HRH1_CAVPO
ID HRH1_CAVPO Reviewed; 488 AA.
AC P31389;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=HRH1;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=8282735; DOI=10.1093/oxfordjournals.jbchem.a124190;
RA Horio Y., Mori Y., Higuchi I., Fujimoto K., Ito S., Fukui H.;
RT "Molecular cloning of the guinea-pig histamine H1 receptor gene.";
RL J. Biochem. 114:408-414(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8294913; DOI=10.1046/j.1471-4159.1994.62020507.x;
RA Traiffort E., Leurs R., Arrang J.-M., Tardivel-Lacombe J., Diaz J.,
RA Schwartz J.-C., Ruat M.;
RT "Guinea pig histamine H1 receptor. I. Gene cloning, characterization, and
RT tissue expression revealed by in situ hybridization.";
RL J. Neurochem. 62:507-518(1994).
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:8282735}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8282735};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8282735}.
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; D15074; BAA03669.1; -; Genomic_DNA.
DR EMBL; S68706; AAC60674.1; -; Genomic_DNA.
DR PIR; I56507; I56507.
DR AlphaFoldDB; P31389; -.
DR SMR; P31389; -.
DR STRING; 10141.ENSCPOP00000017245; -.
DR BindingDB; P31389; -.
DR ChEMBL; CHEMBL3943; -.
DR DrugCentral; P31389; -.
DR eggNOG; KOG4220; Eukaryota.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P31389; -.
DR OMA; YVAINQS; -.
DR TreeFam; TF333432; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0004969; F:histamine receptor activity; IDA:BHF-UCL.
DR GO; GO:0070509; P:calcium ion import; IDA:MGI.
DR GO; GO:0071420; P:cellular response to histamine; IDA:BHF-UCL.
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:0048016; P:inositol phosphate-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0071421; P:manganese ion transmembrane transport; IDA:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IC:BHF-UCL.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..488
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069674"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..110
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..198
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 199..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 220..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 418..439
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 440..451
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 452..471
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 472..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 116..121
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..429
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 259..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 345
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 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 442..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 488 AA; 55620 MW; 7E58C681E1A2178E CRC64;
MSFLPGMTPV TLSNFSWALE DRMLEGNSTT TPTRQLMPLV VVLSSVSLVT VALNLLVLYA
VRSERKLHTV GNLYIVSLSV ADLIVGAVVM PMSILYLHRS AWILGRPLCL FWLSMDYVAS
TASIFSVFIL CIDRYRSVQQ PLRYLRYRTK TRASATILGA WLLSFLWVIP ILGWHHFMAP
TSEPREKKCE TDFYDVTWFK VMTAIINFYL PTLLMLWFYI RIYKAVRRHC QHRQLINSSL
PSFSEMKLKL ENAKVDTRRM GKESPWEDPK RCSKDASGVH TPMPSSQHLV DMPCAAVLSE
DEGGEVGTRQ MPMLAVGDGR CCEALNHMHS QLELSGQSRA THSISARPEE WTVVDGQSFP
ITDSDTSTEA APMGGQPRSG SNSGLDYIKF TWRRLRSHSR QYTSGLHLNR ERKAAKQLGC
IMAAFILCWI PYFVFFMVIA FCKSCSNEPV HMFTIWLGYL NSTLNPLIYP LCNENFRKTF
KRILRIPP
