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OPSD_ZOSOP
ID   OPSD_ZOSOP              Reviewed;         352 AA.
AC   Q9YGY9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Rhodopsin;
GN   Name=rho;
OS   Zosterisessor ophiocephalus (Grass goby) (Gobius ophiocephalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Gobiinae; Zosterisessor.
OX   NCBI_TaxID=85428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Archer S.N., Hirano J.;
RT   "Comparative analysis of opsins in Mediterranian coastal fish.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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; Y18678; CAA77260.1; -; mRNA.
DR   AlphaFoldDB; Q9YGY9; -.
DR   SMR; Q9YGY9; -.
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; 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   2: Evidence at transcript level;
KW   Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW   Transducer; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..352
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197729"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        37..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        62..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        74..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        97..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        111..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        134..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        153..173
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        174..202
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        203..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        225..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        275..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        287..308
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        309..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          331..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           134..136
FT                   /note="'Ionic lock' involved in activated form
FT                   stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   COMPBIAS        337..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            113
FT                   /note="Plays an important role in the conformation switch
FT                   to the active conformation"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   MOD_RES         296
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   LIPID           322
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   LIPID           323
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
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   352 AA;  39363 MW;  1FC7D21597E62960 CRC64;
     MNGTEGPFFY IPMVNTTGIV RSPYEYPQYY LVNPAAYACL GAYMFFLILV GFPVNFLTLY
     VTLEHKKLRT PLNYILLNLA VADLFMVFGG FTTTMYTSMH GYFVLGRLGC NIEGFFATLG
     GEIALWSLVV LAIERWVVVC KPISNFRFGE NHAIMGVAFT WFMASACAVP PLVGWSRYIP
     EGMQCSCGVD YYTRAEGFNN ESFVIYMFIV HFCIPLAVVG FCYGRLLCAV KEAAAAQQES
     ETTQRAEREV SRMVVIMVIG FLVCWLPYAS VAWYIFTHQG SEFGPPFMTV PAFFAKSSSI
     YNPMIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTKTE ASSVSSSSVS PA
 
 
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