EYS_DANRE
ID EYS_DANRE Reviewed; 2904 AA.
AC B8JI71;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein eyes shut homolog {ECO:0000303|PubMed:27737822};
DE Flags: Precursor;
GN Name=eys {ECO:0000303|PubMed:27737822};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27737822; DOI=10.1242/bio.021584;
RA Yu M., Liu Y., Li J., Natale B.N., Cao S., Wang D., Amack J.D., Hu H.;
RT "Eyes shut homolog is required for maintaining the ciliary pocket and
RT survival of photoreceptors in zebrafish.";
RL Biol. Open 5:1662-1673(2016).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF CYS-1860.
RX PubMed=28378834; DOI=10.1038/srep46098;
RA Lu Z., Hu X., Liu F., Soares D.C., Liu X., Yu S., Gao M., Han S., Qin Y.,
RA Li C., Jiang T., Luo D., Guo A.Y., Tang Z., Liu M.;
RT "Ablation of EYS in zebrafish causes mislocalisation of outer segment
RT proteins, F-actin disruption and cone-rod dystrophy.";
RL Sci. Rep. 7:46098-46098(2017).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-1163.
RX PubMed=30052645; DOI=10.1371/journal.pone.0200789;
RA Messchaert M., Dona M., Broekman S., Peters T.A., Corral-Serrano J.C.,
RA Slijkerman R.W.N., van Wijk E., Collin R.W.J.;
RT "Eyes shut homolog is important for the maintenance of photoreceptor
RT morphology and visual function in zebrafish.";
RL PLoS ONE 13:E0200789-E0200789(2018).
CC -!- FUNCTION: Required to maintain the integrity of photoreceptor cells
CC (PubMed:27737822, PubMed:28378834, PubMed:30052645). Specifically
CC required for normal morphology of the photoreceptor ciliary pocket, and
CC might thus facilitate protein trafficking between the photoreceptor
CC inner and outer segments via the transition zone (PubMed:27737822).
CC {ECO:0000269|PubMed:27737822, ECO:0000269|PubMed:28378834,
CC ECO:0000269|PubMed:30052645}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:27737822, ECO:0000269|PubMed:30052645}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A0A2K5V015}.
CC Secreted, extracellular space, extracellular matrix, interphotoreceptor
CC matrix {ECO:0000250|UniProtKB:A0A2K5V015}. Note=Localizes to discrete
CC puncta at, or adjacent to, the photoreceptor connecting cilium
CC (PubMed:27737822, PubMed:30052645). May localize to the cilium axoneme
CC (By similarity). May also be expressed in the interphotoreceptor
CC extracellular matrix (By similarity). Unlike the primate ortholog, does
CC not appear to be expressed in the photoreceptor outer segment
CC (PubMed:27737822). {ECO:0000250|UniProtKB:A0A2K5V015,
CC ECO:0000269|PubMed:27737822, ECO:0000269|PubMed:30052645}.
CC -!- TISSUE SPECIFICITY: Expressed in retina where it localizes between the
CC retinal pigment epithelium and the outer nuclear layer (at protein
CC level). {ECO:0000269|PubMed:27737822, ECO:0000269|PubMed:30052645}.
CC -!- DISRUPTION PHENOTYPE: Progressive loss of cone photoreceptors in the
CC retina from two months post-fertilization (mpf) onwards, with almost
CC complete loss by 9 mpf. Rod photoreceptors also show signs of
CC degeneration in older animals of 14 mpf. Photoreceptor degeneration is
CC accompanied by increased apoptosis and mislocalization of outer segment
CC proteins. At the ultrastructural level, morphology of the photoreceptor
CC ciliary pocket is frequently abnormal with either complete collapse of
CC the pocket, or presence of multiple membranous vesicles.
CC {ECO:0000269|PubMed:27737822}.
CC -!- SIMILARITY: Belongs to the EYS family. {ECO:0000305}.
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DR EMBL; BX005106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX323836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR456624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU570696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009305788.1; XM_009307513.2.
DR RefSeq; XP_009305789.1; XM_009307514.2.
