ID   OPRX_CAVPO              Reviewed;         370 AA.
AC   P47748;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Nociceptin receptor;
DE   AltName: Full=Kappa-type 3 opioid receptor;
DE            Short=KOR-3;
DE   AltName: Full=Orphanin FQ receptor;
DE   AltName: Full=XOR;
GN   Name=OPRL1; Synonyms=OOR;
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].
RC   STRAIN=Hartley; TISSUE=Brain;
RA   Xie G.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: G-protein coupled opioid receptor that functions as receptor
CC       for the endogenous neuropeptide nociceptin. Ligand binding causes a
CC       conformation change that triggers signaling via guanine nucleotide-
CC       binding proteins (G proteins) and modulates the activity of down-stream
CC       effectors. Signaling via G proteins mediates inhibition of adenylate
CC       cyclase activity and calcium channel activity. Arrestins modulate
CC       signaling via G proteins and mediate the activation of alternative
CC       signaling pathways that lead to the activation of MAP kinases. Plays a
CC       role in modulating nociception and the perception of pain. Plays a role
CC       in the regulation of locomotor activity by the neuropeptide nociceptin
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Ligand
CC       binding leads to receptor internalization into cytoplasmic vesicles,
CC       decreasing the amount of available receptor at the cell surface.
CC       Internalization may require phosphorylation. Can recycle to the cell
CC       membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U04369; AAA58332.1; -; mRNA.
DR   RefSeq; NP_001166462.1; NM_001172991.1.
DR   AlphaFoldDB; P47748; -.
DR   SMR; P47748; -.
DR   STRING; 10141.ENSCPOP00000013520; -.
DR   BindingDB; P47748; -.
DR   ChEMBL; CHEMBL5492; -.
DR   DrugCentral; P47748; -.
DR   GeneID; 100135588; -.
DR   KEGG; cpoc:100135588; -.
DR   CTD; 4987; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P47748; -.
DR   OrthoDB; 1011272at2759; -.
DR   PRO; PR:P47748; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:0001626; F:nociceptin receptor activity; ISS:UniProtKB.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   InterPro; IPR001420; X_opioid_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00384; OPIOIDR.
DR   PRINTS; PR00547; XOPIOIDR.
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; Cytoplasmic vesicle; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..370
FT                   /note="Nociceptin receptor"
FT                   /id="PRO_0000069979"
FT   TOPO_DOM        1..48
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..74
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        75..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        88..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        110..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        125..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        147..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        166..188
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        189..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        212..236
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        237..264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        265..285
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        286..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        301..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        323..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   SITE            110
FT                   /note="Important for G protein-mediated signaling"
FT                   /evidence="ECO:0000250"
FT   SITE            130
FT                   /note="Important for G protein-mediated signaling"
FT                   /evidence="ECO:0000250"
FT   LIPID           334
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   370 AA;  40789 MW;  DAA807CE24283573 CRC64;
     MESLFPAPFW EVLYGSHLQG NLSLLSPNHS GLPPHLLLNA SHSAFLPLGL KVTIVGLYLA
     VCIGGLLGNC LVMYVILRHT KMKTATNIYI FNLALADTLV LLTLPFQATD ILLGFWPFGN
     TLCKTVIAID YYNMFTSTFT LTAMSVDRYV AICHPIRALD VRTSSKAQAV NVAIWALALV
     VGVPVAIMGS AQVEDEEIEC LVEIPDPQDY WGPVFAVSIF LFSFIIPVLI ISVCYSLMIR
     RLHGVRLLSG SREKDRNLRR ITRLVLVVVA VFVGCWTPVQ VFVLVQGLGV QPGSETTVAI
     LRFCTALGYV NSCLNPILYA FLDENFKACF RKFCCASALH REMQVSDRVR SIAKDVALGC
     KTTETVPRPA