OPRK_RAT
ID OPRK_RAT Reviewed; 380 AA.
AC P34975;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Kappa-type opioid receptor;
DE Short=K-OR-1;
DE Short=KOR-1;
GN Name=Oprk1; Synonyms=Ror-d;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=8240267; DOI=10.1042/bj2950625;
RA Chen Y., Mestek A., Liu J., Yu L.;
RT "Molecular cloning of a rat kappa opioid receptor reveals sequence
RT similarities to the mu and delta opioid receptors.";
RL Biochem. J. 295:625-628(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8103466; DOI=10.1016/0014-5793(93)80240-u;
RA Minami M., Toya T., Katao Y., Maekawa K., Nakamura S., Onogi T., Kaneko S.,
RA Satoh M.;
RT "Cloning and expression of a cDNA for the rat kappa-opioid receptor.";
RL FEBS Lett. 329:291-295(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8240268; DOI=10.1042/bj2950629;
RA Li S., Zhu J., Chen C., Chen Y.-W., Deriel J.K., Ashby B., Liu-Chen L.-Y.;
RT "Molecular cloning and expression of a rat kappa opioid receptor.";
RL Biochem. J. 295:629-633(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8234341; DOI=10.1073/pnas.90.21.9954;
RA Meng F., Xie G.-X., Thompson R.C., Mansour A., Goldstein A., Watson S.J.,
RA Akil H.;
RT "Cloning and pharmacological characterization of a rat kappa opioid
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9954-9958(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8396539; DOI=10.1016/0014-5793(93)80923-i;
RA Nishi M., Takeshima H., Fukuda K., Kato S., Mori K.;
RT "cDNA cloning and pharmacological characterization of an opioid receptor
RT with high affinities for kappa-subtype-selective ligands.";
RL FEBS Lett. 330:77-80(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7896774; DOI=10.1074/jbc.270.12.6421;
RA Yakovlev A.G., Krueger K.E., Faden A.I.;
RT "Structure and expression of a rat kappa opioid receptor gene.";
RL J. Biol. Chem. 270:6421-6424(1995).
RN [7]
RP FUNCTION.
RX PubMed=20358363; DOI=10.1007/s00213-010-1834-7;
RA Nemeth C.L., Paine T.A., Rittiner J.E., Beguin C., Carroll F.I., Roth B.L.,
RA Cohen B.M., Carlezon W.A. Jr.;
RT "Role of kappa-opioid receptors in the effects of salvinorin A and ketamine
RT on attention in rats.";
RL Psychopharmacology 210:263-274(2010).
CC -!- FUNCTION: G-protein coupled opioid receptor that functions as receptor
CC for endogenous alpha-neoendorphins and dynorphins, but has low affinity
CC for beta-endorphins. Also functions as receptor for various synthetic
CC opioids and for the psychoactive diterpene salvinorin A. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors, such as adenylate cyclase. Signaling leads to
CC the inhibition of adenylate cyclase activity. Inhibits neurotransmitter
CC release by reducing calcium ion currents and increasing potassium ion
CC conductance. Plays a role in the perception of pain. Plays a role in
CC mediating reduced physical activity upon treatment with synthetic
CC opioids. Plays a role in the regulation of salivation in response to
CC synthetic opioids. May play a role in arousal and regulation of
CC autonomic and neuroendocrine functions. {ECO:0000269|PubMed:20358363,
CC ECO:0000269|PubMed:8240267}.
CC -!- SUBUNIT: Interacts with SLC9A3R1. Interacts with GABARAPL1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8240267};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8240267}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L22001; AAA41495.1; -; mRNA.
DR EMBL; D16829; BAA04109.1; -; mRNA.
DR EMBL; L22536; AAA41496.1; -; mRNA.
DR EMBL; U00442; AAA18261.1; -; mRNA.
DR EMBL; D16534; BAA03971.1; -; mRNA.
DR EMBL; U17995; AAC53249.1; -; Genomic_DNA.
DR EMBL; U17993; AAC53249.1; JOINED; Genomic_DNA.
DR EMBL; U17994; AAC53249.1; JOINED; Genomic_DNA.
DR PIR; S36143; S36143.
DR RefSeq; NP_058863.1; NM_017167.3.
DR AlphaFoldDB; P34975; -.
DR SMR; P34975; -.
DR IntAct; P34975; 1.
DR STRING; 10116.ENSRNOP00000010255; -.
DR BindingDB; P34975; -.
DR ChEMBL; CHEMBL3614; -.
DR DrugCentral; P34975; -.
DR GuidetoPHARMACOLOGY; 318; -.
DR GlyGen; P34975; 2 sites.
DR iPTMnet; P34975; -.
DR PhosphoSitePlus; P34975; -.
DR PaxDb; P34975; -.
DR Ensembl; ENSRNOT00000010254; ENSRNOP00000010255; ENSRNOG00000007647.
DR GeneID; 29335; -.
DR KEGG; rno:29335; -.
DR UCSC; RGD:69426; rat.
DR CTD; 4986; -.
DR RGD; 69426; Oprk1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157341; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P34975; -.
DR OMA; FPFKMRM; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P34975; -.
DR TreeFam; TF315737; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P34975; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007647; Expressed in thymus and 3 other tissues.
DR Genevisible; P34975; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0038048; F:dynorphin receptor activity; ISS:UniProtKB.
DR GO; GO:0004985; F:G protein-coupled opioid receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:RGD.
DR GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:1990708; P:conditioned place preference; IMP:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0042711; P:maternal behavior; IDA:RGD.
DR GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; IMP:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IDA:RGD.
DR GO; GO:1904000; P:positive regulation of eating behavior; IMP:RGD.
DR GO; GO:0040017; P:positive regulation of locomotion; IDA:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0046877; P:regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:1903937; P:response to acrylamide; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IDA:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050951; P:sensory perception of temperature stimulus; IMP:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000452; Kappa_opi_rcpt.
DR InterPro; IPR001418; Opioid_rcpt.
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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..380
FT /note="Kappa-type opioid receptor"
FT /id="PRO_0000069969"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..85
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 86..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..132
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 133..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 155..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 197..222
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..247
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 248..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 275..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 297..311
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 334..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 131..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 42
FT /note="V -> L (in Ref. 2; BAA04109)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="C -> Y (in Ref. 3; AAA41496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42688 MW; 107FEEDB09886F92 CRC64;
MESPIQIFRG EPGPTCAPSA CLLPNSSSWF PNWAESDSNG SVGSEDQQLE PAHISPAIPV
IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN LALADALVTT TMPFQSAVYL
MNSWPFGDVL CKIVISIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPLKAKIINI
CIWLLASSVG ISAIVLGGTK VREDVDVIEC SLQFPDDEYS WWDLFMKICV FVFAFVIPVL
IIIVCYTLMI LRLKSVRLLS GSREKDRNLR RITKLVLVVV AVFIICWTPI HIFILVEALG
STSHSTAVLS SYYFCIALGY TNSSLNPVLY AFLDENFKRC FRDFCFPIKM RMERQSTNRV
RNTVQDPASM RDVGGMNKPV
