OPSD_ENTDO
ID OPSD_ENTDO Reviewed; 455 AA.
AC P09241;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Enteroctopus.
OX NCBI_TaxID=267067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3366250; DOI=10.1016/0014-5793(88)80388-0;
RA Ovchinnikov Y.A., Abdulaev N.G., Zolotarev A.S., Artamonov I.D.,
RA Bespalov I.A., Dergachev A.E., Tsuda M.;
RT "Octopus rhodopsin. Amino acid sequence deduced from cDNA.";
RL FEBS Lett. 232:69-72(1988).
RN [2]
RP SEQUENCE REVISION TO 399.
RA Abdulaev N.G.;
RL Submitted (OCT-1988) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; X07797; CAA30644.1; -; mRNA.
DR PIR; S00610; OOOCG.
DR AlphaFoldDB; P09241; -.
DR SMR; P09241; -.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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:0016918; F:retinal binding; ISS:UniProtKB.
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; IPR027430; Retinal_BS.
DR InterPro; IPR006031; XYPPX.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF02162; XYPPX; 4.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
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 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Repeat; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..455
FT /note="Rhodopsin"
FT /id="PRO_0000197734"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 60..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 99..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 133..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..200
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 226..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 285..294
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 317..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 395..399
FT /note="1-1"
FT REPEAT 400..404
FT /note="1-2"
FT REPEAT 412..416
FT /note="2-1"
FT REPEAT 417..421
FT /note="2-2"
FT REPEAT 422..426
FT /note="3-1"
FT REPEAT 427..431
FT /note="3-2"
FT REGION 378..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..431
FT /note="6 X 5 AA repeats of G-Y-P-P-Q"
FT MOTIF 133..135
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT COMPBIAS 386..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 337
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 338
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 455 AA; 50489 MW; AECF4FC30ED1346C CRC64;
MVESTTLVNQ TWWYNPTVDI HPHWAKFDPI PDAVYYSVGI FIGVVGIIGI LGNGVVIYLF
SKTKSLQTPA NMFIINLAMS DLSFSAINGF PLKTISAFMK KWIFGKVACQ LYGLLGGIFG
FMSINTMAMI SIDRYNVIGR PMAASKKMSH RRAFLMIIFV WMWSIVWSVG PVFNWGAYVP
EGILTSCSFD YLSTDPSTRS FILCMYFCGF MLPIIIIAFC YFNIVMSVSN HEKEMAAMAK
RLNAKELRKA QAGASAEMKL AKISMVIITQ FMLSWSPYAI IALLAQFGPA EWVTPYAAEL
PVLFAKASAI HNPIVYSVSH PKFREAIQTT FPWLLTCCQF DEKECEDAND AEEEVVASER
GGESRDAAQM KEMMAMMQKM QAQQAAYQPP PPPQGYPPQG YPPQGAYPPP QGYPPQGYPP
QGYPPQGYPP QGAPPQVEAP QGAPPQGVDN QAYQA
