ID G5C267_HETGA Unreviewed; 477 AA.
AC G5C267;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Kappa-type opioid receptor {ECO:0000256|ARBA:ARBA00021098};
GN ORFNames=GW7_03075 {ECO:0000313|EMBL:EHB15628.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15628.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15628.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: G-protein coupled opioid receptor that functions as a
CC receptor for endogenous alpha-neoendorphins and dynorphins, but has low
CC affinity for beta-endorphins. Also functions as a receptor for various
CC synthetic opioids and for the psychoactive diterpene salvinorin A.
CC Ligand binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase. Signaling
CC leads to the inhibition of adenylate cyclase activity. Inhibits
CC neurotransmitter release by reducing calcium ion currents and
CC increasing potassium ion conductance. Plays a role in the perception of
CC pain. Plays a role in mediating reduced physical activity upon
CC treatment with synthetic opioids. Plays a role in the regulation of
CC salivation in response to synthetic opioids. May play a role in arousal
CC and regulation of autonomic and neuroendocrine functions.
CC {ECO:0000256|ARBA:ARBA00043871}.
CC -!- SUBUNIT: Interacts with NHERF1. Interacts with GABARAPL1.
CC {ECO:0000256|ARBA:ARBA00034801}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; JH172959; EHB15628.1; -; Genomic_DNA.
DR STRING; 10181.G5C267; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; G5C267; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0038048; F:dynorphin receptor activity; IEA:InterPro.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR CDD; cd15091; 7tmA_Kappa_opioid_R; 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; IPR000452; Kappa_opi_rcpt.
DR InterPro; IPR001418; Opioid_rcpt.
DR PANTHER; PTHR24229:SF1; KAPPA-TYPE OPIOID RECEPTOR; 1.
DR PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00532; KAPPAOPIOIDR.
DR PRINTS; PR00384; OPIOIDR.
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.
PE 3: Inferred from homology;
KW Behavior {ECO:0000256|ARBA:ARBA00022610};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU000688};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..427
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 52829 MW; BBCF25DE4612D4F4 CRC64;
MRSGAWARAL EGRSGGGRAS GGRTSPAVSS GSPQPGCILG ASGSAEPPPV VGAAHGKQLG
SRRRQAEKEP WATLPGPGSK SQRREAGGAW QPRLSQTWNA RVNREPFACL QEAGVLPLPA
XXXXXXXXXX XXXXXXXXXX XXXEPLEPAH ISPAIPVIIT AVYSVVFVVG LVGNSLVMFV
IIRYTKMKTA TNIYIFNLAL ADALVTTTMP FQSTVYLMNS WPFGDVLCKI VISIDYYNMF
TSIFTLTMMS VDRYIAVCHP VKALDFRTPL KAKIINICIW LLSSSVGISA IVLGGTKVRE
DVDIIECSLQ FPDDDYSWWD LLMKICVFVF AFVIPVLIII VCYTLMILRL KSVRLLSGSR
EKDRNLRRIT RLVLVVVAVF IICWTPIHIF ILVEALGSTS HSTAALSSYY FCIALGYTNS
SLNPILYAFL DENFKRCFRD FCFPIKMRME RQSTSRVRNT VQDPAYMRDV DGMNKPV
//
