OX1R_HUMAN
ID OX1R_HUMAN Reviewed; 425 AA.
AC O43613; A8K3A6; Q9HBV6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Orexin/Hypocretin receptor type 1 {ECO:0000305|PubMed:11723285};
DE AltName: Full=Hypocretin receptor type 1 {ECO:0000312|HGNC:HGNC:4848};
DE AltName: Full=Orexin receptor type 1 {ECO:0000305|PubMed:9491897};
DE Short=Ox-1-R;
DE Short=Ox1-R;
DE Short=Ox1R;
GN Name=HCRTR1 {ECO:0000312|HGNC:HGNC:4848};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10973318; DOI=10.1038/79690;
RA Peyron C., Faraco J., Rogers W., Ripley B., Overeem S., Charnay Y.,
RA Nevsimalova S., Aldrich M., Reynolds D., Albin R., Li R., Hungs M.,
RA Pedrazzoli M., Padigaru M., Kucherlapati M., Fan J., Maki R., Lammers G.J.,
RA Bouras C., Kucherlapati R., Nishino S., Mignot E.;
RT "A mutation in a case of early onset narcolepsy and a generalized absence
RT of hypocretin peptides in human narcoleptic brains.";
RL Nat. Med. 6:991-997(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-167; GLN-279; HIS-281
RP AND VAL-408.
RX PubMed=11723285; DOI=10.1212/wnl.57.10.1896;
RA Olafsdottir B.R., Rye D.B., Scammell T.E., Matheson J.K., Stefansson K.,
RA Gulcher J.R.;
RT "Polymorphisms in hypocretin/orexin pathway genes and narcolepsy.";
RL Neurology 57:1896-1899(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yeager M., Welch R., Haque K., Bergen A.;
RT "Genomic sequence of the hypocretin (orexin) receptor 1 (HCRTR1).";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-408.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
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 [10]
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).
RN [11] {ECO:0007744|PDB:4ZJ8, ECO:0007744|PDB:4ZJC}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-246 AND 288-380 IN COMPLEXES
RP WITH THE ANTAGONISTS SUVOREXANT AND SB-674042, DISULFIDE BONDS, FUNCTION,
RP SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF 26-ASP--TYR-41; TRP-36 AND
RP ASN-318, AND DOMAIN.
RX PubMed=26950369; DOI=10.1038/nsmb.3183;
RA Yin J., Babaoglu K., Brautigam C.A., Clark L., Shao Z., Scheuermann T.H.,
RA Harrell C.M., Gotter A.L., Roecker A.J., Winrow C.J., Renger J.J.,
RA Coleman P.J., Rosenbaum D.M.;
RT "Structure and ligand-binding mechanism of the human OX1 and OX2 orexin
RT receptors.";
RL Nat. Struct. Mol. Biol. 23:293-299(2016).
CC -!- FUNCTION: Moderately selective excitatory receptor for orexin-A and,
CC with a lower affinity, for orexin-B neuropeptide (PubMed:9491897,
CC PubMed:26950369). Triggers an increase in cytoplasmic Ca(2+) levels in
CC response to orexin-A binding (PubMed:9491897, PubMed:26950369).
CC {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26950369,
CC ECO:0000269|PubMed:9491897}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26950369}.
CC -!- DOMAIN: The N-terminal region is required for orexin signaling.
CC {ECO:0000269|PubMed:26950369}.
CC -!- MISCELLANEOUS: The antagonists suvorexant and SB-674042 bind at the
CC cognate neuropeptide binding site that is situated between the
CC transmembrane helices and accessible from the extracellular side of the
CC membrane. {ECO:0000269|PubMed:26950369}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF041243; AAC39601.1; -; mRNA.
DR EMBL; AF202084; AAG28020.1; -; Genomic_DNA.
DR EMBL; AF202078; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AF202079; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AF202080; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AF202081; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AF202082; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AF202083; AAG28020.1; JOINED; Genomic_DNA.
DR EMBL; AY062030; AAL47214.1; -; Genomic_DNA.
DR EMBL; AY070269; AAL50221.1; -; Genomic_DNA.
DR EMBL; AK290521; BAF83210.1; -; mRNA.
DR EMBL; AC114488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07602.1; -; Genomic_DNA.
