HRH2_CANLF
ID HRH2_CANLF Reviewed; 359 AA.
AC P17124;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Histamine H2 receptor;
DE Short=H2R;
DE Short=HH2R;
DE AltName: Full=Gastric receptor I;
GN Name=HRH2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1703298; DOI=10.1073/pnas.88.2.429;
RA Gantz I., Schaeffer M., Delvalle J., Logsdon C., Campbell V., Uhler M.,
RA Yamada T.;
RT "Molecular cloning of a gene encoding the histamine H2 receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:429-433(1991).
RN [2]
RP MUTAGENESIS OF HISTAMINE-BINDING RESIDUES.
RX PubMed=1356984; DOI=10.1016/s0021-9258(19)36764-x;
RA Gantz I., DelValle J., Wang L.-D., Tashiro T., Munzert G., Guo Y.-J.,
RA Konda Y., Yamada T.;
RT "Molecular basis for the interaction of histamine with the histamine H2
RT receptor.";
RL J. Biol. Chem. 267:20840-20843(1992).
RN [3]
RP PALMITOYLATION AT CYS-305.
RX PubMed=11420116; DOI=10.1016/s0167-4889(01)00104-5;
RA Fukushima Y., Saitoh T., Anai M., Ogihara T., Inukai K., Funaki M.,
RA Sakoda H., Onishi Y., Ono H., Fujishiro M., Ishikawa T., Takata K.,
RA Nagai R., Omata M., Asano T.;
RT "Palmitoylation of the canine histamine H2 receptor occurs at Cys(305) and
RT is important for cell surface targeting.";
RL Biochim. Biophys. Acta 1539:181-191(2001).
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 -!- TISSUE SPECIFICITY: Gastric fundus and, to a lesser extent, in brain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M32701; AAA85637.1; -; Genomic_DNA.
DR PIR; A39008; A39008.
DR RefSeq; NP_001182773.1; NM_001195844.1.
DR RefSeq; XP_005618925.1; XM_005618868.2.
DR AlphaFoldDB; P17124; -.
DR SMR; P17124; -.
DR STRING; 9615.ENSCAFP00000053813; -.
DR SwissPalm; P17124; -.
DR PaxDb; P17124; -.
DR Ensembl; ENSCAFT00845000497; ENSCAFP00845000340; ENSCAFG00845000310.
DR GeneID; 403812; -.
DR KEGG; cfa:403812; -.
DR CTD; 3274; -.
DR VEuPathDB; HostDB:ENSCAFG00845000310; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000158761; -.
DR InParanoid; P17124; -.
DR OrthoDB; 929700at2759; -.
DR Proteomes; UP000002254; Chromosome 4.
DR Bgee; ENSCAFG00000016718; Expressed in adipose tissue and 44 other tissues.
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 1: Evidence at protein 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..359
FT /note="Histamine H2 receptor"
FT /id="PRO_0000069681"
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 310..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 98
FT /note="Essential for histamine binding"
FT SITE 186
FT /note="Essential for tiotidine binding and H2 selectivity"
FT SITE 190
FT /note="Implicated in histamine binding"
FT LIPID 305
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:11420116"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 98
FT /note="D->N: Abolishes histamine binding."
FT /evidence="ECO:0000269|PubMed:1356984"
FT MUTAGEN 186
FT /note="D->A,N: Abolishes tiotidine, but not cimetidine
FT binding."
FT /evidence="ECO:0000269|PubMed:1356984"
FT MUTAGEN 190
FT /note="T->A,C: Diminishes histamine-stimulated activity."
FT /evidence="ECO:0000269|PubMed:1356984"
SQ SEQUENCE 359 AA; 40201 MW; 37F36412DF5BE805 CRC64;
MISNGTGSSF CLDSPPCRIT VSVVLTVLIL ITIAGNVVVC LAVGLNRRLR SLTNCFIVSL
AITDLLLGLL VLPFSAFYQL SCRWSFGKVF CNIYTSLDVM LCTASILNLF MISLDRYCAV
TDPLRYPVLI TPVRVAVSLV LIWVISITLS FLSIHLGWNS RNETSSFNHT IPKCKVQVNL
VYGLVDGLVT FYLPLLVMCI TYYRIFKIAR DQAKRIHHMG SWKAATIGEH KATVTLAAVM
GAFIICWFPY FTVFVYRGLK GDDAINEAFE AVVLWLGYAN SALNPILYAT LNRDFRTAYQ
QLFRCRPASH NAQETSLRSN SSQLARNQSR EPMRQEEKPL KLQVWSGTEV TAPRGATDR
