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HRH2_RAT
ID   HRH2_RAT                Reviewed;         358 AA.
AC   P25102;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Histamine H2 receptor;
DE            Short=H2R;
DE            Short=HH2R;
DE   AltName: Full=Gastric receptor I;
GN   Name=Hrh2;
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].
RX   PubMed=1930188; DOI=10.1016/0006-291x(91)91738-x;
RA   Ruat M., Traiffort E., Arrang J.-M., Leurs R., Schwartz J.-C.;
RT   "Cloning and tissue expression of a rat histamine H2-receptor gene.";
RL   Biochem. Biophys. Res. Commun. 179:1470-1478(1991).
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; S57565; AAB19935.1; -; Genomic_DNA.
DR   PIR; JQ1278; JQ1278.
DR   RefSeq; NP_037097.3; NM_012965.3.
DR   AlphaFoldDB; P25102; -.
DR   SMR; P25102; -.
DR   IntAct; P25102; 2.
DR   STRING; 10116.ENSRNOP00000024580; -.
DR   BindingDB; P25102; -.
DR   ChEMBL; CHEMBL4654; -.
DR   DrugCentral; P25102; -.
DR   GuidetoPHARMACOLOGY; 263; -.
DR   GlyGen; P25102; 1 site.
DR   PhosphoSitePlus; P25102; -.
DR   PaxDb; P25102; -.
DR   GeneID; 25461; -.
DR   KEGG; rno:25461; -.
DR   CTD; 3274; -.
DR   RGD; 2831; Hrh2.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P25102; -.
DR   OrthoDB; 929700at2759; -.
DR   PhylomeDB; P25102; -.
DR   Reactome; R-RNO-390650; Histamine receptors.
DR   PRO; PR:P25102; -.
DR   Proteomes; UP000002494; 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:0016020; C:membrane; IDA:RGD.
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:1901363; F:heterocyclic compound binding; IDA:RGD.
DR   GO; GO:0004969; F:histamine receptor activity; IDA:RGD.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0071420; P:cellular response to histamine; IEP:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0001698; P:gastrin-induced gastric acid secretion; ISO:RGD.
DR   GO; GO:0048732; P:gland development; ISO:RGD.
DR   GO; GO:0001697; P:histamine-induced gastric acid secretion; ISO:RGD.
DR   GO; GO:0007613; P:memory; ISO:RGD.
DR   GO; GO:1900139; P:negative regulation of arachidonic acid secretion; IDA:RGD.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR   GO; GO:1901998; P:toxin transport; ISO:RGD.
DR   GO; GO:0008542; P:visual learning; ISO:RGD.
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..358
FT                   /note="Histamine H2 receptor"
FT                   /id="PRO_0000069688"
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..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..203
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..257
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..288
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   SITE            98
FT                   /note="Essential for histamine binding"
FT                   /evidence="ECO:0000250"
FT   SITE            185
FT                   /note="Essential for tiotidine binding and implicated in
FT                   histamine binding"
FT                   /evidence="ECO:0000250"
FT   SITE            189
FT                   /note="Implicated in histamine binding"
FT                   /evidence="ECO:0000250"
FT   LIPID           304
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..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   358 AA;  40253 MW;  4889F69B7B5D5DDC CRC64;
     MEPNGTVHSC CLDSMALKVT ISVVLTTLIL ITIAGNVVVC LAVSLNRRLR SLTNCFIVSL
     AATDLLLGLL VLPFSAIYQL SFTWSFGHVF CNIYTSLDVM LCTASILNLF MISLDRYCAV
     TDPLRYPVLV TPVRVAISLV FIWVISITLS FLSIHLGWNS RNGTRGGNDT FKCKVQVNEV
     YGLVDGLVTF YLPLLIMCVT YYRIFKIARE QAKRINHISS WKAATIREHK ATVTLAAVMG
     AFIICWFPYF TAFVYRGLRG DDAINEAVEG IVLWLGYANS ALNPILYAAL NRDFRTAYQQ
     LFHCKFASHN SHKTSLRLNN SLLPRSQSRE GRWQEEKPLK LQVWSGTELT HPQGNPIR
 
 
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