ID OPRK_MOUSE Reviewed; 380 AA. AC P33534; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 24-JAN-2024, entry version 183. DE RecName: Full=Kappa-type opioid receptor; DE Short=K-OR-1; DE Short=KOR-1; DE AltName: Full=MSL-1; GN Name=Oprk1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=8393575; DOI=10.1073/pnas.90.14.6736; RA Yasuda K., Raynor K., Kong H., Breder C.D., Takeda J., Reisine T., RA Bell G.I.; RT "Cloning and functional comparison of kappa and delta opioid receptors from RT mouse brain."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6736-6740(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7802669; DOI=10.1006/bbrc.1994.2814; RA Nishi M., Takeshima H., Mori M., Nakagawara K., Takeuchi T.; RT "Structure and chromosomal mapping of genes for the mouse kappa-opioid RT receptor and an opioid receptor homologue (MOR-C)."; RL Biochem. Biophys. Res. Commun. 205:1353-1357(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7733933; DOI=10.1006/bbrc.1995.1547; RA Liu H.C., Lu S., Augustin L.B., Felsheim R.F., Chen H.C., Loh H.H., RA Wei L.N.; RT "Cloning and promoter mapping of mouse kappa opioid receptor gene."; RL Biochem. Biophys. Res. Commun. 209:639-647(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7499487; DOI=10.1016/0165-5728(95)00116-j; RA Belkowski S.M., Zhu J., Liu-Chen L.Y., Eisenstein T.K., Adler M.W., RA Rogers T.J.; RT "Sequence of kappa-opioid receptor cDNA in the R1.1 thymoma cell line."; RL J. Neuroimmunol. 62:113-117(1995). RN [5] RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=9463367; DOI=10.1093/emboj/17.4.886; RA Simonin F., Valverde O., Smadja C., Slowe S., Kitchen I., Dierich A., RA Le Meur M., Roques B.P., Maldonado R., Kieffer B.L.; RT "Disruption of the kappa-opioid receptor gene in mice enhances sensitivity RT to chemical visceral pain, impairs pharmacological actions of the selective RT kappa-agonist U-50,488H and attenuates morphine withdrawal."; RL EMBO J. 17:886-897(1998). 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:8393575, ECO:0000269|PubMed:9463367}. CC -!- SUBUNIT: Interacts with NHERF1. Interacts with GABARAPL1 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8393575, CC ECO:0000269|PubMed:9463367}; Multi-pass membrane protein CC {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}. CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Brain CC (neocortex, hippocampus, amygdala, medial habenula, hypothalamus, locus CC ceruleus, and parabrachial nucleus). {ECO:0000269|PubMed:8393575, CC ECO:0000269|PubMed:9463367}. CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and CC show no obvious phenotype. Mutant mice do not display analgesia after CC treatment with the synthetic agonist U-50,488H. Unlike wild-type mice, CC they do not show reduced locomotion and increased salivation in CC response to the synthetic agonist U-50,488H. CC {ECO:0000269|PubMed:9463367}. 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; L11065; AAA39363.1; -; mRNA. DR EMBL; D31665; BAA06508.1; -; Genomic_DNA. DR EMBL; S77872; AAB34130.2; -; Genomic_DNA. DR EMBL; S77868; AAB34130.2; JOINED; Genomic_DNA. DR EMBL; S77869; AAB34130.2; JOINED; Genomic_DNA. DR EMBL; S81111; AAP32232.1; -; mRNA. DR CCDS; CCDS14809.1; -. DR PIR; A48227; A48227. DR PIR; JC2434; JC2434. DR RefSeq; NP_001191300.1; NM_001204371.1. DR RefSeq; NP_001305664.1; NM_001318735.1. DR RefSeq; NP_035141.1; NM_011011.2. DR AlphaFoldDB; P33534; -. DR SMR; P33534; -. DR STRING; 10090.ENSMUSP00000125105; -. DR BindingDB; P33534; -. DR