OPSD_ALLSU
ID OPSD_ALLSU Reviewed; 439 AA.
AC Q17094;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Rhodopsin;
DE Flags: Fragment;
GN Name=RHO;
OS Alloteuthis subulata (Squid) (Loligo subulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Alloteuthis.
OX NCBI_TaxID=54069;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Epidermis;
RX PubMed=8108455; DOI=10.1098/rspb.1993.0151;
RA Morris A., Bowmaker J.K., Hunt D.M.;
RT "The molecular basis of a spectral shift in the rhodopsins of two species
RT of squid from different photic environments.";
RL Proc. R. Soc. B 254:233-240(1993).
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; Z49108; CAA88923.1; -; Genomic_DNA.
DR PIR; S60755; S60755.
DR AlphaFoldDB; Q17094; -.
DR SMR; Q17094; -.
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; 3.
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 3: Inferred from homology;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN <1..>439
FT /note="Rhodopsin"
FT /id="PRO_0000197733"
FT TOPO_DOM <1..26
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 27..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 52..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 91..102
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 103..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 125..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 166..192
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 218..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 277..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 309..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 369..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 125..127
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT COMPBIAS 383..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 329
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 330
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 1
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 439
SQ SEQUENCE 439 AA; 49017 MW; B8167DFD8A00390E CRC64;
NETWWYNPYM DIHSHWKQFD QVPAAVYYSL GIFIAICGII GCAGNGIVIY LFTKTKSLQT
PANMFIINLA FSDFTFSLVN GFPMMTISCF LKHWVFGQAA CKVYGLIGGI FGLTSIMTMT
MISIDRYNVI RRPMSASKKM SHRKAFIMIV FVWIWSTIWA IGPIFGWGAY QLEGVLCNCS
FDYITRDAST RSNIVCMYIF AFMFPIVVIF FCYFNIVMSV SNHEKEMAAM AKRLNAKELR
KAQAGASAEM KLAKISIVIV TQSLLSWSPY AIVALLAQFG PIEWVTPYAA QLPVMFAKAS
AIHNPMIYSV SHPKFREAIA SNFPWILTCC QYDEKEIEDD KDAEAEIPAA EQSGGESVDA
AQMKEMMAMM QKMQAQQQQQ PAYPPQGYPP QGYPPPPPQG YPPQGYPPQG YPPQGYPPPP
QGPPPQGPPP QAAPPQGVD
