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 27-MAR-2024, entry version 209. 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 NHERF1, 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 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:12004055, ECO:0000269|PubMed:22437504, CC ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}. CC -!- SUBUNIT: Interacts with NHERF1. Interacts with GABARAPL1. CC {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:16431922, CC ECO:0000269|PubMed:22437504}. CC -!- INTERACTION: CC P41145; P35414: APLNR; NbExp=4; 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"; 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; 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 PDB; 7UL2; EM; 2.40 A; R=246-277. DR PDB; 7UL3; EM; 3.00 A; A=246-284. DR PDB; 7UL5; EM; 3.10 A; A=256-271. DR PDB; 7Y1F; EM; 3.30 A; R=54-358. DR PDB; 7YIT; X-ray; 3.30 A; A=54-358. DR PDB; 7YMJ; EM; 3.35 A; A=249-277. DR PDB; 8DZP; EM; 2.71 A; A=54-358. DR PDB; 8DZQ; EM; 2.82 A; A=54-358. DR PDB; 8DZR; EM; 2.61 A; A=54-338. DR PDB; 8DZS; EM; 2.65 A; A=54-358. DR PDB; 8F7W; EM; 3.19 A; R=3-380. DR PDB; 8FEG; EM; 2.54 A; B=54-358. DR PDB; 8HNN; EM; 3.60 A; R=252-276. DR PDB; 8K2W; EM; 3.00 A; R=252-276. DR PDBsum; 4DJH; -. DR PDBsum; 6B73; -. DR PDBsum; 6VI4; -. DR PDBsum; 7T10; -. DR PDBsum; 7T11; -. DR PDBsum; 7UL2; -. DR PDBsum; 7UL3; -. DR PDBsum; 7UL5; -. DR PDBsum; 7Y1F; -. DR PDBsum; 7YIT; -. DR PDBsum; 7YMJ; -. DR PDBsum; 8DZP; -. DR PDBsum; 8DZQ; -. DR PDBsum; 8DZR; -. DR PDBsum; 8DZS; -. DR PDBsum; 8F7W; -. DR PDBsum; 8FEG; -. DR PDBsum; 8HNN; -. DR PDBsum; 8K2W; -. DR AlphaFoldDB; P41145; -. DR EMDB; EMD-25586; -. DR EMDB; EMD-25587; -. DR EMDB; EMD-27804; -. DR EMDB; EMD-27805; -. DR EMDB; EMD-27806; -. DR EMDB; EMD-27807; -. DR EMDB; EMD-28911; -. DR EMDB; EMD-41876; -. DR SMR; P41145; -. DR BioGRID; 111031; 11. DR IntAct; P41145; 12. DR MINT; P41145; -. 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 GlyCosmos; P41145; 2 sites, No reported glycans. DR GlyGen; P41145; 2 sites. DR iPTMnet; P41145; -. DR PhosphoSitePlus; P41145; -. DR BioMuta; OPRK1; -. DR DMDM; 116242691; -. DR MassIVE; P41145; -. DR PaxDb; 9606-ENSP00000265572; -. DR PeptideAtlas; P41145; -. DR ProteomicsDB; 15940; -. DR ProteomicsDB; 55403; -. [P41145-1] DR ABCD; P41145; 1 sequenced antibody. DR Antibodypedia; 11640; 452 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 AGR; HGNC:8154; -. DR CTD; 4986; -. DR DisGeNET; 4986; -. DR GeneCards; OPRK1; -. DR HGNC; HGNC:8154; OPRK1. DR HPA; ENSG00000082556; Tissue enhanced (brain, prostate, skeletal muscle). 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; QDPTYMR; -. DR OrthoDB; 5393360at2759; -. 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; 11 hits in 1154 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 74 other cell types or tissues. DR ExpressionAtlas; P41145; baseline and differential. 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:0016020; C:membrane; IDA:UniProtKB. 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:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. 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:0042923; F:neuropeptide 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: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: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: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 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; P41145; HS. 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 58..79 FT /evidence="ECO:0007829|PDB:8DZR" FT TURN 80..84 FT /evidence="ECO:0007829|PDB:8DZR" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:8DZS" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:8DZR" FT HELIX 113..120 FT /evidence="ECO:0007829|PDB:8DZR" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:8DZR" FT TURN 125..128 FT /evidence="ECO:0007829|PDB:7YIT" FT HELIX 130..161 FT /evidence="ECO:0007829|PDB:8DZR" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:8DZR" FT HELIX 166..169 FT /evidence="ECO:0007829|PDB:8DZR" FT HELIX 172..196 FT /evidence="ECO:0007829|PDB:8DZR" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:8DZR" FT STRAND 203..206 FT /evidence="ECO:0007829|PDB:4DJH" FT STRAND 209..212 FT /evidence="ECO:0007829|PDB:8DZR" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:8DZP" FT HELIX 222..234 FT /evidence="ECO:0007829|PDB:8DZR" FT HELIX 246..253 FT /evidence="ECO:0007829|PDB:7UL2" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:7T10" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:8DZS" FT HELIX 263..277 FT /evidence="ECO:0007829|PDB:7UL2" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:7Y1F" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:7Y1F" FT HELIX 310..331 FT /evidence="ECO:0007829|PDB:8DZR" FT HELIX 335..338 FT /evidence="ECO:0007829|PDB:8DZP" 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 //