OX2R_RAT
ID OX2R_RAT Reviewed; 460 AA.
AC P56719;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Orexin receptor type 2;
DE Short=Ox-2-R;
DE Short=Ox2-R;
DE Short=Ox2R;
DE AltName: Full=Hypocretin receptor type 2;
GN Name=Hcrtr2;
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 TISSUE=Brain;
RX PubMed=9491897; DOI=10.1016/s0092-8674(00)80949-6;
RA Sakurai T., Amemiya A., Ishii M., Matsuzaki I., Chemelli R.M., Tanaka H.,
RA Williams S.C., Richardson J.A., Kozlowski G.P., Wilson S., Arch J.R.S.,
RA Buckingham R.E., Haynes A.C., Carr S.A., Annan R.S., McNulty D.E.,
RA Liu W.-S., Terrett J.A., Elshourbagy N.A., Bergsma D.J., Yanagisawa M.;
RT "Orexins and orexin receptors: a family of hypothalamic neuropeptides and G
RT protein-coupled receptors that regulate feeding behavior.";
RL Cell 92:573-585(1998).
RN [2]
RP REVIEW.
RX PubMed=11340621; DOI=10.1002/bies.1058;
RA Hungs M., Mignot E.;
RT "Hypocretin/orexin, sleep and narcolepsy.";
RL Bioessays 23:397-408(2001).
RN [3]
RP REVIEW.
RX PubMed=11283317; DOI=10.1146/annurev.neuro.24.1.429;
RA Willie J.T., Chemelli R.M., Sinton C.M., Yanagisawa M.;
RT "To eat or to sleep? Orexin in the regulation of feeding and wakefulness.";
RL Annu. Rev. Neurosci. 24:429-458(2001).
CC -!- FUNCTION: Nonselective, high-affinity receptor for both orexin-A and
CC orexin-B neuropeptides. Triggers an increase in cytoplasmic Ca(2+)
CC levels in response to orexin-A binding. {ECO:0000250|UniProtKB:O43614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43614};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O43614}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain in the cerebral cortex,
CC septal nuclei, hippocampus, medial thalamic groups, dorsal and median
CC raphe nuclei, and many hypothalamic nuclei including the
CC tuberomammillary nucleus, dorsomedial hypothalamus, paraventricular
CC hypothalamic nucleus, and ventral premammillary nucleus. Not detected
CC in the spleen, lung, liver, skeletal muscle, kidney and testis. Orexin
CC receptor mRNA expression has also been reported in the adrenal gland,
CC enteric nervous system, and pancreas. {ECO:0000269|PubMed:9491897}.
CC -!- DOMAIN: The N-terminal region is required for orexin signaling.
CC {ECO:0000250|UniProtKB:O43614}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF041246; AAC40042.1; -; mRNA.
DR RefSeq; NP_037206.1; NM_013074.1.
DR AlphaFoldDB; P56719; -.
DR SMR; P56719; -.
DR STRING; 10116.ENSRNOP00000015824; -.
DR BindingDB; P56719; -.
DR ChEMBL; CHEMBL1275216; -.
DR GuidetoPHARMACOLOGY; 322; -.
DR GlyGen; P56719; 3 sites.
DR PhosphoSitePlus; P56719; -.
DR PaxDb; P56719; -.
DR Ensembl; ENSRNOT00000015824; ENSRNOP00000015824; ENSRNOG00000011251.
DR GeneID; 25605; -.
DR KEGG; rno:25605; -.
DR UCSC; RGD:2788; rat.
DR CTD; 3062; -.
DR RGD; 2788; Hcrtr2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; P56719; -.
DR OMA; AEVYPKM; -.
DR OrthoDB; 981089at2759; -.
DR PhylomeDB; P56719; -.
DR TreeFam; TF315303; -.
DR Reactome; R-RNO-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P56719; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000011251; Expressed in cerebellum and 1 other tissue.
DR Genevisible; P56719; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR GO; GO:0016499; F:orexin receptor activity; IDA:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
DR GO; GO:0022410; P:circadian sleep/wake cycle process; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0040011; P:locomotion; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0010840; P:regulation of circadian sleep/wake cycle, wakefulness; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000204; Orexin_rcpt.
DR InterPro; IPR004060; Orexin_rcpt_2.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF03827; Orexin_rec2; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01522; OREXIN2R.
DR PRINTS; PR01064; OREXINR.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..460
FT /note="Orexin receptor type 2"
FT /id="PRO_0000069992"
FT TOPO_DOM 1..54
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 76..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 89..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 111..127
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 128..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 151..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 171..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 192..222
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 244..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 305..326
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 327..342
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TRANSMEM 343..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT TOPO_DOM 367..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT REGION 33..49
FT /note="Required for response to orexin-A"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT SITE 44
FT /note="Important for responses to orexin"
FT /evidence="ECO:0000250|UniProtKB:O43614"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..210
FT /evidence="ECO:0000250|UniProtKB:O43614"
SQ SEQUENCE 460 AA; 52489 MW; 3B44E3D82F8B85D5 CRC64;
MSSTKLEDSL PRRNWSSASE LNETQEPFLN PTDYDDEEFL RYLWREYLHP KEYEWVLIAG
YIIVFVVALI GNVLVCVAVW KNHHMRTVTN YFIVNLSLAD VLVTITCLPA TLVVDITETW
FFGQSLCKVI PYLQTVSVSV SVLTLSCIAL DRWYAICHPL MFKSTAKRAR NSIVVIWIVS
CIIMIPQAIV MERSSMLPGL ANKTTLFTVC DERWGGEVYP KMYHICFFLV TYMAPLCLMV
LAYLQIFRKL WCRQIPGTSS VVQRKWKQPQ PVSQPRGSGQ QSKARISAVA AEIKQIRARR
KTARMLMVVL LVFAICYLPI SILNVLKRVF GMFTHTEDRE TVYAWFTFSH WLVYANSAAN
PIIYNFLSGK FREEFKAAFS CCLGVHRRQG DRLARGRTST ESRKSLTTQI SNFDNVSKLS
EHVALTSIST LPAANGAGPL QNWYLQQGVP SSLLSTWLEV
