ID   OPSD_SARPI              Reviewed;         351 AA.
AC   Q9YGZ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Rhodopsin;
GN   Name=rho;
OS   Sardina pilchardus (European pilchard) (Clupea pilchardus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC   Clupeidae; Sardina.
OX   NCBI_TaxID=27697;
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; Y18677; CAA77259.1; -; mRNA.
DR   AlphaFoldDB; Q9YGZ0; -.
DR   SMR; Q9YGZ0; -.
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..351
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197712"
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..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          330..351
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        331..351
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   351 AA;  39425 MW;  AACD5D0E3924ADE3 CRC64;
     MNGTEGPFFY IPMSNATGLV RSPYDYPQYY LVPPWGYACL AAYMFLLILT GFPVNFLTLY
     VTIEHKKLRS PLNYILLNLA VADLFMVIGG FTTTMWTSLN GYFVFGRMGC NIEGFFATLG
     GEIALWSLVV LSMERWIVVC KPISNFRFGE NHAVMGVAFS WFMAAACAVP PLVGWSRYIP
     EGMQCSCGID YYTRAEGFNN ESFVIYMFVV HFTCPLTIIT FCYGRLVCTV KEAAAQQQES
     ETTQRAEREV TRMVIIMFVA FLACWVPYAS VAWYIFTHQG SEFGPVFMTI PAFFAKSSAV
     YNPVIYICLN KQFRHCMITT LCCGKNPFEE EEGSTTASKT EASSVCSVSP A