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   27-MAR-2024, entry version 198.
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   EMDB; EMD-30665; -.
DR   SMR; P35367; -.
DR   BioGRID; 109505; 16.
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; DB00912; Repaglinide.
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; DB09185; Viloxazine.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugBank; DB01624; Zuclopenthixol.
DR   DrugCentral; P35367; -.
DR   GuidetoPHARMACOLOGY; 262; -.
DR   GlyCosmos; P35367; 2 sites, No reported glycans.
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; 9606-ENSP00000380247; -.
DR   PeptideAtlas; P35367; -.
DR   ProteomicsDB; 55036; -.
DR   Antibodypedia; 10679; 607 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   AGR; HGNC:5182; -.
DR   CTD; 3269; -.
DR   DisGeNET; 3269; -.
DR   GeneCards; HRH1; -.
DR   HGNC; HGNC:5182; HRH1.
DR   HPA; ENSG00000196639; Low tissue specificity.
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; 4136179at2759; -.
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 1162 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 166 other cell types or tissues.
DR   ExpressionAtlas; P35367; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
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: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; 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; 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   CDD; cd15050; 7tmA_Histamine_H1R; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000921; Histamine_H1_rcpt.
DR   PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR   PANTHER; PTHR24247:SF195; HISTAMINE H1 RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00530; HISTAMINEH1R.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P35367; HS.
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
//