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   27-MAR-2024, entry version 163.
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 a
CC       receptor for the endogenous neuropeptide nociceptin. 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. Signaling via G proteins mediates inhibition of
CC       adenylate cyclase activity and calcium channel activity. Arrestins
CC       modulate signaling via G proteins and mediate the activation of
CC       alternative signaling pathways that lead to the activation of MAP
CC       kinases. Plays a role in modulating nociception and the perception of
CC       pain. Plays a role in the regulation of locomotor activity by the
CC       neuropeptide nociceptin. {ECO:0000269|PubMed:15937148,
CC       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   GlyCosmos; P35370; 3 sites, No reported glycans.
DR   GlyGen; P35370; 3 sites.
DR   iPTMnet; P35370; -.
DR   PhosphoSitePlus; P35370; -.
DR   PaxDb; 10116-ENSRNOP00000047053; -.
DR   Ensembl; ENSRNOT00000045845.4; ENSRNOP00000047053.1; ENSRNOG00000016768.8.
DR   Ensembl; ENSRNOT00055002097; ENSRNOP00055001632; ENSRNOG00055001262.
DR   Ensembl; ENSRNOT00060002205; ENSRNOP00060001392; ENSRNOG00060001471.
DR   Ensembl; ENSRNOT00065023194; ENSRNOP00065018063; ENSRNOG00065014024.
DR   GeneID; 29256; -.
DR   KEGG; rno:29256; -.
DR   UCSC; RGD:68438; rat.
DR   AGR; RGD:68438; -.
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; VNICIWA; -.
DR   OrthoDB; 5393360at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; P35370; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; ISO:RGD.
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:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
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: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:0007270; P:neuron-neuron synaptic transmission; ISO:RGD.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO: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:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   CDD; cd15092; 7tmA_NOFQ_opioid_R; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   InterPro; IPR001420; X_opioid_rcpt.
DR   PANTHER; PTHR24229; NEUROPEPTIDES RECEPTOR; 1.
DR   PANTHER; PTHR24229:SF11; NOCICEPTIN RECEPTOR; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P35370; RN.
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
//