OPRX_RAT
ID OPRX_RAT Reviewed; 367 AA.
AC P35370; Q791R4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
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=ROR-C;
DE AltName: Full=XOR1;
GN Name=Oprl1; Synonyms=Oor, Oprl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8163014; DOI=10.1016/0014-5793(94)80603-9;
RA Fukuda K., Kato S., Mori K., Nishi M., Takeshima H., Iwabe N., Miyata T.,
RA Houtani T., Sugimoto T.;
RT "cDNA cloning and regional distribution of a novel member of the opioid
RT receptor family.";
RL FEBS Lett. 343:42-46(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RA Meng F., Xie G., Alfred M., Thompson R., Hoversten M., Watson S., Akil H.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8034019; DOI=10.1016/0014-5793(94)00561-3;
RA Bunzow J.R., Saez C., Mortrud M., Bouvier C., Williams J.T., Low M.,
RA Grandy D.K.;
RT "Molecular cloning and tissue distribution of a putative member of the rat
RT opioid receptor gene family that is not a mu, delta or kappa opioid
RT receptor type.";
RL FEBS Lett. 347:284-288(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8034018; DOI=10.1016/0014-5793(94)00560-5;
RA Chen Y., Fan Y., Liu J., Mestek A., Tian M., Kozak C.A., Yu L.;
RT "Molecular cloning, tissue distribution and chromosomal localization of a
RT novel member of the opioid receptor gene family.";
RL FEBS Lett. 347:279-283(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7798930; DOI=10.1046/j.1471-4159.1995.64010034.x;
RA Lachowicz J.E., Shen Y., Monsma F.J. Jr., Sibley D.R.;
RT "Molecular cloning of a novel G protein-coupled receptor related to the
RT opiate receptor family.";
RL J. Neurochem. 64:34-40(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8026588; DOI=10.1016/0014-5793(94)00557-5;
RA Wang J.B., Johnson P.S., Imai Y., Persico A.M., Ozenberger B.A.,
RA Eppler C.M., Uhl G.R.;
RT "cDNA cloning of an orphan opiate receptor gene family member and its
RT splice variant.";
RL FEBS Lett. 348:75-79(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7877452; DOI=10.1016/0169-328x(94)90181-3;
RA Wick M.J., Minnerath S.R., Lin X., Elde R.P., Law P.Y., Loh H.H.;
RT "Isolation of a novel cDNA encoding a putative membrane receptor with high
RT homology to the cloned mu, delta, and kappa opioid receptors.";
RL Brain Res. Mol. Brain Res. 27:37-44(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11290428; DOI=10.1016/s0378-1119(00)00553-9;
RA Curro D., Song I., Anderson M., Yoo J.H., Del Valle J., Owyang C.;
RT "Molecular cloning of the orphanin FQ receptor gene and differential tissue
RT expression of splice variants in rat.";
RL Gene 266:139-145(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=15937148; DOI=10.1124/jpet.105.089284;
RA Ruiz-Velasco V., Puhl H.L., Fuller B.C., Sumner A.D.;
RT "Modulation of Ca2+ channels by opioid receptor-like 1 receptors natively
RT expressed in rat stellate ganglion neurons innervating cardiac muscle.";
RL J. Pharmacol. Exp. Ther. 314:987-994(2005).
RN [10]
RP FUNCTION.
RX PubMed=18588920; DOI=10.1016/j.regpep.2008.06.001;
RA Chen L.Y., Huang J.X., Yu L.C.;
RT "Involvement of ORL1 receptor and ERK kinase in the orphanin FQ-induced
RT nociception in the nucleus accumbens of rats.";
RL Regul. Pept. 151:43-47(2008).
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 {ECO:0000269|PubMed:15937148, ECO:0000269|PubMed:18588920}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasmic vesicle {ECO:0000250}. Note=Ligand binding leads to
CC receptor internalization into cytoplasmic vesicles, decreasing the
CC amount of available receptor at the cell surface (By similarity).
CC Internalization requires phosphorylation at Ser-360. Can recycle to the
CC cell membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in several brain areas, the
CC intestine, liver and spleen. Detected in sympathetic stellate ganglion
CC neurons. {ECO:0000269|PubMed:11290428, ECO:0000269|PubMed:15937148,
CC ECO:0000269|PubMed:7798930, ECO:0000269|PubMed:8026588,
CC ECO:0000269|PubMed:8034018, ECO:0000269|PubMed:8034019,
CC ECO:0000269|PubMed:8163014}.
