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 24-JAN-2024, entry version 143.
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 GlyCosmos; Q9BZV3; 10 sites, No reported glycans.
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; 9606-ENSP00000193391; -.
DR PeptideAtlas; Q9BZV3; -.
DR ProteomicsDB; 79907; -.
DR Antibodypedia; 32271; 63 antibodies from 20 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 AGR; HGNC:18362; -.
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; 4244504at2759; -.
DR PhylomeDB; Q9BZV3; -.
DR TreeFam; TF331340; -.
DR PathwayCommons; Q9BZV3; -.
DR BioGRID-ORCS; 50939; 9 hits in 1146 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 right uterine tube and 63 other cell types or 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:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; SEA domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR039861; IMPG.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR PANTHER; PTHR12199; INTERPHOTORECEPTOR MATRIX PROTEOGLYCAN; 1.
DR PANTHER; PTHR12199:SF4; INTERPHOTORECEPTOR MATRIX PROTEOGLYCAN 2; 1.
DR Pfam; PF01390; SEA; 2.
DR SMART; SM00200; SEA; 2.
DR SUPFAM; SSF82671; SEA domain; 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; uncertain significance; dbSNP:rs1706811719)"
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; uncertain 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; uncertain 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; uncertain
FT 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; uncertain 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
//
