HRH1_MOUSE
ID HRH1_MOUSE Reviewed; 488 AA.
AC P70174; Q91V75; Q91XN0; Q91XN1; Q91XN2; Q91XN3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=Hrh1; Synonyms=Bphs;
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 [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=8812432; DOI=10.1006/geno.1996.0441;
RA Inoue I., Taniuchi I., Kitamura D., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Watanabe T.;
RT "Characteristics of the mouse genomic histamine H1 receptor gene.";
RL Genomics 36:178-181(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND VARIANTS LEU-263; MET-312 AND SER-330.
RC STRAIN=129/SvJ, A/J, B10.S/DvTe, BALB/cByJ, BALB/cJ, C3H/HeJ, C57BL/6J,
RC CBA/J, DBA/1, DBA/2J, FVB/NCr, NOD, SJL/J, and SWR; TISSUE=Spleen;
RX PubMed=12142541; DOI=10.1126/science.1072810;
RA Ma R.Z., Gao J., Meeker N.D., Fillmore P.D., Tung K.S.K., Watanabe T.,
RA Zachary J.F., Offner H., Blankenhorn E.P., Teuscher C.;
RT "Identification of Bphs, an autoimmune disease locus, as histamine receptor
RT H1.";
RL Science 297:620-623(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, Hypothalamus, and Mesonephros;
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 [4]
RP FUNCTION.
RX PubMed=8917588; DOI=10.1073/pnas.93.23.13316;
RA Inoue I., Yanai K., Kitamura D., Taniuchi I., Kobayashi T., Niimura K.,
RA Watanabe T., Watanabe T.;
RT "Impaired locomotor activity and exploratory behavior in mice lacking
RT histamine H1 receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13316-13320(1996).
RN [5]
RP FUNCTION.
RX PubMed=12595443; DOI=10.1128/iai.71.3.1281-1287.2003;
RA Gao J.F., Call S.B., Fillmore P.D., Watanabe T., Meeker N.D., Teuscher C.;
RT "Analysis of the role of Bphs/Hrh1 in the genetic control of responsiveness
RT to pertussis toxin.";
RL Infect. Immun. 71:1281-1287(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-347; SER-381 AND
RP SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Involved in circadian rhythm of locomotor
CC activity and exploratory behavior. Also involved in responsiveness to
CC pertussis toxin through its control of susceptibility to histamine
CC hypersensitivity and enhancement of antigen-specific delayed-type
CC hypersensitivity responses. {ECO:0000269|PubMed:12595443,
CC ECO:0000269|PubMed:8917588}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylation at sites in the second and third cytoplasmic loops
CC independently contribute to agonist-induced receptor down-regulation.
CC {ECO:0000250}.
CC -!- POLYMORPHISM: Strains C3H/HeJ and CBA/J are resistant to vasoactive
CC amine sensitization elicited by histamine (VAASH) which is induced by
CC pertussis toxin. {ECO:0000269|PubMed:12142541}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D50095; BAA08791.1; -; Genomic_DNA.
DR EMBL; AF387890; AAK71654.1; -; mRNA.
DR EMBL; AF387891; AAK71655.1; -; mRNA.
DR EMBL; AF387892; AAK71656.1; -; mRNA.
DR EMBL; AF387893; AAK71657.1; -; mRNA.
DR EMBL; AF387894; AAK71658.1; -; mRNA.
DR EMBL; AF387895; AAK71659.1; -; mRNA.
DR EMBL; AF387896; AAK71660.1; -; mRNA.
DR EMBL; AF388052; AAK66774.2; -; mRNA.
DR EMBL; AF388053; AAK66775.1; -; mRNA.
DR EMBL; AF388054; AAK66776.1; -; mRNA.
DR EMBL; AF388055; AAK66777.1; -; mRNA.
DR EMBL; AF388056; AAK66778.1; -; mRNA.
DR EMBL; AF388057; AAK66779.1; -; mRNA.
DR EMBL; AF388058; AAK66780.1; -; mRNA.
DR EMBL; AK032763; BAC28011.1; -; mRNA.
DR EMBL; AK038480; BAC30013.1; -; mRNA.
DR EMBL; AK046607; BAC32805.1; -; mRNA.
DR EMBL; AK047070; BAC32950.1; -; mRNA.
DR CCDS; CCDS20435.1; -.
DR RefSeq; NP_001239571.1; NM_001252642.2.
DR RefSeq; NP_001239572.1; NM_001252643.2.
DR RefSeq; NP_001304053.1; NM_001317124.1.
