OX2R_MOUSE
ID OX2R_MOUSE Reviewed; 460 AA.
AC P58308; Q5SGC8; Q6VLX3; Q8BG12;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
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; Synonyms=Mox2r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15256537; DOI=10.1210/me.2004-0167;
RA Chen J., Randeva H.S.;
RT "Genomic organization of mouse orexin receptors: characterization of two
RT novel tissue-specific splice variants.";
RL Mol. Endocrinol. 18:2790-2804(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-311 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J;
RA Szendro P.I., Maevers K., Eichele G.;
RT "Cloning of mouse orexin receptors.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=2b;
CC IsoId=P58308-1; Sequence=Displayed;
CC Name=2; Synonyms=2a;
CC IsoId=P58308-2; Sequence=VSP_016466;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 not detected in
CC skeletal muscle and kidney. {ECO:0000269|PubMed:15256537}.
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; AY336084; AAR01327.1; -; mRNA.
DR EMBL; AY336085; AAR01328.1; -; mRNA.
DR EMBL; AY339390; AAR11293.1; -; Genomic_DNA.
DR EMBL; AY339383; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339384; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339385; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339386; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339387; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339388; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339389; AAR11293.1; JOINED; Genomic_DNA.
DR EMBL; AY339389; AAR11294.1; -; Genomic_DNA.
DR EMBL; AY339383; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AY339384; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AY339385; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AY339386; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AY339387; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AY339388; AAR11294.1; JOINED; Genomic_DNA.
DR EMBL; AK038551; BAC30039.1; -; mRNA.
DR EMBL; AK048781; BAC33457.1; -; mRNA.
DR EMBL; AF394597; AAK71327.1; -; mRNA.
DR CCDS; CCDS23350.1; -. [P58308-1]
DR CCDS; CCDS90628.1; -. [P58308-2]
DR RefSeq; NP_945200.1; NM_198962.3. [P58308-1]
DR AlphaFoldDB; P58308; -.
DR SMR; P58308; -.
DR STRING; 10090.ENSMUSP00000058230; -.
DR BindingDB; P58308; -.
DR ChEMBL; CHEMBL2434818; -.
DR DrugCentral; P58308; -.
DR GlyGen; P58308; 3 sites.
DR PhosphoSitePlus; P58308; -.
DR SwissPalm; P58308; -.
DR PaxDb; P58308; -.
DR PRIDE; P58308; -.
DR ProteomicsDB; 294353; -. [P58308-1]
DR ProteomicsDB; 294354; -. [P58308-2]
DR Antibodypedia; 17332; 369 antibodies from 38 providers.
DR DNASU; 387285; -.
DR Ensembl; ENSMUST00000063140; ENSMUSP00000058230; ENSMUSG00000032360. [P58308-1]
DR Ensembl; ENSMUST00000184757; ENSMUSP00000139377; ENSMUSG00000032360. [P58308-2]
DR GeneID; 387285; -.
DR KEGG; mmu:387285; -.
DR UCSC; uc009qsz.1; mouse. [P58308-1]
DR CTD; 3062; -.
DR MGI; MGI:2680765; Hcrtr2.
DR VEuPathDB; HostDB:ENSMUSG00000032360; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; P58308; -.
DR OMA; AEVYPKM; -.
DR OrthoDB; 981089at2759; -.
DR PhylomeDB; P58308; -.
DR TreeFam; TF315303; -.
DR Reactome; R-MMU-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 387285; 2 hits in 60 CRISPR screens.
DR ChiTaRS; Hcrtr2; mouse.
DR PRO; PR:P58308; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58308; protein.
DR Bgee; ENSMUSG00000032360; Expressed in morula and 15 other tissues.
DR Genevisible; P58308; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0016499; F:orexin receptor activity; IDA:MGI.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0022410; P:circadian sleep/wake cycle process; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0040011; P:locomotion; IGI:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Orexin receptor type 2"
FT /id="PRO_0000069990"
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"
FT VAR_SEQ 444..460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15256537"
FT /id="VSP_016466"
FT CONFLICT 201
FT /note="A -> T (in Ref. 3; AAK71327)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="I -> V (in Ref. 3; AAK71327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 52461 MW; D62A67C15BA67DCC CRC64;
MSSTKLEDSL SRRNWSSASE LNETQEPFLN PTDYDDEEFL RYLWREYLHP KEYEWVLIAG
YIIVFVVALI GNVLVCVAVW KNHHMRTVTN YFIVNLSLAD VLVTITCLPA TLVVDITETW
FFGQSLCKVI PYLQTVSVSV SVLTLSCIAL DRWYAICHPL MFKSTAKRAR NSIVVIWIVS
CIIMIPQAIV MECSSMLPGL ANKTTLFTVC DEHWGGEVYP KMYHICFFLV TYMAPLCLMI
LAYLQIFRKL WCRQIPGTSS VVQRKWKQQQ PVSQPRGSGQ QSKARISAVA AEIKQIRARR
KTARMLMVVL LVFAICYLPI SILNVLKRVF GMFTHTEDRE TVYAWFTFSH WLVYANSAAN
PIIYNFLSGK FREEFKAAFS CCLGVHHRQG DRLARGRTST ESRKSLTTQI SNFDNVSKLS
EHVVLTSIST LPAANGAGPL QNWYLQQGVP SSLLSTWLEV
