OPRK_HUMAN
ID OPRK_HUMAN Reviewed; 380 AA.
AC P41145; E5RHC9; Q499G4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Kappa-type opioid receptor;
DE Short=K-OR-1;
DE Short=KOR-1;
GN Name=OPRK1; Synonyms=OPRK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8060324; DOI=10.1006/bbrc.1994.2091;
RA Mansson E., Bare L.A., Yang D.;
RT "Isolation of a human kappa opioid receptor cDNA from placenta.";
RL Biochem. Biophys. Res. Commun. 202:1431-1437(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=7624359; DOI=10.1073/pnas.92.15.7006;
RA Simonin F., Gaveriaus-Ruff C., Befort K., Lannes B., Micheletti G.,
RA Mattei M.-G., Charon G., Bloch B., Kieffer B.;
RT "Kappa-opioid receptor in humans: cDNA and genomic cloning, chromosomal
RT assignment, functional expression, pharmacology, and expression pattern in
RT the central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7006-7010(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7869844; DOI=10.1016/0024-3205(94)00507-o;
RA Zhu J., Chen C., Xue J.-C., Kunapuli S., Deriel J.K., Liu-Chen L.-Y.;
RT "Cloning of a human kappa opioid receptor from the brain.";
RL Life Sci. 56:PL201-PL207(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-279 (ISOFORMS 1/2).
RC TISSUE=Brain;
RX PubMed=7929306; DOI=10.1016/s0021-9258(18)47144-x;
RA Wang J.B., Johnson P.S., Wu J.M., Wang W.F., Uhl G.R.;
RT "Human kappa opiate receptor second extracellular loop elevates dynorphin's
RT affinity for human mu/kappa chimeras.";
RL J. Biol. Chem. 269:25966-25969(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-203 (ISOFORMS 1/2).
RA Grandy D.K.;
RT "Mapping of the human kappa opioid receptor gene to chromosome 8q11.2-q12:
RT no evidence for multiple kappa opioid receptor genes.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP INTERACTION WITH SLC9A3R1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12004055; DOI=10.1074/jbc.m200058200;
RA Li J.-G., Chen C., Liu-Chen L.-Y.;
RT "Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory
RT factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human
RT kappa opioid receptor by enhancing its recycling rate.";
RL J. Biol. Chem. 277:27545-27552(2002).
RN [11]
RP INTERACTION WITH GABARAPL1.
RX PubMed=16431922; DOI=10.1074/jbc.m509805200;
RA Chen C., Li J.-G., Chen Y., Huang P., Wang Y., Liu-Chen L.-Y.;
RT "GEC1 interacts with the kappa opioid receptor and enhances expression of
RT the receptor.";
RL J. Biol. Chem. 281:7983-7993(2006).
RN [12]
RP GLYCOSYLATION AT ASN-25 AND ASN-39.
RX PubMed=17711303; DOI=10.1021/bi700443j;
RA Li J.G., Chen C., Liu-Chen L.Y.;
RT "N-glycosylation of the human kappa opioid receptor enhances its stability
RT but slows its trafficking along the biosynthesis pathway.";
RL Biochemistry 46:10960-10970(2007).
RN [13]
RP REVIEW.
RX PubMed=20729876; DOI=10.1038/aps.2010.138;
RA Wang Y.H., Sun J.F., Tao Y.M., Chi Z.Q., Liu J.G.;
RT "The role of kappa-opioid receptor activation in mediating antinociception
RT and addiction.";
RL Acta Pharmacol. Sin. 31:1065-1070(2010).
RN [14]
RP REVIEW.
RX PubMed=20401607; DOI=10.1007/s00213-010-1806-y;
RA Bruchas M.R., Chavkin C.;
RT "Kinase cascades and ligand-directed signaling at the kappa opioid
RT receptor.";
RL Psychopharmacology 210:137-147(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 43-358 IN COMPLEX WITH ANTAGONIST,
RP FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX PubMed=22437504; DOI=10.1038/nature10939;
RA Wu H., Wacker D., Mileni M., Katritch V., Han G.W., Vardy E., Liu W.,
RA Thompson A.A., Huang X.P., Carroll F.I., Mascarella S.W., Westkaemper R.B.,
RA Mosier P.D., Roth B.L., Cherezov V., Stevens R.C.;
RT "Structure of the human kappa-opioid receptor in complex with JDTic.";
RL Nature 485:327-332(2012).
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:12004055,
CC ECO:0000269|PubMed:22437504, ECO:0000269|PubMed:7624359,
CC ECO:0000269|PubMed:8060324}.
CC -!- SUBUNIT: Interacts with SLC9A3R1. Interacts with GABARAPL1.
CC {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:16431922,
CC ECO:0000269|PubMed:22437504}.
CC -!- INTERACTION:
CC P41145; P35414: APLNR; NbExp=3; IntAct=EBI-925028, EBI-2875891;
CC P41145; Q9H0R8: GABARAPL1; NbExp=5; IntAct=EBI-925028, EBI-746969;
CC P41145; Q16617: NKG7; NbExp=3; IntAct=EBI-925028, EBI-3919611;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12004055,
CC ECO:0000269|PubMed:22437504, ECO:0000269|PubMed:7624359,
CC ECO:0000269|PubMed:8060324}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:22437504,
CC ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41145-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41145-2; Sequence=VSP_055313;
CC -!- TISSUE SPECIFICITY: Detected in brain and placenta.