DR STRING; 7955.ENSDARP00000109425; -.
DR PaxDb; B8JI71; -.
DR GeneID; 557044; -.
DR KEGG; dre:557044; -.
DR CTD; 346007; -.
DR ZFIN; ZDB-GENE-130530-959; eys.
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_004826_3_2_1; -.
DR PhylomeDB; B8JI71; -.
DR PRO; PR:B8JI71; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:ZFIN.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:ZFIN.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0046549; P:retinal cone cell development; IMP:ZFIN.
DR GO; GO:0007601; P:visual perception; IMP:ZFIN.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 24.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 5.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 41.
DR SMART; SM00179; EGF_CA; 38.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; SSF49899; 5.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 21.
DR PROSITE; PS00022; EGF_1; 41.
DR PROSITE; PS01186; EGF_2; 32.
DR PROSITE; PS50026; EGF_3; 41.
DR PROSITE; PS01187; EGF_CA; 16.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cytoplasm; Cytoskeleton; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Sensory transduction; Signal; Vision.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..2904
FT /note="Protein eyes shut homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446503"
FT DOMAIN 174..216
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..259
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 263..298
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 300..336
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 375..411
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 413..451
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 453..496
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 498..534
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 565..603
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 605..641
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 642..677
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 679..715
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 717..753
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 755..793
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 795..831
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 833..869
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 871..907
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 909..945
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 947..983
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 984..1026
FT /note="EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1028..1063
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1065..1101
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1103..1139
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1141..1179
FT /note="EGF-like 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1181..1220
FT /note="EGF-like 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1222..1258
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1260..1296
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1298..1334
FT /note="EGF-like 28; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1336..1372
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1374..1409
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1411..1447
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1449..1491
FT /note="EGF-like 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1493..1529
FT /note="EGF-like 33; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1531..1568
FT /note="EGF-like 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1640..1818
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1856..1897
FT /note="EGF-like 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1902..2102
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2098..2134
FT /note="EGF-like 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2135..2171
FT /note="EGF-like 37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2182..2372
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2373..2409
FT /note="EGF-like 38"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2411..2452
FT /note="EGF-like 39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2459..2642
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2638..2675
FT /note="EGF-like 40"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2676..2714
FT /note="EGF-like 41"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2719..2894
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 178..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 187..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 206..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 221..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 226..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 249..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 267..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 271..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 288..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 304..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 309..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 326..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 379..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 384..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 417..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 424..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 441..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 457..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 464..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 486..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 502..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 507..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 524..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 568..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 575..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 593..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 609..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 631..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 650..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 667..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 688..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 705..714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 721..732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 726..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 743..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 759..772
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 783..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 799..810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 804..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 821..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 837..848
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 842..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 859..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 875..886
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 880..895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 897..906
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 913..924
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 918..933
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 935..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 951..962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 956..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 973..982
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 987..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 993..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1016..1025
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1032..1042
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1037..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1053..1062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1069..1080
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1074..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1091..1100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1107..1118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1112..1127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1129..1138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1145..1156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1150..1167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1169..1178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1185..1198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1192..1208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1210..1219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1226..1237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1231..1246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1248..1257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1264..1275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1269..1284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1286..1295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1302..1313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1307..1322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1324..1333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1340..1351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1345..1360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1362..1371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1378..1388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1383..1397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1399..1408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1415..1426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1420..1435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1437..1446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1453..1469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1463..1479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1481..1490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1497..1508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1502..1517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1519..1528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1535..1545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1540..1556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1558..1567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1792..1818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1860..1871
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1865..1885
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1887..1896
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2071..2102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2102..2113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2107..2122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2124..2133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2138..2149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2143..2159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2161..2170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2339..2372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 2377..2388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2382..2397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2399..2408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2415..2431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2425..2440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2442..2451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2642..2653
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2647..2663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2665..2674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2680..2691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2685..2702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2704..2713
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 1163
FT /note="Missing: In rmc101; impaired visual function from an
FT early age. Light-induced locomotor activity is
FT significantly reduced. Morphology of the photoreceptor
FT outer segment is impaired. Localization of rho (rhodopsin)
FT and gnat2 to the photoreceptor outer segment and
FT photoreceptor F-actin morphology is also disrupted."
