OPSD_TURTR
ID OPSD_TURTR Reviewed; 348 AA.
AC O62798;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9471225; DOI=10.1021/bi972500j;
RA Fasick J.I., Robsinson P.R.;
RT "Mechanism of spectral tuning in the dolphin visual pigments.";
RL Biochemistry 37:433-438(1998).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF 50-67.
RX PubMed=14985753; DOI=10.1038/nature02342;
RA Halic M., Becker T., Pool M.R., Spahn C.M.T., Grassucci R.A., Frank J.,
RA Beckmann R.;
RT "Structure of the signal recognition particle interacting with the
RT elongation-arrested ribosome.";
RL Nature 427:808-814(2004).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Light-induced isomerization of 11-cis to all-trans retinal
CC triggers a conformational change that activates signaling via G-
CC proteins. Signaling mediates the activation of phospholipase C (By
CC similarity). Subsequent receptor phosphorylation mediates displacement
CC of the bound G-protein alpha subunit by arrestin and terminates
CC signaling (By similarity). {ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P31356}.
CC -!- SUBUNIT: Homodimer. May form a complex composed of RHO, GRK1 and RCVRN
CC in a Ca(2+)-dependent manner; RCVRN prevents the interaction between
CC GRK1 and RHO (By similarity). Interacts with GRK1 (By similarity).
CC Interacts (phosphorylated form) with SAG (By similarity). Interacts
CC with GNAT1 (By similarity). Interacts with GNAT3. SAG and G-proteins
CC compete for a common binding site (By similarity). Interacts with PRCD;
CC the interaction promotes PRCD stability (By similarity).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P15409}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P31356}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P31356}. Note=Detected on
CC the rhabdomere membrane in the photoreceptor outer segment.
CC {ECO:0000250|UniProtKB:P31356}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal (By similarity). After hydrolysis of the Schiff base and
CC release of the covalently bound all-trans-retinal, active rhodopsin is
CC regenerated by binding of a fresh molecule of 11-cis-retinal (By
CC similarity). {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P31356}.
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; AF055456; AAC12940.1; -; mRNA.
DR RefSeq; NP_001267588.1; NM_001280659.1.
DR PDB; 1RY1; EM; 12.00 A; S=50-67.
DR PDB; 2J28; EM; 8.00 A; 7=50-67.
DR PDBsum; 1RY1; -.
DR PDBsum; 2J28; -.
DR AlphaFoldDB; O62798; -.
DR SMR; O62798; -.
DR STRING; 9739.XP_004325882.1; -.
DR GeneID; 101320374; -.
DR CTD; 6010; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR EvolutionaryTrace; O62798; -.
DR Proteomes; UP000245320; Chromosome 10.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
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 3D-structure; Acetylation; Chromophore; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197726"
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:P31356"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 100..111
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P31356"
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:P31356"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 228..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 307..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 343
FT /note="Phosphoserine"
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:0000250|UniProtKB:P02699"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 348 AA; 39093 MW; 32605DE5ED94723A CRC64;
MNGTEGLNFY VPFSNKTGVV RSPFEYPQYY LAEPWQFSVL AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VANLFMVFGG FTTTLYTSLH AYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGLALT WIMAMACAAA PLVGWSRYIP
EGMQCSCGID YYTSRQEVNN ESFVIYMFVV HFTIPLVIIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVVA FLICWVPYAS VAFYIFTHQG SDFGPIFMTI PSFFAKSSSI
YNPVIYIMMN KQFRNCMLTT LCCGRNPLGD DEASTTASKT ETSQVAPA