CC {ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Kappa opioid receptor entry;
CC URL="https://en.wikipedia.org/wiki/Kappa_opioid_receptor";
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DR EMBL; U11053; AAA20985.1; -; mRNA.
DR EMBL; U17298; AAC50158.1; -; mRNA.
DR EMBL; L37362; AAA63906.1; -; mRNA.
DR EMBL; AF498922; AAM21070.1; -; mRNA.
DR EMBL; AK310233; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC009646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099912; AAH99912.1; -; mRNA.
DR EMBL; L36130; AAA63646.1; -; mRNA.
DR EMBL; U16860; AAA56758.1; -; Genomic_DNA.
DR CCDS; CCDS6152.1; -. [P41145-1]
DR CCDS; CCDS64895.1; -. [P41145-2]
DR PIR; JC2338; JC2338.
DR RefSeq; NP_000903.2; NM_000912.4. [P41145-1]
DR RefSeq; NP_001269833.1; NM_001282904.1. [P41145-2]
DR RefSeq; NP_001305426.1; NM_001318497.1.
DR PDB; 4DJH; X-ray; 2.90 A; A/B=43-358.
DR PDB; 6B73; X-ray; 3.10 A; A/B=54-358.
DR PDB; 6VI4; X-ray; 3.30 A; A/B=54-358.
DR PDB; 7T10; EM; 2.50 A; R=256-270.
DR PDB; 7T11; EM; 2.70 A; R=256-270.
DR PDBsum; 4DJH; -.
DR PDBsum; 6B73; -.
DR PDBsum; 6VI4; -.
DR PDBsum; 7T10; -.
DR PDBsum; 7T11; -.
DR AlphaFoldDB; P41145; -.
DR SMR; P41145; -.
DR BioGRID; 111031; 11.
DR IntAct; P41145; 11.
DR MINT; P41145; -.
DR STRING; 9606.ENSP00000265572; -.
DR BindingDB; P41145; -.
DR ChEMBL; CHEMBL237; -.
DR DrugBank; DB01571; 3-Methylfentanyl.
DR DrugBank; DB01439; 3-Methylthiofentanyl.
DR DrugBank; DB05443; ADL 10-0101.
DR DrugBank; DB06274; Alvimopan.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB05104; Asimadoline.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB00921; Buprenorphine.
DR DrugBank; DB00611; Butorphanol.
DR DrugBank; DB09173; Butyrfentanyl.
DR DrugBank; DB01535; Carfentanil.
DR DrugBank; DB00318; Codeine.
DR DrugBank; DB05155; CR665.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00647; Dextropropoxyphene.
DR DrugBank; DB01209; Dezocine.
DR DrugBank; DB01452; Diamorphine.
DR DrugBank; DB11938; Difelikefalin.
DR DrugBank; DB01565; Dihydromorphine.
DR DrugBank; DB01548; Diprenorphine.
DR DrugBank; DB09272; Eluxadoline.
DR DrugBank; DB01497; Etorphine.
DR DrugBank; DB00813; Fentanyl.
DR DrugBank; DB00327; Hydromorphone.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB06738; Ketobemidone.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00825; Levomenthol.
DR DrugBank; DB00854; Levorphanol.
DR DrugBank; DB00836; Loperamide.
DR DrugBank; DB14146; Loxicodegol.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB06800; Methylnaltrexone.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB00370; Mirtazapine.
DR DrugBank; DB00295; Morphine.
DR DrugBank; DB06409; Morphine glucuronide.
DR DrugBank; DB00844; Nalbuphine.
DR DrugBank; DB11691; Naldemedine.
DR DrugBank; DB06230; Nalmefene.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB00704; Naltrexone.
DR DrugBank; DB11130; Opium.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB00652; Pentazocine.
DR DrugBank; DB11186; Pentoxyverine.
DR DrugBank; DB09209; Pholcodine.
DR DrugBank; DB00396; Progesterone.
DR DrugBank; DB00899; Remifentanil.
DR DrugBank; DB12543; Samidorphan.
DR DrugBank; DB00708; Sufentanil.
DR DrugBank; DB06204; Tapentadol.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB05046; V1003.
DR DrugCentral; P41145; -.
DR GuidetoPHARMACOLOGY; 318; -.
DR TCDB; 9.A.14.13.32; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P41145; 2 sites.
DR iPTMnet; P41145; -.
DR PhosphoSitePlus; P41145; -.
DR BioMuta; OPRK1; -.
DR DMDM; 116242691; -.
DR MassIVE; P41145; -.
DR PaxDb; P41145; -.
DR PeptideAtlas; P41145; -.
DR PRIDE; P41145; -.
DR ProteomicsDB; 15940; -.
DR ProteomicsDB; 55403; -. [P41145-1]
DR ABCD; P41145; 1 sequenced antibody.
