ID   OPSG_GEKGE              Reviewed;         365 AA.
AC   P35358;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Green-sensitive opsin P521;
DE   AltName: Full=Green photoreceptor pigment;
OS   Gekko gecko (Tokay gecko).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae; Gekko.
OX   NCBI_TaxID=36310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1379723; DOI=10.1073/pnas.89.15.6841;
RA   Kojima D., Okano T., Fukada Y., Shichida Y., Yoshizawa T., Ebrey T.G.;
RT   "Cone visual pigments are present in gecko rod cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6841-6845(1992).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=521 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: In this lizard the color pigments are found in the
CC       rod-shaped photoreceptor cells which have been derived from ancestral
CC       cone-like photoreceptors.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250}.
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; M92036; AAA49308.1; -; mRNA.
DR   PIR; B46191; B46191.
DR   AlphaFoldDB; P35358; -.
DR   SMR; P35358; -.
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   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..365
FT                   /note="Green-sensitive opsin P521"
FT                   /id="PRO_0000197783"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT   TRANSMEM        52..76
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..88
FT                   /note="Cytoplasmic"
FT   TRANSMEM        89..113
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..128
FT                   /note="Extracellular"
FT   TRANSMEM        129..148
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..167
FT                   /note="Cytoplasmic"
FT   TRANSMEM        168..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..217
FT                   /note="Extracellular"
FT   TRANSMEM        218..245
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..267
FT                   /note="Cytoplasmic"
FT   TRANSMEM        268..291
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..299
FT                   /note="Extracellular"
FT   TRANSMEM        300..324
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..365
FT                   /note="Cytoplasmic"
FT   REGION          342..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         311
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   365 AA;  40737 MW;  4C938D03FF43BE95 CRC64;
     MTEAWNVAVF AARRSRDDDD TTRGSVFTYT NTNNTRGPFE GPNYHIAPRW VYNLVSFFMI
     IVVIASCFTN GLVLVATAKF KKLRHPLNWI LVNLAFVDLV ETLVASTISV FNQIFGYFIL
     GHPLCVIEGY VVSSCGITGL WSLAIISWER WFVVCKPFGN IKFDSKLAII GIVFSWVWAW
     GWSAPPIFGW SRYWPHGLKT SCGPDVFSGS VELGCQSFML TLMITCCFLP LFIIIVCYLQ
     VWMAIRAVAA QQKESESTQK AEREVSRMVV VMIVAFCICW GPYASFVSFA AANPGYAFHP
     LAAALPAYFA KSATIYNPVI YVFMNRQFRN CIMQLFGKKV DDGSEASTTS RTEVSSVSNS
     SVAPA