ChEMBL; CHEMBL4329; -. DR DrugCentral; P33534; -. DR GuidetoPHARMACOLOGY; 318; -. DR GlyCosmos; P33534; 2 sites, No reported glycans. DR GlyGen; P33534; 2 sites. DR iPTMnet; P33534; -. DR PhosphoSitePlus; P33534; -. DR SwissPalm; P33534; -. DR PaxDb; 10090-ENSMUSP00000027038; -. DR Antibodypedia; 11640; 452 antibodies from 38 providers. DR DNASU; 18387; -. DR Ensembl; ENSMUST00000027038.11; ENSMUSP00000027038.5; ENSMUSG00000025905.15. DR Ensembl; ENSMUST00000160339.2; ENSMUSP00000124030.2; ENSMUSG00000025905.15. DR Ensembl; ENSMUST00000160777.8; ENSMUSP00000125105.2; ENSMUSG00000025905.15. DR GeneID; 18387; -. DR KEGG; mmu:18387; -. DR UCSC; uc007afo.2; mouse. DR AGR; MGI:97439; -. DR CTD; 4986; -. DR MGI; MGI:97439; Oprk1. DR VEuPathDB; HostDB:ENSMUSG00000025905; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000157341; -. DR HOGENOM; CLU_009579_8_1_1; -. DR InParanoid; P33534; -. DR OMA; QDPTYMR; -. DR OrthoDB; 5393360at2759; -. DR PhylomeDB; P33534; -. DR TreeFam; TF315737; -. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 18387; 3 hits in 78 CRISPR screens. DR PRO; PR:P33534; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P33534; Protein. DR Bgee; ENSMUSG00000025905; Expressed in decidua basalis and 77 other cell types or tissues. DR ExpressionAtlas; P33534; baseline and differential. DR GO; GO:0043679; C:axon terminus; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI. DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI. DR GO; GO:0038048; F:dynorphin receptor activity; ISS: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; ISO:MGI. DR GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI. DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI. DR GO; GO:1990708; P:conditioned place preference; ISO:MGI. DR GO; GO:0051607; P:defense response to virus; ISO:MGI. DR GO; GO:0042755; P:eating behavior; ISO:MGI. DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; ISO:MGI. DR GO; GO:0006955; P:immune response; ISO:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB. DR GO; GO:0042711; P:maternal behavior; ISO:MGI. DR GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; ISO:MGI. 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; ISO:MGI. DR GO; GO:1904000; P:positive regulation of eating behavior; ISO:MGI. DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI. DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI. DR GO; GO:0046877; P:regulation of saliva secretion; IMP:UniProtKB. DR GO; GO:0032868; P:response to insulin; ISO:MGI. DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB. DR GO; GO:0050951; P:sensory perception of temperature stimulus; ISO:MGI. 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; P33534; MM. PE 1: Evidence at protein 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_0000069968" 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 211 FT /note="S -> L (in Ref. 2; BAA06508)" FT /evidence="ECO:0000305" FT CONFLICT 231 FT /note="F -> V (in Ref. 2; BAA06508)" FT /evidence="ECO:0000305" SQ SEQUENCE 380 AA; 42652 MW; FA4FC947D4545318 CRC64; MESPIQIFRG DPGPTCSPSA CLLPNSSSWF PNWAESDSNG SVGSEDQQLE SAHISPAIPV IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN LALADALVTT TMPFQSAVYL MNSWPFGDVL CKIVISIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPLKAKIINI CIWLLASSVG ISAIVLGGTK VREDVDVIEC SLQFPDDEYS WWDLFMKICV FVFAFVIPVL IIIVCYTLMI LRLKSVRLLS GSREKDRNLR RITKLVLVVV AVFIICWTPI HIFILVEALG STSHSTAALS SYYFCIALGY TNSSLNPVLY AFLDENFKRC FRDFCFPIKM RMERQSTNRV RNTVQDPASM RDVGGMNKPV //