HRH2_CAVPO
ID HRH2_CAVPO Reviewed; 359 AA.
AC P47747;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Histamine H2 receptor;
DE Short=H2R;
DE Short=HH2R;
DE AltName: Full=Gastric receptor I;
GN Name=HRH2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=7794271; DOI=10.1006/bbrc.1995.1851;
RA Traiffort E., Vizuete M.L., Tardivel-Lacombe J., Souil E., Schwartz J.-C.,
RA Ruat M.;
RT "The guinea pig histamine H2 receptor: gene cloning, tissue expression and
RT chromosomal localization of its human counterpart.";
RL Biochem. Biophys. Res. Commun. 211:570-577(1995).
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}.
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DR EMBL; U25440; AAA65713.1; -; Genomic_DNA.
DR PIR; JC4120; JC4120.
DR AlphaFoldDB; P47747; -.
DR SMR; P47747; -.
DR STRING; 10141.ENSCPOP00000003138; -.
DR BindingDB; P47747; -.
DR ChEMBL; CHEMBL2882; -.
DR DrugCentral; P47747; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P47747; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004969; F:histamine receptor activity; IEA:InterPro.
DR GO; GO:0001696; P:gastric acid secretion; IEA:InterPro.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000503; Histamine_H2_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00531; HISTAMINEH2R.
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 3: Inferred from homology;
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..359
FT /note="Histamine H2 receptor"
FT /id="PRO_0000069682"
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..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..204
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 98
FT /note="Essential for histamine binding"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Essential for tiotidine binding and implicated in
FT histamine binding"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Implicated in histamine binding"
FT /evidence="ECO:0000250"
FT LIPID 305
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..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 359 AA; 40557 MW; 58DB81BD8FC3C0E9 CRC64;
MAFNGTVPSF CMDFTVYKVT ISVILIILIL VTVAGNVVVC LAVGLNRRLR SLTNCFIVSL
AVTDLLLGLL VLPFSAIYQL SCKWSFSKVF CNIYTSLDVM LCTASILNLF MISLDRYCAV
TDPLRYPVLI TPARVAISLV FIWVISITLS FLSIHLGWNS RNETSKDNDT IVKCKVQVNE
VYGLVDGLVT FYLPLLIMCI TYFRIFKIAR EQARRINHIG SWKAATIREH KATVTLAAVM
GAFIICWFPY FTVFVYRGLK GDDAVNEVFE DVVLWLGYAN SALNPILYAA LNRDFRTAYH
QLFCCRLASH NSHETSLRLN NSQLNRSQCQ EPRWQEDKPL NLQVWSGTEV TAPQGATNR
