ID HRH2_MOUSE Reviewed; 397 AA. AC P97292; Q9D282; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-OCT-2013, sequence version 2. DT 27-MAR-2024, entry version 159. DE RecName: Full=Histamine H2 receptor; DE Short=H2R; DE Short=HH2R; DE AltName: Full=Gastric receptor I; GN Name=Hrh2; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cecum, and Corpus striatum; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-358. RC STRAIN=129/Ola; RX PubMed=8938453; DOI=10.1006/geno.1996.0575; RA Kobayashi T., Inoue I., Jenkins N.A., Gilbert D.J., Copeland N.G., RA Watanabe T.; RT "Cloning, RNA expression, and chromosomal location of a mouse histamine H2 RT receptor gene."; RL Genomics 37:390-394(1996). CC -!- FUNCTION: The H2 subclass of histamine receptors mediates gastric acid CC secretion. The activity of this receptor is mediated by G proteins CC which activate adenylyl cyclase. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK020259; BAB32044.1; -; mRNA. DR EMBL; AK163760; BAE37484.1; -; mRNA. DR EMBL; AC163343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC164086; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D50096; BAA08792.1; -; Genomic_DNA. DR CCDS; CCDS26526.1; -. DR RefSeq; NP_001010973.1; NM_001010973.2. DR RefSeq; NP_032312.2; NM_008286.2. DR RefSeq; XP_006516915.1; XM_006516852.2. DR RefSeq; XP_017170886.1; XM_017315397.1. DR AlphaFoldDB; P97292; -. DR SMR; P97292; -. DR STRING; 10090.ENSMUSP00000038170; -. DR BindingDB; P97292; -. DR ChEMBL; CHEMBL2245; -. DR GlyCosmos; P97292; 1 site, No reported glycans. DR GlyGen; P97292; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P97292; -. DR PhosphoSitePlus; P97292; -. DR PaxDb; 10090-ENSMUSP00000038170; -. DR ProteomicsDB; 267158; -. DR Antibodypedia; 2931; 370 antibodies from 39 providers. DR DNASU; 15466; -. DR Ensembl; ENSMUST00000038101.4; ENSMUSP00000038170.4; ENSMUSG00000034987.5. DR GeneID; 15466; -. DR KEGG; mmu:15466; -. DR UCSC; uc007qob.1; mouse. DR AGR; MGI:108482; -. DR CTD; 3274; -. DR MGI; MGI:108482; Hrh2. DR VEuPathDB; HostDB:ENSMUSG00000034987; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000158761; -. DR HOGENOM; CLU_009579_11_0_1; -. DR InParanoid; P97292; -. DR OMA; SQKRMDF; -. DR OrthoDB; 2900736at2759; -. DR PhylomeDB; P97292; -. DR TreeFam; TF316350; -. DR Reactome; R-MMU-390650; Histamine receptors. DR Reactome; R-MMU-418555; G alpha (s) signalling events. DR BioGRID-ORCS; 15466; 2 hits in 78 CRISPR screens. DR ChiTaRS; Dhx15; mouse. DR PRO; PR:P97292; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P97292; Protein. DR Bgee; ENSMUSG00000034987; Expressed in granulocyte and 41 other cell types or tissues. DR ExpressionAtlas; P97292; baseline and differential. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:1901363; F:heterocyclic compound binding; ISO:MGI. DR GO; GO:0004969; F:histamine receptor activity; ISO:MGI. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0048565; P:digestive tract development; IMP:MGI. DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central. DR GO; GO:0001696; P:gastric acid secretion; IGI:MGI. DR GO; GO:0001698; P:gastrin-induced gastric acid secretion; IMP:MGI. DR GO; GO:0048732; P:gland development; IMP:MGI. DR GO; GO:0001697; P:histamine-induced gastric acid secretion; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:1900139; P:negative regulation of arachidonic acid secretion; ISO:MGI. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro. DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI. DR GO; GO:0008542; P:visual learning; IMP:MGI. DR CDD; cd15051; 7tmA_Histamine_H2R; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR000503; Histamine_H2_rcpt. DR PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1. DR PANTHER; PTHR24247:SF276; HISTAMINE H2 RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00531; HISTAMINEH2R. 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; P97292; MM. PE 2: Evidence at transcript level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..397 FT /note="Histamine H2 receptor" FT /id="PRO_0000069685" FT TOPO_DOM 1..22 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 23..44 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 45..57 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 58..81 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 82..92 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 93..114 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 115..134 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 135..159 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 160..179 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 180..203 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 204..233 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 234..257 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 258..266 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 267..288 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 289..397 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT SITE 98 FT /note="Essential for histamine binding" FT /evidence="ECO:0000250" FT SITE 185 FT /note="Essential for tiotidine binding and implicated in FT histamine binding" FT /evidence="ECO:0000250" FT SITE 189 FT /note="Implicated in histamine binding" FT /evidence="ECO:0000250" FT LIPID 304 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 4 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 91..173 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 85 FT /note="S -> R (in Ref. 3; BAA08792)" FT /evidence="ECO:0000305" FT CONFLICT 263 FT /note="A -> P (in Ref. 3; BAA08792)" FT /evidence="ECO:0000305" SQ SEQUENCE 397 AA; 44794 MW; BB4719084F4BDD59 CRC64; MEPNGTVHSC CLDSIALKVT ISVVLTTLIF ITVAGNVVVC LAVSLNRRLR SLTNCFIVSL AATDLLLGLL VMPFSAIYQL SFKWSFGQVF CNIYTSLDVM LCTASILNLF MISLDRYCAV TDPLRYPVLV TPVRVAISLV FIWVISITLS FLSIHLGWNS RNGTRGGNDT FKCKVQVNEV YGLVDGMVTF YLPLLIMCVT YYRIFKIARE QAKRINHISS WKAATIREHK ATVTLAAVMG AFIVCWFPYF TAFVYRGLRG DDAVNEVVEG IVLWLGYANS ALNPILYATL NRDFRMAYQQ LFHCKLASHN SHKTSLRLNN SLLSRSQSRE GRWQEEKPLK LQVWSGTELT HPQGSPVRTR LSHSSCLLSL SLLSFIWKLG TWIHHRRPFQ PSLHISA //