DR Antibodypedia; 11640; 397 antibodies from 38 providers.
DR DNASU; 4986; -.
DR Ensembl; ENST00000265572.8; ENSP00000265572.3; ENSG00000082556.14. [P41145-1]
DR Ensembl; ENST00000520287.5; ENSP00000429706.1; ENSG00000082556.14. [P41145-1]
DR Ensembl; ENST00000524278.5; ENSP00000430923.1; ENSG00000082556.14. [P41145-2]
DR GeneID; 4986; -.
DR KEGG; hsa:4986; -.
DR MANE-Select; ENST00000265572.8; ENSP00000265572.3; NM_000912.5; NP_000903.2.
DR UCSC; uc003xrh.2; human. [P41145-1]
DR CTD; 4986; -.
DR DisGeNET; 4986; -.
DR GeneCards; OPRK1; -.
DR HGNC; HGNC:8154; OPRK1.
DR HPA; ENSG00000082556; Tissue enriched (brain).
DR MIM; 165196; gene.
DR neXtProt; NX_P41145; -.
DR OpenTargets; ENSG00000082556; -.
DR PharmGKB; PA31943; -.
DR VEuPathDB; HostDB:ENSG00000082556; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157341; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P41145; -.
DR OMA; FPFKMRM; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P41145; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P41145; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR SignaLink; P41145; -.
DR SIGNOR; P41145; -.
DR BioGRID-ORCS; 4986; 10 hits in 1070 CRISPR screens.
DR GeneWiki; %CE%9A-opioid_receptor; -.
DR GenomeRNAi; 4986; -.
DR Pharos; P41145; Tclin.
DR PRO; PR:P41145; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P41145; protein.
DR Bgee; ENSG00000082556; Expressed in endothelial cell and 72 other tissues.
DR ExpressionAtlas; P41145; baseline and differential.
DR Genevisible; P41145; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0038048; F:dynorphin receptor activity; IDA:UniProtKB.
DR GO; GO:0004985; F:G protein-coupled opioid receptor activity; IDA: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; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:1990708; P:conditioned place preference; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IEA:Ensembl.
DR GO; GO:1904000; P:positive regulation of eating behavior; IEA:Ensembl.
DR GO; GO:0040017; P:positive regulation of locomotion; IEA:Ensembl.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0046877; P:regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:1903937; P:response to acrylamide; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050951; P:sensory perception of temperature stimulus; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Behavior; Cell membrane;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..380
FT /note="Kappa-type opioid receptor"
FT /id="PRO_0000069967"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT TRANSMEM 58..85
FT /note="Helical; Name=1"
FT TOPO_DOM 86..95
FT /note="Cytoplasmic"
FT TRANSMEM 96..119
FT /note="Helical; Name=2"
FT TOPO_DOM 120..132
FT /note="Extracellular"
FT TRANSMEM 133..154
FT /note="Helical; Name=3"
FT TOPO_DOM 155..173
FT /note="Cytoplasmic"
FT TRANSMEM 174..196
FT /note="Helical; Name=4"
FT TOPO_DOM 197..222
FT /note="Extracellular"
FT TRANSMEM 223..247
FT /note="Helical; Name=5"
FT TOPO_DOM 248..274
FT /note="Cytoplasmic"
FT TRANSMEM 275..296
FT /note="Helical; Name=6"
FT TOPO_DOM 297..311
FT /note="Extracellular"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT TOPO_DOM 334..380
FT /note="Cytoplasmic"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17711303"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17711303"
FT DISULFID 131..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:22437504"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055313"
FT VARIANT 374
FT /note="D -> N (in dbSNP:rs9282808)"
FT /id="VAR_028067"
FT CONFLICT 2
FT /note="D -> E (in Ref. 1; AAA20985 and 4; AAM21070)"
FT /evidence="ECO:0000305"
FT HELIX 57..86
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 127..159
FT /evidence="ECO:0007829|PDB:4DJH"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:4DJH"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 170..196
FT /evidence="ECO:0007829|PDB:4DJH"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4DJH"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:4DJH"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4DJH"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 236..259
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 267..299
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 309..333
FT /evidence="ECO:0007829|PDB:4DJH"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:4DJH"
SQ SEQUENCE 380 AA; 42645 MW; 3DA6E9F90FB48825 CRC64;
MDSPIQIFRG EPGPTCAPSA CLPPNSSAWF PGWAEPDSNG SAGSEDAQLE PAHISPAIPV
IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN LALADALVTT TMPFQSTVYL
MNSWPFGDVL CKIVISIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPLKAKIINI
CIWLLSSSVG ISAIVLGGTK VREDVDVIEC SLQFPDDDYS WWDLFMKICV FIFAFVIPVL
IIIVCYTLMI LRLKSVRLLS GSREKDRNLR RITRLVLVVV AVFVVCWTPI HIFILVEALG
STSHSTAALS SYYFCIALGY TNSSLNPILY AFLDENFKRC FRDFCFPLKM RMERQSTSRV
RNTVQDPAYL RDIDGMNKPV
