ID   OPSG1_ASTFA             Reviewed;         355 AA.
AC   P22330;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Green-sensitive opsin-1;
DE   AltName: Full=Green cone photoreceptor pigment 1;
GN   Name=G103; Synonyms=GF;
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].
RC   TISSUE=Pineal gland;
RX   PubMed=2385921; DOI=10.1016/0042-6989(90)90049-q;
RA   Yokoyama R., Yokoyama S.;
RT   "Isolation, DNA sequence and evolution of a color visual pigment gene of
RT   the blind cave fish Astyanax fasciatus.";
RL   Vision Res. 30:807-816(1990).
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; M60945; AAA48545.1; -; Genomic_DNA.
DR   EMBL; M60938; AAA48545.1; JOINED; Genomic_DNA.
DR   EMBL; M60939; AAA48545.1; JOINED; Genomic_DNA.
DR   EMBL; M60940; AAA48545.1; JOINED; Genomic_DNA.
DR   EMBL; M60943; AAA48545.1; JOINED; Genomic_DNA.
DR   EMBL; M60944; AAA48545.1; JOINED; Genomic_DNA.
DR   EMBL; U12025; AAA67216.1; -; Genomic_DNA.
DR   PIR; I50091; I50091.
DR   AlphaFoldDB; P22330; -.
DR   SMR; P22330; -.
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; IPR000378; Opsin_red/grn.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein 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..355
FT                   /note="Green-sensitive opsin-1"
FT                   /id="PRO_0000197772"
FT   TOPO_DOM        1..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..74
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         309
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   355 AA;  39696 MW;  9B7B6B8F361BCDA2 CRC64;
     MAAHADEPVF AARRYNEETT RESAFVYTNA NNTRDPFEGP NYHIAPRWVY NLASLWMIIV
     VIASIFTNSL VIVATAKFKK LRHPLNWILV NLAIADLGET VLASTISVFN QVFGYFVLGH
     PMCIFEGWTV SVCGITALWS LTIISWERWV VVCKPFGNVK FDGKWAAGGI IFAWTWAIIW
     CTPPIFGWSR YWPHGLKTSC GPDVFSGSED PGVASYMVTL LLTCCILPLS VIIICYIFVW
     NAIHQVAQQQ KDSESTQKAE KEVSRMVVVM ILAFILCWGP YASFATFSAL NPGYAWHPLA
     AALPAYFAKS ATIYNPIIYV FMNRQFRSCI MQLFGKKVED ASEVSGSTTE VSTAS