HRH1_HUMAN
ID HRH1_HUMAN Reviewed; 487 AA.
AC P35367; A8K047; Q6P9E5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=HRH1;
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].
RX PubMed=8280179; DOI=10.1006/bbrc.1993.2662;
RA de Backer M.D., Gommeren W., Moereels H., Nobels G., van Gompel P.,
RA Leysen J.E., Luyten W.H.M.L.;
RT "Genomic cloning, heterologous expression and pharmacological
RT characterization of a human histamine H1 receptor.";
RL Biochem. Biophys. Res. Commun. 197:1601-1608(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8003029; DOI=10.1006/bbrc.1994.1786;
RA Fukui K., Fujimoto K., Mizuguchi H., Sakamoto K., Horio Y., Takai S.,
RA Yamada K., Ito S.;
RT "Molecular cloning of the human histamine H1 receptor gene.";
RL Biochem. Biophys. Res. Commun. 201:894-901(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7925364; DOI=10.1111/j.1432-1033.1994.00489.x;
RA Moguilevsky N., Varsalona F., Noyer M., Gillard M., Guillaume J.P.,
RA Garcia L., Szpirer C., Szpirer J., Bollen A.;
RT "Stable expression of human H1-histamine-receptor cDNA in Chinese hamster
RT ovary cells. Pharmacological characterisation of the protein, tissue
RT distribution of messenger RNA and chromosomal localisation of the gene.";
RL Eur. J. Biochem. 224:489-495(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [10]
RP PHOSPHORYLATION AT THR-140; THR-142; SER-396 AND SER-398.
RX PubMed=15328002; DOI=10.1016/j.febslet.2004.07.072;
RA Horio S., Kato T., Ogawa M., Fujimoto K., Fukui H.;
RT "Two threonine residues and two serine residues in the second and third
RT intracellular loops are both involved in histamine H1 receptor
RT downregulation.";
RL FEBS Lett. 573:226-230(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 20-487 IN COMPLEX WITH ANTAGONIST,
RP DISULFIDE BOND, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21697825; DOI=10.1038/nature10236;
RA Shimamura T., Shiroishi M., Weyand S., Tsujimoto H., Winter G.,
RA Katritch V., Abagyan R., Cherezov V., Liu W., Han G.W., Kobayashi T.,
RA Stevens R.C., Iwata S.;
RT "Structure of the human histamine H1 receptor complex with doxepin.";
RL Nature 475:65-70(2011).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-385.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: In peripheral tissues, the H1 subclass of histamine receptors
CC mediates the contraction of smooth muscles, increase in capillary
CC permeability due to contraction of terminal venules, and catecholamine
CC release from adrenal medulla, as well as mediating neurotransmission in
CC the central nervous system.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21697825};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21697825}.
CC -!- PTM: Phosphorylation at sites in the second and third cytoplasmic loops
CC independently contribute to agonist-induced receptor down-regulation.
CC {ECO:0000269|PubMed:15328002}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z34897; CAA84380.1; -; mRNA.
DR EMBL; X76786; CAA54182.1; -; Genomic_DNA.
DR EMBL; D14436; BAA03319.1; -; Genomic_DNA.
DR EMBL; D28481; BAA05840.1; -; mRNA.
DR EMBL; AF026261; AAB95156.1; -; mRNA.
DR EMBL; AB041380; BAA94465.1; -; Genomic_DNA.
DR EMBL; AY136743; AAN01269.1; -; mRNA.
DR EMBL; AK289412; BAF82101.1; -; mRNA.
DR EMBL; CH471055; EAW64092.1; -; Genomic_DNA.
DR EMBL; BC060802; AAH60802.1; -; mRNA.
DR CCDS; CCDS2604.1; -.
DR PIR; JC2495; JC2495.
DR RefSeq; NP_000852.1; NM_000861.3.
DR RefSeq; NP_001091681.1; NM_001098211.1.
DR RefSeq; NP_001091682.1; NM_001098212.1.
DR RefSeq; NP_001091683.1; NM_001098213.1.
DR RefSeq; XP_011531954.1; XM_011533652.1.
DR RefSeq; XP_011531955.1; XM_011533653.2.
DR RefSeq; XP_016861772.1; XM_017006283.1.
DR RefSeq; XP_016861773.1; XM_017006284.1.
DR PDB; 3RZE; X-ray; 3.10 A; A=20-221, A=405-487.
DR PDB; 7DFL; EM; 3.30 A; R=1-487.
DR PDBsum; 3RZE; -.
DR PDBsum; 7DFL; -.
DR AlphaFoldDB; P35367; -.
DR SMR; P35367; -.
DR BioGRID; 109505; 15.
DR DIP; DIP-41996N; -.
DR IntAct; P35367; 15.
DR MINT; P35367; -.
DR STRING; 9606.ENSP00000380247; -.
