OPRK_CAVPO
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 03-AUG-2022, entry version 116.
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 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:8170987}.
CC -!- SUBUNIT: Interacts with SLC9A3R1. 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.ENSCPOP00000020555; -.
DR BindingDB; P41144; -.
DR ChEMBL; CHEMBL3952; -.
DR DrugCentral; P41144; -.
DR GeneID; 100135587; -.
DR KEGG; cpoc:100135587; -.
DR CTD; 4986; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P41144; -.
DR OrthoDB; 1011272at2759; -.
DR PRO; PR:P41144; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of 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 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 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