OX1R_MOUSE
ID OX1R_MOUSE Reviewed; 416 AA.
AC P58307; Q0VDP5; Q3USS9; Q6VNS3; Q80T45;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Orexin/Hypocretin receptor type 1 {ECO:0000305|PubMed:11340621};
DE AltName: Full=Hypocretin receptor type 1 {ECO:0000312|MGI:MGI:2385650};
DE AltName: Full=Orexin receptor type 1 {ECO:0000305|PubMed:15256537};
DE Short=Ox-1-R;
DE Short=Ox1-R;
DE Short=Ox1R;
GN Name=Hcrtr1 {ECO:0000312|MGI:MGI:2385650};
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], 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].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-393.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-339.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [7]
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 [8]
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: Moderately selective excitatory receptor for orexin-A and,
CC with a lower affinity, for orexin-B neuropeptide. Triggers an increase
CC in cytoplasmic Ca(2+) levels in response to orexin-A binding.
CC {ECO:0000250|UniProtKB:O43613}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43613};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O43613}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15256537}.
CC -!- DOMAIN: The N-terminal region is required for orexin signaling.
CC {ECO:0000250|UniProtKB:O43613}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY336083; AAR01326.1; -; mRNA.
DR EMBL; AK140137; BAE24252.1; -; mRNA.
DR EMBL; AL606925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU207372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119583; AAI19584.1; -; mRNA.
DR EMBL; AF394596; AAK71326.1; -; mRNA.
DR EMBL; AY255599; AAO85111.1; -; mRNA.
DR CCDS; CCDS18707.1; -.
DR RefSeq; NP_001156499.1; NM_001163027.1.
DR RefSeq; NP_945197.2; NM_198959.2.
DR RefSeq; XP_017175645.1; XM_017320156.1.
DR RefSeq; XP_017175646.1; XM_017320157.1.
DR AlphaFoldDB; P58307; -.
DR SMR; P58307; -.
DR STRING; 10090.ENSMUSP00000112630; -.
DR BindingDB; P58307; -.
DR ChEMBL; CHEMBL2434819; -.
DR DrugCentral; P58307; -.
DR GlyGen; P58307; 1 site.
DR iPTMnet; P58307; -.
DR PhosphoSitePlus; P58307; -.
DR PaxDb; P58307; -.
DR PRIDE; P58307; -.
DR Antibodypedia; 2934; 415 antibodies from 38 providers.
DR DNASU; 230777; -.
DR Ensembl; ENSMUST00000030562; ENSMUSP00000030562; ENSMUSG00000028778.
DR Ensembl; ENSMUST00000119423; ENSMUSP00000112630; ENSMUSG00000028778.
DR Ensembl; ENSMUST00000120154; ENSMUSP00000113198; ENSMUSG00000028778.
DR Ensembl; ENSMUST00000164887; ENSMUSP00000127290; ENSMUSG00000028778.
DR GeneID; 230777; -.
DR KEGG; mmu:230777; -.
DR UCSC; uc008uyx.1; mouse.
DR CTD; 3061; -.
DR MGI; MGI:2385650; Hcrtr1.
DR VEuPathDB; HostDB:ENSMUSG00000028778; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; P58307; -.
DR OMA; VMECRSV; -.
DR OrthoDB; 981089at2759; -.
DR PhylomeDB; P58307; -.
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; 230777; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Hcrtr1; mouse.
DR PRO; PR:P58307; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P58307; protein.
DR Bgee; ENSMUSG00000028778; Expressed in substantia nigra and 28 other tissues.
DR Genevisible; P58307; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016499; F:orexin receptor activity; ISS:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
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; IPR004059; OX1R.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01521; OREXIN1R.
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..416
FT /note="Orexin/Hypocretin receptor type 1"
FT /id="PRO_0000069985"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 68..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 83..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 106..119
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 161..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 183..213
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 214..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 236..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 299..321
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 322..336
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TRANSMEM 337..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT TOPO_DOM 361..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..41
FT /note="Required for response to orexin-A"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT SITE 36
FT /note="Important for responses to orexin"
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..202
FT /evidence="ECO:0000250|UniProtKB:O43613"
FT CONFLICT 139
FT /note="F -> V (in Ref. 5; AAK71326)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> G (in Ref. 1; AAR01326, 5; AAK71326 and 6;
FT AAO85111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46781 MW; AB338FFCEF905E06 CRC64;
MEPSATPGAQ PGVPTSSGEP FHLPPDYEDE FLRYLWRDYL YPKQYEWVLI AAYVAVFLIA
LVGNTLVCLA VWRNHHMRTV TNYFIVNLSL ADVLVTAICL PASLLVDITE SWLFGQALCK
VIPYLQAVSV SVAVLTLSFI ALDRWYAICH PLLFKSTARR ARGSILGIWA VSLAVMVPQA
AVMECSSVLP ELANRTRLFS VCDEHWADEL YPKIYHSCFF IVTYLAPLGL MAMAYFQIFR
KLWGRQIPGT TSALVRNWKR PSEQLEAQHQ GLCTEPQPRA RAFLAEVKQM RARRKTAKML
MVVLLVFALC YLPISVLNVL KRVFGMFRQA SDREAVYACF TFSHWLVYAN SAANPIIYNF
LSGKFREQFK AAFSCCLPGL GPGSSARHKS LSLQSRCSVS KVSEHVVLTT VTTVLS