DR EMBL; BC074796; AAH74796.1; -; mRNA.
DR CCDS; CCDS344.1; -.
DR RefSeq; NP_001516.2; NM_001525.2.
DR RefSeq; XP_016856594.1; XM_017001105.1.
DR RefSeq; XP_016856595.1; XM_017001106.1.
DR PDB; 4ZJ8; X-ray; 2.75 A; A=1-246, A=288-380.
DR PDB; 4ZJC; X-ray; 2.83 A; A=1-246, A=288-380.
DR PDB; 6TO7; X-ray; 2.26 A; A/B=28-380.
DR PDB; 6TOD; X-ray; 2.11 A; A/B=28-380.
DR PDB; 6TOS; X-ray; 2.13 A; A/B=28-380.
DR PDB; 6TOT; X-ray; 2.22 A; A/B=28-380.
DR PDB; 6TP3; X-ray; 3.04 A; A/B=28-380.
DR PDB; 6TP4; X-ray; 3.01 A; A/B=28-380.
DR PDB; 6TP6; X-ray; 2.34 A; A/B=28-380.
DR PDB; 6TQ4; X-ray; 2.30 A; A/B=28-380.
DR PDB; 6TQ6; X-ray; 2.55 A; A/B=28-380.
DR PDB; 6TQ7; X-ray; 2.66 A; A/B=28-380.
DR PDB; 6TQ9; X-ray; 2.65 A; A/B=28-381.
DR PDB; 6V9S; X-ray; 3.50 A; A=1-246, A=288-380.
DR PDBsum; 4ZJ8; -.
DR PDBsum; 4ZJC; -.
DR PDBsum; 6TO7; -.
DR PDBsum; 6TOD; -.
DR PDBsum; 6TOS; -.
DR PDBsum; 6TOT; -.
DR PDBsum; 6TP3; -.
DR PDBsum; 6TP4; -.
DR PDBsum; 6TP6; -.
DR PDBsum; 6TQ4; -.
DR PDBsum; 6TQ6; -.
DR PDBsum; 6TQ7; -.
DR PDBsum; 6TQ9; -.
DR PDBsum; 6V9S; -.
DR AlphaFoldDB; O43613; -.
DR SMR; O43613; -.
DR BioGRID; 109311; 6.
DR ELM; O43613; -.
DR IntAct; O43613; 2.
DR STRING; 9606.ENSP00000384387; -.
DR BindingDB; O43613; -.
DR ChEMBL; CHEMBL5113; -.
DR DrugBank; DB11951; Lemborexant.
DR DrugBank; DB09034; Suvorexant.
DR DrugCentral; O43613; -.
DR GuidetoPHARMACOLOGY; 321; -.
DR GlyGen; O43613; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O43613; -.
DR PhosphoSitePlus; O43613; -.
DR BioMuta; HCRTR1; -.
DR PaxDb; O43613; -.
DR PeptideAtlas; O43613; -.
DR PRIDE; O43613; -.
DR ProteomicsDB; 49081; -.
DR Antibodypedia; 2934; 415 antibodies from 38 providers.
DR DNASU; 3061; -.
DR Ensembl; ENST00000373706.9; ENSP00000362810.5; ENSG00000121764.12.
DR Ensembl; ENST00000403528.7; ENSP00000384387.2; ENSG00000121764.12.
DR GeneID; 3061; -.
DR KEGG; hsa:3061; -.
DR MANE-Select; ENST00000403528.7; ENSP00000384387.2; NM_001525.3; NP_001516.2.
DR UCSC; uc001btd.3; human.
DR CTD; 3061; -.
DR DisGeNET; 3061; -.
DR GeneCards; HCRTR1; -.
DR HGNC; HGNC:4848; HCRTR1.
DR HPA; ENSG00000121764; Tissue enhanced (brain).
DR MIM; 602392; gene.
DR neXtProt; NX_O43613; -.
DR OpenTargets; ENSG00000121764; -.
DR PharmGKB; PA29222; -.
DR VEuPathDB; HostDB:ENSG00000121764; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_3_1; -.
DR InParanoid; O43613; -.
DR OMA; VMECRSV; -.
DR OrthoDB; 981089at2759; -.
DR PhylomeDB; O43613; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; O43613; -.
DR Reactome; R-HSA-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; O43613; -.
