ID   OPSB_GEKGE              Reviewed;         355 AA.
AC   P35357;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Blue-sensitive opsin P467;
DE   AltName: Full=Blue 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)=467 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; M92035; AAA49307.1; -; mRNA.
DR   PIR; A46191; A46191.
DR   AlphaFoldDB; P35357; -.
DR   SMR; P35357; -.
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   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="Blue-sensitive opsin P467"
FT                   /id="PRO_0000197760"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT   TRANSMEM        37..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..73
FT                   /note="Cytoplasmic"
FT   TRANSMEM        74..98
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..113
FT                   /note="Extracellular"
FT   TRANSMEM        114..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..152
FT                   /note="Cytoplasmic"
FT   TRANSMEM        153..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..202
FT                   /note="Extracellular"
FT   TRANSMEM        203..230
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..252
FT                   /note="Cytoplasmic"
FT   TRANSMEM        253..276
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..284
FT                   /note="Extracellular"
FT   TRANSMEM        285..309
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..355
FT                   /note="Cytoplasmic"
FT   REGION          333..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         296
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        110..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   355 AA;  39688 MW;  691124B45CEAE83C CRC64;
     MNGTEGINFY VPLSNKTGLV RSPFEYPQYY LADPWKFKVL SFYMFFLIAA GMPLNGLTLF
     VTFQHKKLRQ PLNYILVNLA AANLVTVCCG FTVTFYASWY AYFVFGPIGC AIEGFFATIG
     GQVALWSLVV LAIERYIVIC KPMGNFRFSA THAIMGIAFT WFMALACAGP PLFGWSRFIP
     EGMQCSCGPD YYTLNPDFHN ESYVIYMFIV HFTVPMVVIF FSYGRLVCKV REAAAQQQES
     ATTQKAEKEV TRMVILMVLG FLLAWTPYAA TAIWIFTNRG AAFSVTFMTI PAFFSKSSSI
     YNPIIYVLLN KQFRNCMVTT ICCGKNPFGD EDVSSSVSQS KTEVSSVSSS QVAPA