OPRX_PIG
ID OPRX_PIG Reviewed; 370 AA.
AC P79292;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Nociceptin receptor;
DE AltName: Full=K3 opiate receptor;
DE AltName: Full=Kappa-type 3 opioid receptor;
DE Short=KOR-3;
DE AltName: Full=ORGC;
DE AltName: Full=Orphanin FQ receptor;
GN Name=OPRL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=9988113; DOI=10.1016/s0014-2999(98)00869-3;
RA Osinski M.A., Pampusch M.S., Murtaugh M.P., Brown D.R.;
RT "Cloning, expression and functional role of a nociceptin/orphanin FQ
RT receptor in the porcine gastrointestinal tract.";
RL Eur. J. Pharmacol. 365:281-289(1999).
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 requires phosphorylation at Ser-363. Can recycle to the
CC cell membrane (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, stomach, ileum, jejunum
CC and colon. {ECO:0000269|PubMed:9988113}.
CC -!- PTM: Phosphorylation at Ser-363 requires GRK3. {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; U72758; AAB39702.1; -; mRNA.
DR RefSeq; NP_999341.1; NM_214176.1.
DR AlphaFoldDB; P79292; -.
DR SMR; P79292; -.
DR BindingDB; P79292; -.
DR GeneID; 397364; -.
DR KEGG; ssc:397364; -.
DR CTD; 4987; -.
DR InParanoid; P79292; -.
DR OrthoDB; 1011272at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0001626; F:nociceptin receptor activity; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
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:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
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 Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Nociceptin receptor"
FT /id="PRO_0000069982"
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; 40610 MW; 48E4F3E6DA223BCD CRC64;
MESLFPAPFW EVLYGSPLQG NLSLLSPNHS LLPPHLLLNA SHGAFLPLGL KVTIVGLYLA
VCVGGLLGNC LVMYVILRHT KMKTATNIYI FNLALADTAV LLTLPFQGTD VLLGFWPFGN
ALCKAVIAID YYNMFTSAFT LTAMSVDRYV AICHPIRALD VRTSSKAQAV NVAIWALASI
VGVPVAIMGS AQVEDEEIEC LVEIPAPQDY WGPVFAVCIF LFSFVIPVLI ISVCYSLMVR
RLRGVRLLSG SREKDRNLRR ITRLVLVVVA VFVGCWTPVQ VFVLVQGLGV QPGSETAVAV
LRFCTALGYV NSCLNPILYA FLDENFKACF RKFCCAPTRR REMQVSDRVR SIAKDVALAC
KTSETVPRPA
