ID E9JM80_HYPNO Unreviewed; 288 AA.
AC E9JM80;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
GN Name=RH {ECO:0000313|EMBL:ADV57100.1};
OS Hypophthalmichthys nobilis (Bighead carp) (Aristichthys nobilis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Hypophthalmichthys.
OX NCBI_TaxID=7965 {ECO:0000313|EMBL:ADV57100.1};
RN [1] {ECO:0000313|EMBL:ADV57100.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20976012; DOI=10.1371/journal.pone.0013508;
RA Tao W., Zou M., Wang X., Gan X., Mayden R.L., He S.;
RT "Phylogenomic analysis resolves the formerly intractable adaptive
RT diversification of the endemic clade of east Asian Cyprinidae
RT (Cypriniformes).";
RL PLoS ONE 5:E13508-E13508(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000256|PIRSR:PIRSR600732-50}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000256|RuleBase:RU004951}.
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; GU218590; ADV57100.1; -; Genomic_DNA.
DR AlphaFoldDB; E9JM80; -.
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: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 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; IPR000732; Rhodopsin.
DR PANTHER; PTHR24240; OPSIN; 1.
DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
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 Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRSR:PIRSR600732-
KW 50};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600732-3};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU004951};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|RuleBase:RU004951};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951};
KW Retinal protein {ECO:0000256|ARBA:ARBA00022925,
KW ECO:0000256|PIRSR:PIRSR600732-50};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|RuleBase:RU004951};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004951};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004951};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW Zinc {ECO:0000256|PIRSR:PIRSR600732-1}.
FT TRANSMEM 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 31..283
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT SITE 90
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT MOD_RES 273
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT DISULFID 87..164
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADV57100.1"
FT NON_TER 288
FT /evidence="ECO:0000313|EMBL:ADV57100.1"
SQ SEQUENCE 288 AA; 32735 MW; 2BEC3BE2BBBA9BE6 CRC64;
YDYPQYYLVA PWAYGCLAAY MFFLILTGFP INFLTLYVTL EHKKLRTPLN YSLLNLAVAD
LFMVFGGFTT TMYTSLHGYF VFGRLGCNLE GFFATLGGEM ALWSIVTLAI ERWLVVCKPI
SNFRFGENHA IIGVIFTWVM ACSCAVPPLI GWSRYIPEGM QCSCGVDYYT RAEGYNNESF
VIYMFTVHAC IPFCVIFFCY GRLVCAVKDA AAQQQESETT QRAEREVTRM VILMGFAYLV
CWLPYACTAW YIFTHKGANF GPVLMTVPAF FAKTSAVYNP VIYICMNK
//
