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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
 
 
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