ID D2YZ12_9NEOB Unreviewed; 113 AA.
AC D2YZ12;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Rhodopsin {ECO:0000313|EMBL:BAI58310.1};
DE Flags: Fragment;
GN Name=rhod {ECO:0000313|EMBL:BAI58310.1};
OS Occidozyga sp. Kuala Lumpur.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Dicroglossidae; Occidozyginae;
OC Occidozyga.
OX NCBI_TaxID=622604 {ECO:0000313|EMBL:BAI58310.1};
RN [1] {ECO:0000313|EMBL:BAI58310.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20443685; DOI=10.2108/zsj.27.386;
RA Kotaki M., Kurabayashi A., Matsui M., Kuramoto M., Djong T.H., Sumida M.;
RT "Molecular phylogeny of the diversified frogs of genus Fejervarya (Anura:
RT Dicroglossidae).";
RL Zool. Sci. 27:386-395(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AB489043; BAI58310.1; -; Genomic_DNA.
DR AlphaFoldDB; D2YZ12; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProt.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 4.10.840.10; Rhodopsin, N-terminal domain; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR InterPro; IPR037114; Rhodopsin_N_sf.
DR PANTHER; PTHR24240; OPSIN; 1.
DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00579; RHODOPSIN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 4: Predicted;
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600732-
KW 4}; Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600732-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW Transducer {ECO:0000256|ARBA:ARBA00023040};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW Zinc {ECO:0000256|PIRSR:PIRSR600732-2}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..113
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT SITE 110
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAI58310.1"
FT NON_TER 113
FT /evidence="ECO:0000313|EMBL:BAI58310.1"
SQ SEQUENCE 113 AA; 13169 MW; E123D5F9B81E03D2 CRC64;
TEGPNFYVPM SNKTGVVRSP FEYPQYYLAE PWKYSVLAAY MFMLILLGLP INFMTLYVTI
QHKKLRTPLN YILLNLAFAN HFMILCGFTV TLYTSLHGYF VFGQNGCYFE GFF
//
