSIHLL GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT ISNFRDYIAE TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT QSSSLQATPS SILDNTFQAA WPSADESITS SIPPLDFSSG PPSATGRELW SESPLGDLVS THKLAFPSKM GLSSSPEVLE VSSLTLHSVT PAVLQTGLPV ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV PKETIPSMED SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV LVDKMDSTDQ ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL TLPKHISEVP GVDDYSVTKA PLILTSVAIS ASTDKSDQAD AILREDMEQI TESSNYEWFD SEVSMVKPDM QTLWTILPES ERVWTRTSSL EKLSRDILAS TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL ELDRIGTDYY QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE ILNFRNGSIV VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK YSLDVESGDE ANPCKFQACN EFSECLVNPW SGEAKCRCFP GYLSVEERPC QSLCDLQPDF CLNDGKCDIM PGHGAICRCR VGENWWYRGK HCEEFVSEPV IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF SGSSRQPDSL SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVEE V //