DR SIGNOR; O43613; -.
DR BioGRID-ORCS; 3061; 149 hits in 1062 CRISPR screens.
DR ChiTaRS; HCRTR1; human.
DR GeneWiki; Hypocretin_(orexin)_receptor_1; -.
DR GenomeRNAi; 3061; -.
DR Pharos; O43613; Tclin.
DR PRO; PR:O43613; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43613; protein.
DR Bgee; ENSG00000121764; Expressed in apex of heart and 99 other tissues.
DR ExpressionAtlas; O43613; baseline and differential.
DR Genevisible; O43613; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016499; F:orexin receptor activity; IDA:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA: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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..425
FT /note="Orexin/Hypocretin receptor type 1"
FT /id="PRO_0000069984"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 68..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 83..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 106..119
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 141..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 161..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 183..213
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 214..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 236..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 299..321
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 322..336
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TRANSMEM 337..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:26950369"
FT TOPO_DOM 361..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26950369"
FT REGION 1..24
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:0000269|PubMed:26950369"
FT BINDING 318
FT /ligand="suvorexant"
FT /ligand_id="ChEBI:CHEBI:82698"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:26950369,
FT ECO:0007744|PDB:4ZJ8"
FT SITE 36
FT /note="Important for responses to orexin"
FT /evidence="ECO:0000269|PubMed:26950369"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..202
FT /evidence="ECO:0007744|PDB:4ZJ8, ECO:0007744|PDB:4ZJC"
FT VARIANT 167
FT /note="G -> S (in dbSNP:rs144603792)"
FT /evidence="ECO:0000269|PubMed:11723285"
FT /id="VAR_044505"
FT VARIANT 279
FT /note="R -> Q (in dbSNP:rs7516785)"
FT /evidence="ECO:0000269|PubMed:11723285"
FT /id="VAR_033480"
FT VARIANT 281
FT /note="R -> H (in dbSNP:rs41439244)"
FT /evidence="ECO:0000269|PubMed:11723285"
FT /id="VAR_044506"
FT VARIANT 408
FT /note="I -> V (in dbSNP:rs2271933)"
FT /evidence="ECO:0000269|PubMed:11723285,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_022063"
FT MUTAGEN 26..41
FT /note="Missing: Abolishes response to orexin-A."
FT /evidence="ECO:0000269|PubMed:26950369"
FT MUTAGEN 36
FT /note="W->A: Strongly impairs response to orexin-A."
FT /evidence="ECO:0000269|PubMed:26950369"
FT MUTAGEN 318
FT /note="N->A: Strongly impairs response to orexin-A."
FT /evidence="ECO:0000269|PubMed:26950369"
FT CONFLICT 280
FT /note="A -> G (in Ref. 1; AAC39601)"
FT /evidence="ECO:0000305"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 80..109
FT /evidence="ECO:0007829|PDB:6TOD"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6TP6"
FT HELIX 115..149
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4ZJ8"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6TOD"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6TOD"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6TOD"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6TOD"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 287..322
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 333..361
FT /evidence="ECO:0007829|PDB:6TOD"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:6TOD"
SQ SEQUENCE 425 AA; 47536 MW; B650B37F3A2CA096 CRC64;
MEPSATPGAQ MGVPPGSREP SPVPPDYEDE FLRYLWRDYL YPKQYEWVLI AAYVAVFVVA
LVGNTLVCLA VWRNHHMRTV TNYFIVNLSL ADVLVTAICL PASLLVDITE SWLFGHALCK
VIPYLQAVSV SVAVLTLSFI ALDRWYAICH PLLFKSTARR ARGSILGIWA VSLAIMVPQA
AVMECSSVLP ELANRTRLFS VCDERWADDL YPKIYHSCFF IVTYLAPLGL MAMAYFQIFR
KLWGRQIPGT TSALVRNWKR PSDQLGDLEQ GLSGEPQPRA RAFLAEVKQM RARRKTAKML
MVVLLVFALC YLPISVLNVL KRVFGMFRQA SDREAVYACF TFSHWLVYAN SAANPIIYNF
LSGKFREQFK AAFSCCLPGL GPCGSLKAPS PRSSASHKSL SLQSRCSISK ISEHVVLTSV
TTVLP
