OPSD_CAMSC
ID OPSD_CAMSC Reviewed; 301 AA.
AC O16018;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Rhodopsin;
DE Flags: Fragment;
GN Name=RHO;
OS Cambarellus shufeldtii (Cajun dwarf crayfish).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Cambaridae; Cambarellus; Dirigicambarus.
OX NCBI_TaxID=60963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9192889; DOI=10.1038/42628;
RA Crandall K.A., Hillis D.M.;
RT "Rhodopsin evolution in the dark.";
RL Nature 387:667-668(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9342400; DOI=10.1007/pl00006257;
RA Crandall K.A., Cronin T.W.;
RT "The molecular evolution of visual pigments of freshwater crayfishes
RT (Decapoda: Cambaridae).";
RL J. Mol. Evol. 45:524-534(1997).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Can use both retinal and 3-dehydroretinal as visual pigment.
CC Light-induced isomerization of 11-cis to all-trans retinal triggers a
CC conformational change that activates signaling via G-proteins.
CC Signaling via GNAQ probably mediates the activation of phospholipase C.
CC {ECO:0000250|UniProtKB:P35356}.
CC -!- SUBUNIT: Homodimer. Interacts with GNAQ.
CC {ECO:0000250|UniProtKB:P35356}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P35356}; 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:P35356}.
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; AF003544; AAB97666.1; -; Genomic_DNA.
DR AlphaFoldDB; O16018; -.
DR SMR; O16018; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
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; IPR001391; Opsin_lateye.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00578; OPSINLTRLEYE.
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 Chromophore; Disulfide bond; 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..>301
FT /note="Rhodopsin"
FT /id="PRO_0000197740"
FT TOPO_DOM <1..18
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 44..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 79..92
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 116..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 156..182
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..204
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 205..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 268..278
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOTIF 116..118
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 288
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 301
SQ SEQUENCE 301 AA; 34654 MW; 627A27C2ECEBFDF2 CRC64;
LHMIHLHWYQ YPPMNPMMYP LLLIFMFITG IPCLAGNFVT IWVFMTTKSL RSPANLLVVN
LAMSDFLMMF TMFPPMMITC YYHTWTLGPT FCQVYAFLGN LFGCTSIWTM VFITFDRYNV
IVKGVAGEPL SNKKAALWIL SAWVLSFSWC SAPFFGWNRY VPEGNLTGCG TDYLSEDALS
RSYLYVYSVW VYFLPLLITI YCYVFIIKAV AAHEKGMRDQ AKKMGIKSLR NEEAQKTSAE
CRLAKIAMTT VALWFIAWTP YLLINWVGMF ARSYLSPVYT IWGYVFAKAN AVYNPIVYAI
S
