ID   OPSD_CORAU              Reviewed;         131 AA.
AC   Q90305;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Rhodopsin;
DE   Flags: Fragment;
GN   Name=rho;
OS   Coregonus autumnalis (Arctic cisco) (Salmo autumnalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Coregoninae; Coregonus.
OX   NCBI_TaxID=27773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=7590342; DOI=10.1016/0378-1119(95)00458-i;
RA   Fitzgibbon J., Hope A., Slobodyanyuk S.J., Bellingham J., Bowmaker J.K.,
RA   Hunt D.M.;
RT   "The rhodopsin-encoding gene of bony fish lacks introns.";
RL   Gene 164:273-277(1995).
CC   -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC       intensity. While most salt water fish species use retinal as
CC       chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of
CC       retinal and 3-dehydroretinal (By similarity). Light-induced
CC       isomerization of 11-cis to all-trans retinal triggers a conformational
CC       change that activates signaling via G-proteins. Subsequent receptor
CC       phosphorylation mediates displacement of the bound G-protein alpha
CC       subunit by arrestin and terminates signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC       ECO:0000250|UniProtKB:P32309}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection,
CC       cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P35359}.
CC       Note=Synthesized in the inner segment (IS) of rod photoreceptor cells
CC       before vectorial transport to disk membranes in the rod outer segment
CC       (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.
CC   -!- PTM: Contains one covalently linked retinal chromophore.
CC       {ECO:0000250|UniProtKB:P02699}.
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; L42954; AAA96438.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90305; -.
DR   SMR; Q90305; -.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR   GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR   GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR027430; Retinal_BS.
DR   InterPro; IPR000732; Rhodopsin.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   3: Inferred from homology;
KW   Cell projection; Chromophore; 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..>131
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197662"
FT   TOPO_DOM        <1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        17..38
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        39..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        67..88
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        89..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        101..122
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        123..>131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   MOD_RES         110
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         131
SQ   SEQUENCE   131 AA;  15037 MW;  8D2C88554897F462 CRC64;
     CGIDYYTRAP GYNNESFVIY MFIVHFLIPL FIISFCYGNL LCAVKAAAAA QEESETTQRA
     EREVTRMVIM MVISYLVSWV PYASVAWYIF SNQGSEFGPV FMTIPAFFAK SSALYNPLIY
     VLMNKQFRHC M