DR RefSeq; NP_001304054.1; NM_001317125.1.
DR RefSeq; NP_001304055.1; NM_001317126.1.
DR RefSeq; NP_032311.2; NM_008285.4.
DR AlphaFoldDB; P70174; -.
DR SMR; P70174; -.
DR STRING; 10090.ENSMUSP00000086383; -.
DR BindingDB; P70174; -.
DR ChEMBL; CHEMBL4322; -.
DR DrugBank; DB11160; Phenyltoloxamine.
DR DrugBank; DB00512; Vancomycin.
DR GlyGen; P70174; 2 sites.
DR iPTMnet; P70174; -.
DR PhosphoSitePlus; P70174; -.
DR jPOST; P70174; -.
DR MaxQB; P70174; -.
DR PaxDb; P70174; -.
DR PRIDE; P70174; -.
DR ProteomicsDB; 273382; -.
DR Antibodypedia; 10679; 552 antibodies from 38 providers.
DR DNASU; 15465; -.
DR Ensembl; ENSMUST00000088987; ENSMUSP00000086383; ENSMUSG00000053004.
DR Ensembl; ENSMUST00000160780; ENSMUSP00000124320; ENSMUSG00000053004.
DR Ensembl; ENSMUST00000161220; ENSMUSP00000124037; ENSMUSG00000053004.
DR Ensembl; ENSMUST00000161650; ENSMUSP00000124460; ENSMUSG00000053004.
DR GeneID; 15465; -.
DR KEGG; mmu:15465; -.
DR UCSC; uc009dhw.1; mouse.
DR CTD; 3269; -.
DR MGI; MGI:107619; Hrh1.
DR VEuPathDB; HostDB:ENSMUSG00000053004; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000160690; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P70174; -.
DR OMA; YVAINQS; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P70174; -.
DR TreeFam; TF333432; -.
DR Reactome; R-MMU-390650; Histamine receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 15465; 2 hits in 73 CRISPR screens.
DR PRO; PR:P70174; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70174; protein.
DR Bgee; ENSMUSG00000053004; Expressed in subparaventricular zone and 76 other tissues.
DR ExpressionAtlas; P70174; baseline and differential.
DR Genevisible; P70174; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0051381; F:histamine binding; ISO:MGI.
DR GO; GO:0004969; F:histamine receptor activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
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:0071421; P:manganese ion transmembrane transport; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
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 Biological rhythms; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..488
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069677"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 30..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 53..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..101
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 124..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 418..439
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 440..451
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 452..471
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 472..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 107..112
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT REGION 245..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..429
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 245..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
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 DISULFID 442..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 263
FT /note="P -> L (in strain: C3H/HeJ and CBA/J)"
FT /evidence="ECO:0000269|PubMed:12142541"
FT VARIANT 312
FT /note="V -> M (in strain: C3H/HeJ and CBA/J)"
FT /evidence="ECO:0000269|PubMed:12142541"
FT VARIANT 330
FT /note="P -> S (in strain: C3H/HeJ and CBA/J)"
FT /evidence="ECO:0000269|PubMed:12142541"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="L -> G (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> I (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="KA -> NG (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> P (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="E -> D (in Ref. 2; AAK66778)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="A -> S (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="K -> T (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="E -> A (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="S -> R (in Ref. 1; BAA08791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55682 MW; 82612DF712998B41 CRC64;
MSLPNTSSAS EDKMCEGNRT AMASPQLLPL VVVLSSISLV TVGLNLLVLY AVRSERKLHT
VGNLYIVSLS VADLIVGAVV MPMNILYLIM TKWSLGRPLC LFWLSMDYVA STASIFSVFI
LCIDRYRSVQ QPLRYLRYRT KTRASATILG AWFLSFLWVI PILGWHHFTP LAPELREDKC
ETDFYNVTWF KIMTAIINFY LPTLLMLWFY VKIYKAVRRH CQHRQLTNGS LPTFLEIKLR
SEDAKEGAKK PGKESPWGVQ KRPSRDPTGG LDQKSTSEDP KVTSPTVFSQ EGERETVTRP
CFRLDVMQTQ PVPEGDARGS KANDQTLSQP KMDEQSLSTC RRISETSEDQ TLVDRQSFSR
TTDSDTSIEP GLGKVKARSR SNSGLDYIKV TWKRLRSHSR QYVSGLHLNR ERKAAKQLGC
IMAAFILCWI PYFIFFMVIA FCNSCCSEPV HMFTIWLGYI NSTLNPLIYP LCNENFKKTF
KKILHIRS
