OPSD_TETNG
ID OPSD_TETNG Reviewed; 353 AA.
AC Q9DGG4; Q4RJW7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Rhodopsin;
GN Name=rho; Synonyms=rhod; ORFNames=GSTENG00033246001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fischer C.;
RT "Tetraodon nigroviridis gene for rhodopsin.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG11315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ293018; CAC04526.1; -; Genomic_DNA.
DR EMBL; CAAE01015033; CAG11315.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q9DGG4; -.
DR SMR; Q9DGG4; -.
DR STRING; 99883.ENSTNIP00000021070; -.
DR Ensembl; ENSTNIT00000021303; ENSTNIP00000021070; ENSTNIG00000017909.
DR KEGG; tng:GSTEN00033246G001; -.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; Q9DGG4; -.
DR OMA; QYYLVNP; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..353
FT /note="Rhodopsin"
FT /id="PRO_0000197724"
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..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 330..353
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..353
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 353 AA; 39538 MW; EA2B5484C2720232 CRC64;
MNGTEGPFFY VPMLNTTGIV RSPYDYPQYY LVNPAAYAAL GAYMFLLILL GFPINFLTLY
VTIEHKKLRT PLNYILLNLA VANLFMVFGG FTTTMYTSMH GYFVLGRLGC NLEGFFATLG
GEIGLWSLVV LAIERWMVVC KPISNFRFGE NHAIMGLAFT WIMACACAVP PLVGWSRYIP
EGMQCSCGVD YYTRAEGFNN ESFVVYMFIC HFLIPMAVVF FCYGRLLCAV KEAAAAQQES
ETTQRAEREV TRMVVIMVVA FLICWLPYAG VAWWIFTHQG SEFGPVFMTI PAFFAKSSSI
YNPLIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTSKT EASSVSSSSV SPA
