ID   OPSG2_ASTFA             Reviewed;         353 AA.
AC   P22331;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Green-sensitive opsin-2;
DE   AltName: Full=Green cone photoreceptor pigment 2;
GN   Name=G101;
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=2123554; DOI=10.1073/pnas.87.23.9315;
RA   Yokoyama R., Yokoyama S.;
RT   "Convergent evolution of the red- and green-like visual pigment genes in
RT   fish, Astyanax fasciatus, and human.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9315-9318(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; M38624; AAA62671.1; -; Genomic_DNA.
DR   EMBL; M38619; AAA62671.1; JOINED; Genomic_DNA.
DR   EMBL; M38620; AAA62671.1; JOINED; Genomic_DNA.
DR   EMBL; M38621; AAA62671.1; JOINED; Genomic_DNA.
DR   EMBL; M38622; AAA62671.1; JOINED; Genomic_DNA.
DR   EMBL; M38623; AAA62671.1; JOINED; Genomic_DNA.
DR   PIR; A38421; A38421.
DR   AlphaFoldDB; P22331; -.
DR   SMR; P22331; -.
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..353
FT                   /note="Green-sensitive opsin-2"
FT                   /id="PRO_0000197773"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..287
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         307
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   353 AA;  39465 MW;  A7E7B8296AD93253 CRC64;
     MAAHEPVFAA RRHNEDTTRE SAFVYTNANN TRDPFEGPNY HIAPRWVYNV SSLWMIFVVI
     ASVFTNGLVI VATAKFKKLR HPLNWILVNL AIADLGETVL ASTISVINQI FGYFILGHPM
     CVFEGWTVSV CGITALWSLT IISWERWVVV CKPFGNVKFD GKWAAGGIIF SWVWAIIWCT
     PPIFGWSRYW PHGLKTSCGP DVFSGSEDPG VASYMITLML TCCILPLSII IICYIFVWSA
     IHQVAQQQKD SESTQKAEKE VSRMVVVMIL AFIVCWGPYA SFATFSAVNP GYAWHPLAAA
     MPAYFAKSAT IYNPIIYVFM NRQFRSCIMQ LFGKKVEDAS EVSGSTTEVS TAS