CC -!- PTM: Phosphorylation at Ser-360 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; D16438; BAA03908.1; -; mRNA.
DR EMBL; U05239; AAA16201.1; -; mRNA.
DR EMBL; U01913; AAA21025.1; -; mRNA.
DR EMBL; L28144; AAC37661.1; -; mRNA.
DR EMBL; U07871; AAA69927.1; -; mRNA.
DR EMBL; L33916; AAA50827.1; -; mRNA.
DR EMBL; L29419; AAC42041.1; -; mRNA.
DR EMBL; AF216218; AAF80990.1; -; Genomic_DNA.
DR EMBL; AY152731; AAN77720.1; -; mRNA.
DR PIR; I56520; I56520.
DR RefSeq; NP_113757.1; NM_031569.4.
DR RefSeq; XP_006235798.1; XM_006235736.3.
DR RefSeq; XP_006235800.1; XM_006235738.3.
DR RefSeq; XP_017447001.1; XM_017591512.1.
DR RefSeq; XP_017447002.1; XM_017591513.1.
DR RefSeq; XP_017447003.1; XM_017591514.1.
DR AlphaFoldDB; P35370; -.
DR SMR; P35370; -.
DR STRING; 10116.ENSRNOP00000047053; -.
DR BindingDB; P35370; -.
DR ChEMBL; CHEMBL4503; -.
DR GuidetoPHARMACOLOGY; 320; -.
DR GlyGen; P35370; 3 sites.
DR iPTMnet; P35370; -.
DR PhosphoSitePlus; P35370; -.
DR PaxDb; P35370; -.
DR PRIDE; P35370; -.
DR Ensembl; ENSRNOT00000045845; ENSRNOP00000047053; ENSRNOG00000016768.
DR GeneID; 29256; -.
DR KEGG; rno:29256; -.
DR UCSC; RGD:68438; rat.
DR CTD; 4987; -.
DR RGD; 68438; Oprl1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160661; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P35370; -.
DR OMA; SNWFNNG; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P35370; -.
DR TreeFam; TF315737; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P35370; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016768; Expressed in frontal cortex and 4 other tissues.
DR ExpressionAtlas; P35370; baseline and differential.
DR Genevisible; P35370; RN.
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:0016020; C:membrane; IDA:RGD.
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:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1990708; P:conditioned place preference; IMP:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; ISO:RGD.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IMP:RGD.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:RGD.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; IMP:RGD.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0035810; P:positive regulation of urine volume; IDA:RGD.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IMP:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
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..367
FT /note="Nociceptin receptor"
FT /id="PRO_0000069983"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..121
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 144..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 163..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 186..208
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 209..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 234..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 283..297
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 298..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 320..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT SITE 107
FT /note="Important for G protein-mediated signaling"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Important for G protein-mediated signaling"
FT /evidence="ECO:0000250"
FT LIPID 331
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 105
FT /note="G -> R (in Ref. 2; AAA16201)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="L -> V (in Ref. 2; AAA16201)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="S -> P (in Ref. 2; AAA16201)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="S -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40523 MW; EB2637582747B4AD CRC64;
MESLFPAPYW EVLYGSHFQG NLSLLNETVP HHLLLNASHS AFLPLGLKVT IVGLYLAVCI
GGLLGNCLVM YVILRHTKMK TATNIYIFNL ALADTLVLLT LPFQGTDILL GFWPFGNALC
KTVIAIDYYN MFTSTFTLTA MSVDRYVAIC HPIRALDVRT SSKAQAVNVA IWALASVVGV
PVAIMGSAQV EDEEIECLVE IPAPQDYWGP VFAICIFLFS FIIPVLIISV CYSLMIRRLR
GVRLLSGSRE KDRNLRRITR LVLVVVAVFV GCWTPVQVFV LVQGLGVQPG SETAVAILRF
CTALGYVNSC LNPILYAFLD ENFKACFRKF CCASSLHREM QVSDRVRSIA KDVGLGCKTS
ETVPRPA
