ID   OPSD_PROSE              Reviewed;         301 AA.
AC   O18486;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Rhodopsin;
DE   Flags: Fragment;
GN   Name=RHO;
OS   Procambarus seminolae (Crayfish).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Cambaridae; Procambarus.
OX   NCBI_TaxID=61505;
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).
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; AF005388; AAB63379.1; -; Genomic_DNA.
DR   AlphaFoldDB; O18486; -.
DR   SMR; O18486; -.
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_0000197746"
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;  34585 MW;  B68EDA41E8168B99 CRC64;
     LHMIHLHWYQ YPPMNPMMYP LLLIFMLFTG ILCLAGNFVT IWVFMNTKSL RTPANLLVVN
     LAMSDFLMMF TMFPPMMVTC YYHTWTLGPT FCQVYAFLGN LCGCASIWTM VFITFDRYNV
     IVKGVAGEPL STKKASLWIL TIWVLSTTWC IAPFFGWNHY VPEGNLTGCG TDYLSEDILS
     RSYLYVYSTW VYFLPLAITI YCYVFIIKAV AAHEKGMRDQ AKKMGIKSLR NEEAQKTSAE
     CRLAKIAMTT VALWFIAWTP CLLINWVGMF ARSYLSPVYT IWGYVFAKAN AVYNPIVYAI
     S