HRH2_GORGO
ID HRH2_GORGO Reviewed; 359 AA.
AC Q76MS7;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Histamine H2 receptor;
DE Short=H2R;
DE Short=HH2R;
DE AltName: Full=Gastric receptor I;
GN Name=HRH2;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
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).
CC -!- FUNCTION: The H2 subclass of histamine receptors mediates gastric acid
CC secretion. Also appears to regulate gastrointestinal motility and
CC intestinal secretion. Possible role in regulating cell growth and
CC differentiation. The activity of this receptor is mediated by G
CC proteins which activate adenylyl cyclase and, through a separate G
CC protein-dependent mechanism, the phosphoinositide/protein kinase (PKC)
CC signaling pathway (By similarity). {ECO:0000250}.
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; AB041386; BAA94471.1; -; Genomic_DNA.
DR AlphaFoldDB; Q76MS7; -.
DR SMR; Q76MS7; -.
DR STRING; 9593.ENSGGOP00000010410; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q76MS7; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IEA:InterPro.
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: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; 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_0000069683"
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 REGION 316..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 H2
FT selectivity"
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; 40098 MW; 9835AE2BA60B9B0F CRC64;
MAPNGTASSF CLDSTACKIT ITVVLAVLIL ITVAGNVVVC LAVGLNRRLR NLTNCFIVSL
AITDLLLGLL VLPFSAIYQL SCKWSFGKVF CNIYTSLDVM LCTASILNLF MISLDRYCAV
MDPLRYPVLV TPVRVAISLV LIWVISITLS FLSIHLGWNS RNETSKGNHT TSKCKVQVNE
VYGLVDGLVT FYLPLLIMCI TYYRIFKVAR DQAKRINHIS SWKAATIREH KATVTLAAVM
GAFIICWFPY FTAFVYRGLR GDDAINEVLE AIVLWLGYAN SALNPILYAA LNRDFRTGYQ
QLFCCRLANR NSHKTSLRSN ASQLSRTQSR EPRQQEEKPL KLQVWSGTEV TAPQGATDR