FT /evidence="ECO:0000269|PubMed:30052645"
FT MUTAGEN 1860
FT /note="Missing: In del8; impaired visual function from an
FT early age. Progressive degeneration of the retinal outer
FT nuclear layer is detected from 2 months of age onwards,
FT associated with increased apoptosis. Both rod and cone type
FT photoreceptors show progressively reduced outer segment
FT length. The photoreceptor outer segment proteins gnb3b and
FT prph2 are mislocalized to the inner segment, and
FT photoreceptor F-actin morphology is disrupted. Cone type
FT photoreceptors also decline in number with age."
FT /evidence="ECO:0000269|PubMed:28378834"
SQ SEQUENCE 2904 AA; 317343 MW; C8A6BB9E89AA6108 CRC64;
MRNPKLAIIV FLLSCVIYGP VYSQVTCRRA TSREWHTQPK NISVRWTLME NTCSSLTQCW
SSFAETNGHF WTTGPYHFPQ LCPLELQLGD LLFVSADGTL EQHGVQLIKV SKEEFDKCAI
LEPRKEQLVF ASSINGTLQV ESKWLMSGLN YFTIINRGSS HLCRFGLRIA VLVKPQLCQS
SPLLRLCSGK GECRTTLKDD SFTCRCHKHF SGRYCENVDG CYEQPCLNGG TCLSEGSAYT
DLPPYTCLCP APFTGVNCSE IIGNQNCSKW CKEGACLKVS STSYRCECFT GYTGTYCERK
RLFCDSNPCR NDGRCEETAN GYVCTCPGGF TGLNCETTAE ADSYCKSSGC QLDEACATDK
LNATCICVDP ECLEQAEVCG TLPCLNGGIC VVPNGQYHCR CRQGFSGKNC EEIIDFCKLL
NINCLNEGLC LNRVGGYNCL CAPGWTGEFC QYLENACLAY PNRCLNGATC ISMSQTTAPP
HYMCTCLPGY TGPYCEAEVN ECDSSPCQHQ GTCTDFVGYY KCTCPSGYTG IDCEIDINSC
WLPNATCPPE TLCVDLPGDQ LFKCHTPCPH YLQPCANGGH CVLHNITSYS CVCAPGWTGA
TCLVNINECV QHRCQNRATC VDEVGGYSCL CGHGYTGVHC ELDFCSGHQC SEHAVCVDQQ
HNYTCRCMLG YEGTLCELET DECKSAPCTN NATCIDLVAG YQCLCAPGFK GRTCSESMNE
CWSRPCNNGG SCIDLVNDYI CNCPLGFTGH DCSMPATGCT SNPCNTKGTS MCEEQQDGFK
CVCHHGYTGL FCETSINHCV EGLCHHGSEC VDLTKGFMCE CLPGLRGRLC EVNIDDCLDK
PCGALSICKD GINAYDCFCA PGFVGNNCEI EVNECLSQPC QNGASCSDEL NSFSCLCLAG
TTGSLCEINI DECQSSPCMN NGTCLDLSDG FKCICPSGFS GPECSMDINE CVSYPCKNGG
SCIDQPGNYY CRCLAPFKGL NCELLPCEAV NPCDNGAECV EEADLVLFPL GFQCRCRKGF
TGPRCEVNID ECSSNPCLNG FCYDAVDGFY CLCNPGYAGV RCEQHINDCA SNMCENNSTC
VDLHLSYNCL CLPGWEGEYC QRETNECLSN PCKNNATCTD LLNAYRCVCP QGWTGLDCDE
