OPRK_MOUSE
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 03-AUG-2022, entry version 175.
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 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:8393575,
CC ECO:0000269|PubMed:9463367}.
CC -!- SUBUNIT: Interacts with SLC9A3R1. 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}.
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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.ENSMUSP00000027038; -.
DR BindingDB; P33534; -.
DR ChEMBL; CHEMBL4329; -.
DR DrugCentral; P33534; -.
DR GuidetoPHARMACOLOGY; 318; -.
DR GlyGen; P33534; 2 sites.
DR iPTMnet; P33534; -.
DR PhosphoSitePlus; P33534; -.
DR SwissPalm; P33534; -.
DR PaxDb; P33534; -.
DR PRIDE; P33534; -.
DR Antibodypedia; 11640; 397 antibodies from 38 providers.
DR DNASU; 18387; -.
DR Ensembl; ENSMUST00000027038; ENSMUSP00000027038; ENSMUSG00000025905.
DR Ensembl; ENSMUST00000160339; ENSMUSP00000124030; ENSMUSG00000025905.
DR Ensembl; ENSMUST00000160777; ENSMUSP00000125105; ENSMUSG00000025905.
DR GeneID; 18387; -.
DR KEGG; mmu:18387; -.
DR UCSC; uc007afo.2; mouse.
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; FPFKMRM; -.
DR OrthoDB; 1011272at2759; -.
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 73 CRISPR screens.
DR PRO; PR:P33534; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P33534; protein.
DR Bgee; ENSMUSG00000025905; Expressed in decidua basalis and 75 other tissues.
DR ExpressionAtlas; P33534; baseline and differential.
DR Genevisible; P33534; MM.
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:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045202; C:synapse; 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: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; 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:0040017; P:positive regulation of locomotion; 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:0051930; P:regulation of sensory perception of pain; ISO:MGI.
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 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 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