DR BindingDB; P35367; -.
DR ChEMBL; CHEMBL231; -.
DR DrugBank; DB01615; Aceprometazine.
DR DrugBank; DB09488; Acrivastine.
DR DrugBank; DB06766; Alcaftadine.
DR DrugBank; DB01246; Alimemazine.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB08799; Antazoline.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB00637; Astemizole.
DR DrugBank; DB00719; Azatadine.
DR DrugBank; DB00972; Azelastine.
DR DrugBank; DB00245; Benzatropine.
DR DrugBank; DB00767; Benzquinamide.
DR DrugBank; DB04890; Bepotastine.
DR DrugBank; DB06698; Betahistine.
DR DrugBank; DB11591; Bilastine.
DR DrugBank; DB01237; Bromodiphenhydramine.
DR DrugBank; DB00835; Brompheniramine.
DR DrugBank; DB00354; Buclizine.
DR DrugBank; DB09016; Butriptyline.
DR DrugBank; DB00748; Carbinoxamine.
DR DrugBank; DB06016; Cariprazine.
DR DrugBank; DB00341; Cetirizine.
DR DrugBank; DB08936; Chlorcyclizine.
DR DrugBank; DB08800; Chloropyramine.
DR DrugBank; DB01114; Chlorpheniramine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB00215; Citalopram.
DR DrugBank; DB00283; Clemastine.
DR DrugBank; DB04837; Clofedanol.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB01176; Cyclizine.
DR DrugBank; DB00434; Cyproheptadine.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB00967; Desloratadine.
DR DrugBank; DB00405; Dexbrompheniramine.
DR DrugBank; DB09555; Dexchlorpheniramine maleate.
DR DrugBank; DB00985; Dimenhydrinate.
DR DrugBank; DB08801; Dimetindene.
DR DrugBank; DB01075; Diphenhydramine.
DR DrugBank; DB01146; Diphenylpyraline.
DR DrugBank; DB09167; Dosulepin.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB00366; Doxylamine.
DR DrugBank; DB01084; Emedastine.
DR DrugBank; DB05492; Epicept NP-1.
DR DrugBank; DB00751; Epinastine.
DR DrugBank; DB01175; Escitalopram.
DR DrugBank; DB06678; Esmirtazapine.
DR DrugBank; DB00950; Fexofenadine.
DR DrugBank; DB04841; Flunarizine.
DR DrugBank; DB00502; Haloperidol.
DR DrugBank; DB05381; Histamine.
DR DrugBank; DB05079; HY10275.
DR DrugBank; DB00557; Hydroxyzine.
DR DrugBank; DB04946; Iloperidone.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB08802; Isothipendyl.
DR DrugBank; DB00920; Ketotifen.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB01106; Levocabastine.
DR DrugBank; DB06282; Levocetirizine.
DR DrugBank; DB00455; Loratadine.
DR DrugBank; DB09195; Lorpiprazole.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB00934; Maprotiline.
DR DrugBank; DB00737; Meclizine.
DR DrugBank; DB06691; Mepyramine.
DR DrugBank; DB01071; Mequitazine.
DR DrugBank; DB00902; Methdilazine.
DR DrugBank; DB01403; Methotrimeprazine.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB00370; Mirtazapine.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB05080; OBE101.
DR DrugBank; DB06229; Ocaperidone.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB00768; Olopatadine.
DR DrugBank; DB01173; Orphenadrine.
DR DrugBank; DB01267; Paliperidone.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB08922; Perospirone.
DR DrugBank; DB01619; Phenindamine.
DR DrugBank; DB01620; Pheniramine.
DR DrugBank; DB06153; Pizotifen.
DR DrugBank; DB00433; Prochlorperazine.
DR DrugBank; DB00420; Promazine.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB00777; Propiomazine.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB11614; Rupatadine.
DR DrugBank; DB05345; SO-101.
DR DrugBank; DB00342; Terfenadine.
DR DrugBank; DB04905; Tesmilifene.
DR DrugBank; DB11235; Thonzylamine.
DR DrugBank; DB00797; Tolazoline.
DR DrugBank; DB00656; Trazodone.
DR DrugBank; DB00726; Trimipramine.
DR DrugBank; DB00792; Tripelennamine.
DR DrugBank; DB00427; Triprolidine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB01624; Zuclopenthixol.
DR DrugCentral; P35367; -.
DR GuidetoPHARMACOLOGY; 262; -.
DR GlyGen; P35367; 2 sites.
DR iPTMnet; P35367; -.
DR PhosphoSitePlus; P35367; -.
DR BioMuta; HRH1; -.
DR DMDM; 547645; -.
DR EPD; P35367; -.
DR jPOST; P35367; -.
DR MassIVE; P35367; -.
DR MaxQB; P35367; -.
DR PaxDb; P35367; -.
DR PeptideAtlas; P35367; -.
