ID   OPSG3_ASTFA             Reviewed;         354 AA.
AC   P51474;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Green-sensitive opsin-3;
DE   AltName: Full=Green cone photoreceptor pigment 3;
GN   Name=RH11;
OS   Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Psalidodon.
OX   NCBI_TaxID=223369;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7932788; DOI=10.1007/bf00160150;
RA   Register E.A., Yokoyama R., Yokoyama S.;
RT   "Multiple origins of the green-sensitive opsin genes in fish.";
RL   J. Mol. Evol. 39:268-273(1994).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: The color pigments are found in the cone
CC       photoreceptor cells.
CC   -!- MISCELLANEOUS: This fish possesses three genes for green opsin. Two
CC       (G103 and G101) that belong to the LWS/MWS group and one (RH11) that
CC       belongs to the RH2 group.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; S75255; AAB32221.2; -; Genomic_DNA.
DR   EMBL; S75251; AAB32221.2; JOINED; Genomic_DNA.
DR   EMBL; S75252; AAB32221.2; JOINED; Genomic_DNA.
DR   EMBL; S75253; AAB32221.2; JOINED; Genomic_DNA.
DR   EMBL; S75254; AAB32221.2; JOINED; Genomic_DNA.
DR   PIR; I51266; I51266.
DR   AlphaFoldDB; P51474; -.
DR   SMR; P51474; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   InterPro; IPR000732; Rhodopsin.
DR   InterPro; IPR019477; Rhodopsin_N.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF10413; Rhodopsin_N; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   2: Evidence at transcript level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..354
FT                   /note="Green-sensitive opsin-3"
FT                   /id="PRO_0000197774"
FT   TOPO_DOM        1..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..64
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..102
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..179
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..279
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..287
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..312
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..354
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         299
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   354 AA;  39117 MW;  023C474F9F08048A CRC64;
     MSGLNGFEGD NFYIPMSNRT GLVRDPFVYE QYYLAEPWQF KLLACYMFFL ICLGLPINGF
     TLFVTAQHKK LQQPLNFILV NLAVAGMIMV CFGFTITISS AVNGYFYFGP TACAIEGFMA
     TLGGEVALWS LVVLAIERYI VVCKPMGSFK FSASHALGGI GFTWFMAMTC AAPPLVGWSR
     YIPEGLQCSC GPDYYTLNPK YNNESYVIYM FVVHFIVPVT VIFFTYGRLV CTVKSAAAAQ
     QDSASTQKAE KEVTRMVILM VVGFLVAWTP YATVAAWIFF NKGAAFTAQF MAVPAFFSKS
     SALFNPIIYV LLNKQFRNCM LTTLFCGKNP LGDEESSTVS TKTEVSTVSS VSPA