DVKECSSSPC LNGAHCVESD TPGEFSCTCP PFFTGPLCEQ PYDPCELQRN PCLHNSTCRA
QSDGTALCVC PVGFEGTRCE IDSDDCVSRP CQNRGICVDG VNSYSCFCEP GFSGLHCEED
INECASNPCQ NQAVCQDLVN GFQCSCVPGY FGPHCNLDVN ECDSSPCLHE SVCINKPGGF
ACVCSAGFSG KWCELNVDEC KSNPCRNNGS CIDGLNGYQC VCSRGFMGDH CERNTDECSS
GPCVHGSCLD EIDAFSCQCE VGWTGHRCQI NINECEAHPC LNGGSCVDLL DKYACICADG
FTGKNCDIDQ NVCLQTSLNF SLCFNGGTCV DGPGVNFTCS CRPGFMGDFC EVEMNECCSE
PCFNGAICQD LINGYQCHCR PGWTGLHCED DINECLLQPC NQGMCIQNEP GHGYTCFCRP
GFVGENCEYN YDDCLIQSCP ETFSCKDGIN NVSCVPVKTD TSSLPPISVV SWRSTDISTE
LQPTFAPVEN LQHTEQPADA SFGGYSGNSF LEFGGFEVAV PISVTVRFQT ESMYGTLLYS
ASAKRSVFFI KLYISNGILQ YDFLCNQKQG VQRINTAQWV ADGNEHVVIF RQCLFPCVAE
VTVSGVRTVR SAPGNYTSAL RLQRTDHVFI GGLPRHRSPY KEAEPFHNYT GCIEIIEINK
LRRFHMDHAI ARNNVDNCRS QWHHEPPTSS THSPTLLITV ETPPGEWVRV LSPTQPAPVC
PQGICLNGGT CRPVSLPSGA SSFFCDCPLH FTGRLCEQDI TVFSPRFDGN SFLELPSLTS
LFQSDTYFPS RSSEDKRILY LTMKSRTPHG SLLYCREQDL GERFLHVFLQ NARAVARLGC
GAAHILTAVA AQNIRIDSLV AITVRYALPS QNNGQLCFIE IAADNGTANQ QQKYMDEPVS
EVVFGPTFLG GFPSVLELHH NSGNVSGFIG CIRELQMGSK ELYVVGEAIR GQNIQNCDAA
VCQHQPCRNG GTCISDAESW FCACPSLYSG KLCQFTACER NPCARGATCV PQTQLEAACL
CPYGRQGLLC DEAINITRPK FSGLDEFGYS SYVAYPSIPS TGHFYEFHLK LTFANNASAL
RNNLILFSGQ KGQGLSGDDF FALGVRNGRI VHKYNLGSGL ATIISDRLNP RINIHTVHFG
RYLKTGWLKV NGQKRRTGTS PGPLMGLNTF SQLYIGGYEE YTPELLPPGS RFQNSFQGCI
FDMLFRTRQD GKFHALGGPD IRPLSGRNVG QCGVNPCSLV FCHNGGTCVD SGSSVYCQCV
FGWKGALCSE KVSFCDAEHI PPPFCARGST CVPLSDGYTC QCPLGSAGLH CQQAITISDP
FFSGNQSSWM SFPPINIRHR THVQLQFQTL SPEGILFYTA QHLSTHSGDF LSISLSAGFL
QLRYNLGNQT IVLQSPKELD VTGVRWHTVK AGREGNSGFL IVDGESVTRN SSEGSTTLDV
GANIFIGGIS SLNTVSIDAV EKELVGFTGG IREVVVNGQE LELTETGALD GANVGDWDGT
ACGYKVCKNG GHCHPSGDFS FTCICPSLWT GSRCQQSIQC LNNLCQHNSV CIHNSTSASY
SCMCSLGWTG THCDREVTLK TIRFIGNSYL KYKDPKYNSR NLMHTEVSLN FSTSAGDGLI
FWMGKAESED DDHLAVGLQD GYLKISVNLG ERTALPLVYQ NSFCCNYWNY LSITHNRTLI
QVYVNEERVI FEDIDPFEQY VAVNYGGVIY LGGFELNRDV ASVTSGVFTK GFEGSIKDVF
LYQDTKQLQF LQTCEGFNVY QGEE