DR PRIDE; P35367; -.
DR ProteomicsDB; 55036; -.
DR Antibodypedia; 10679; 552 antibodies from 38 providers.
DR DNASU; 3269; -.
DR Ensembl; ENST00000397056.1; ENSP00000380247.1; ENSG00000196639.7.
DR Ensembl; ENST00000431010.3; ENSP00000397028.2; ENSG00000196639.7.
DR Ensembl; ENST00000438284.2; ENSP00000406705.2; ENSG00000196639.7.
DR GeneID; 3269; -.
DR KEGG; hsa:3269; -.
DR MANE-Select; ENST00000431010.3; ENSP00000397028.2; NM_001098212.2; NP_001091682.1.
DR UCSC; uc003bwb.5; human.
DR CTD; 3269; -.
DR DisGeNET; 3269; -.
DR GeneCards; HRH1; -.
DR HGNC; HGNC:5182; HRH1.
DR HPA; ENSG00000196639; Tissue enhanced (urinary).
DR MIM; 600167; gene.
DR neXtProt; NX_P35367; -.
DR OpenTargets; ENSG00000196639; -.
DR PharmGKB; PA29456; -.
DR VEuPathDB; HostDB:ENSG00000196639; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000160690; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P35367; -.
DR OMA; YVAINQS; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P35367; -.
DR TreeFam; TF333432; -.
DR PathwayCommons; P35367; -.
DR Reactome; R-HSA-390650; Histamine receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P35367; -.
DR SIGNOR; P35367; -.
DR BioGRID-ORCS; 3269; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; HRH1; human.
DR GeneWiki; Histamine_H1_receptor; -.
DR GenomeRNAi; 3269; -.
DR Pharos; P35367; Tclin.
DR PRO; PR:P35367; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P35367; protein.
DR Bgee; ENSG00000196639; Expressed in cartilage tissue and 164 other tissues.
DR ExpressionAtlas; P35367; baseline and differential.
DR Genevisible; P35367; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0004969; F:histamine receptor activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048245; P:eosinophil chemotaxis; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISS:BHF-UCL.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000921; Histamine_H1_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00530; HISTAMINEH1R.
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; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..487
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069676"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 30..52
FT /note="Helical; Name=1"
FT TOPO_DOM 53..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT TOPO_DOM 84..101
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT TOPO_DOM 124..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT TOPO_DOM 211..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 417..438
FT /note="Helical; Name=6"
FT TOPO_DOM 439..450
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21697825"
FT TRANSMEM 451..470
FT /note="Helical; Name=7"
FT TOPO_DOM 471..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21697825"
FT REGION 107..112
FT /note="Important for agonist binding"
FT REGION 238..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..428
FT /note="Important for agonist binding"
FT COMPBIAS 240..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15328002"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15328002"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15328002"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15328002"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:21697825"
FT DISULFID 441..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:21697825"
FT VARIANT 19
FT /note="K -> N (in dbSNP:rs2067466)"
FT /id="VAR_049410"
FT VARIANT 270
FT /note="G -> E (in dbSNP:rs7651620)"
FT /id="VAR_033476"
FT VARIANT 385
FT /note="D -> E (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1370695377)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035761"
FT CONFLICT 308
FT /note="V -> E (in Ref. 9; AAH60802)"
FT /evidence="ECO:0000305"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 33..54
FT /evidence="ECO:0007829|PDB:3RZE"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7DFL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:3RZE"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 96..130
FT /evidence="ECO:0007829|PDB:3RZE"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:7DFL"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 408..441
FT /evidence="ECO:0007829|PDB:3RZE"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:7DFL"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 450..471
FT /evidence="ECO:0007829|PDB:3RZE"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:3RZE"
SQ SEQUENCE 487 AA; 55784 MW; E5DB418A4C17A985 CRC64;
MSLPNSSCLL EDKMCEGNKT TMASPQLMPL VVVLSTICLV TVGLNLLVLY AVRSERKLHT
VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC LFWLSMDYVA STASIFSVFI
LCIDRYRSVQ QPLRYLKYRT KTRASATILG AWFLSFLWVI PILGWNHFMQ QTSVRREDKC
ETDFYDVTWF KVMTAIINFY LPTLLMLWFY AKIYKAVRQH CQHRELINRS LPSFSEIKLR
PENPKGDAKK PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDREVDKL
YCFPLDIVHM QAAAEGSSRD YVAVNRSHGQ LKTDEQGLNT HGASEISEDQ MLGDSQSFSR
TDSDTTTETA PGKGKLRSGS NTGLDYIKFT WKRLRSHSRQ YVSGLHMNRE RKAAKQLGFI
MAAFILCWIP YFIFFMVIAF CKNCCNEHLH MFTIWLGYIN STLNPLIYPL CNENFKKTFK
RILHIRS
