ID OPRK_CAVPO Reviewed; 380 AA.
AC P41144;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 24-JAN-2024, entry version 119.
DE RecName: Full=Kappa-type opioid receptor;
DE Short=K-OR-1;
DE Short=KOR-1;
GN Name=OPRK1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Hartley; TISSUE=Brain;
RX PubMed=8170987; DOI=10.1073/pnas.91.9.3779;
RA Xie G.X., Meng F., Mansour A., Thompson R.C., Hoversten M.T., Goldstein A.,
RA Watson S.J., Akil H.;
RT "Primary structure and functional expression of a guinea pig kappa opioid
RT (dynorphin) receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3779-3783(1994).
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:8170987}.
CC -!- SUBUNIT: Interacts with NHERF1. Interacts with GABARAPL1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8170987};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8170987}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U04092; AAA67171.1; -; mRNA.
DR PIR; A55259; A55259.
DR RefSeq; NP_001166461.1; NM_001172990.1.
DR AlphaFoldDB; P41144; -.
DR SMR; P41144; -.
DR STRING; 10141.ENSCPOP00000005950; -.
DR BindingDB; P41144; -.
DR ChEMBL; CHEMBL3952; -.
DR DrugCentral; P41144; -.
DR GlyCosmos; P41144; 2 sites, No reported glycans.
DR GeneID; 100135587; -.
DR KEGG; cpoc:100135587; -.
DR CTD; 4986; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P41144; -.
DR OrthoDB; 5393360at2759; -.
DR PRO; PR:P41144; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046877; P:regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
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.
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_0000069966"
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"
SQ SEQUENCE 380 AA; 42736 MW; 4FF053834DBBA623 CRC64;
MGRRRQGPAQ PASELPARNA CLLPNGSAWL PGWAEPDGNG SAGPQDEQLE PAHISPAIPV
IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN LALADALVTT TMPFQSTVYL
MNSWPFGDVL CKIVISIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPLKAKIINI
CIWLLSSSVG ISAIILGGTK VREDVDIIEC SLQFPDDDYS WWDLFMKICV FVFAFVIPVL
IIIVCYTLMI LRLKSVRLLS GSREKDRNLR RITRLVLVVV AVFIICWTPI HIFILVEALG
STSHSTAALS SYYFCIALGY TNSSLNPILY AFLDENFKRC FRDFCFPIKM RMERQSTSRV
RNTVQDPAYM RNVDGVNKPV
//
