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   27-MAR-2024, entry version 166.
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 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:0000269|PubMed:20358363, ECO:0000269|PubMed:8240267}.
CC   -!- SUBUNIT: Interacts with NHERF1. 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}.
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; 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   GlyCosmos; P34975; 2 sites, No reported glycans.
DR   GlyGen; P34975; 2 sites.
DR   iPTMnet; P34975; -.
DR   PhosphoSitePlus; P34975; -.
DR   PaxDb; 10116-ENSRNOP00000010255; -.
DR   Ensembl; ENSRNOT00000010254.4; ENSRNOP00000010255.1; ENSRNOG00000007647.4.
DR   Ensembl; ENSRNOT00055029914; ENSRNOP00055024030; ENSRNOG00055017680.
DR   Ensembl; ENSRNOT00060016244; ENSRNOP00060012690; ENSRNOG00060009622.
DR   Ensembl; ENSRNOT00065030660; ENSRNOP00065024397; ENSRNOG00065018294.
DR   GeneID; 29335; -.
DR   KEGG; rno:29335; -.
DR   UCSC; RGD:69426; rat.
DR   AGR; RGD:69426; -.
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; QDPTYMR; -.
DR   OrthoDB; 5393360at2759; -.
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 cell types or tissues.
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:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
DR   GO; GO:0030315; C:T-tubule; 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:0042923; F:neuropeptide 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: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: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:0035094; P:response to nicotine; 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   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.
DR   Genevisible; P34975; RN.
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
//