HRH1_RAT
ID HRH1_RAT Reviewed; 486 AA.
AC P31390;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=Hrh1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7678492; DOI=10.1006/bbrc.1993.1045;
RA Fujimoto K., Horio Y., Sugama K., Ito S., Liu Y.Q., Fukui H.;
RT "Genomic cloning of the rat histamine H1 receptor.";
RL Biochem. Biophys. Res. Commun. 190:294-301(1993).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:7678492}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7678492};
CC Multi-pass membrane protein {ECO:0000269|PubMed:7678492}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D12800; BAA02245.1; -; Genomic_DNA.
DR PIR; JC1415; JC1415.
DR RefSeq; NP_058714.1; NM_017018.1.
DR AlphaFoldDB; P31390; -.
DR SMR; P31390; -.
DR STRING; 10116.ENSRNOP00000009775; -.
DR BindingDB; P31390; -.
DR ChEMBL; CHEMBL4701; -.
DR DrugCentral; P31390; -.
DR GlyGen; P31390; 2 sites.
DR PhosphoSitePlus; P31390; -.
DR PaxDb; P31390; -.
DR GeneID; 24448; -.
DR KEGG; rno:24448; -.
DR UCSC; RGD:2830; rat.
DR CTD; 3269; -.
DR RGD; 2830; Hrh1.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; P31390; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P31390; -.
DR Reactome; R-RNO-390650; Histamine receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P31390; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0051381; F:histamine binding; IMP:RGD.
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; IDA:RGD.
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:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; TAS:RGD.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069680"
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..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 416..437
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 438..449
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 450..469
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 470..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 107..112
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT REGION 241..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..427
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 241..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..366
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 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 397
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 440..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 486 AA; 55693 MW; E44C02A743A95E88 CRC64;
MSFANTSSTF EDKMCEGNRT AMASPQLLPL VVVLSSISLV TVGLNLLVLY AVHSERKLHT
VGNLYIVSLS VADLIVGAVV MPMNILYLIM TKWSLGRPLC LFWLSMDYVA STASIFSVFI
LCIDRYRSVQ QPLRYLRYRT KTRASATILG AWFFSFLWVI PILGWHHFMP PAPELREDKC
ETDFYNVTWF KIMTAIINFY LPTLLMLWFY VKIYKAVRRH CQHRQLTNGS LPSFSELKLR
SDDTKEGAKK PGRESPWGVL KRPSRDPSVG LDQKSTSEDP KMTSPTVFSQ EGERETRPCF
RLDIMQKQSV AEGDVRGSKA NDQALSQPKM DEQSLNTCRR ISETSEDQTL VDQQSFSRTT
DSDTSIEPGP GRVKSRSGSN SGLDYIKITW KRLRSHSRQY VSGLHLNRER KAAKQLGFIM
AAFILCWIPY FIFFMVIAFC KSCCSEPMHM FTIWLGYINS TLNPLIYPLC NENFKKTFKK
ILHIRS
