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 27-MAR-2024, entry version 97. 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; Myopsida; 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: Cell projection, rhabdomere membrane CC {ECO:0000250|UniProtKB:P31356}; Multi-pass membrane protein 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49108; CAA88923.1; -; Genomic_DNA. DR PIR; S60755; S60755. DR AlphaFoldDB; Q17094; -. DR SMR; Q17094; -. DR GlyCosmos; Q17094; 1 site, No reported glycans. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0016020; C: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 CDD; cd15337; 7tmA_Opsin_Gq_invertebrates; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. 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 PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF85; OPSIN RH1-RELATED; 1. DR Pfam; PF00001; 7tm_1; 1. DR Pfam; PF02162; XYPPX; 3. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00239; RHODOPSNTAIL. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 Cell membrane; Cell projection; Chromophore; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix; KW 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 //