HRH1_BOVIN
ID HRH1_BOVIN Reviewed; 491 AA.
AC P30546;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=HRH1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adrenal medulla;
RX PubMed=1722337; DOI=10.1073/pnas.88.24.11515;
RA Yamashita M., Fukui H., Sugama K., Horio Y., Ito S., Mizuguchi H., Wada H.;
RT "Expression cloning of a cDNA encoding the bovine histamine H1 receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11515-11519(1991).
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:1722337}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1722337};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1722337}.
CC -!- TISSUE SPECIFICITY: Brain, lung, small intestine, uterus, adrenal
CC medulla and spleen. {ECO:0000269|PubMed:1722337}.
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; D10197; BAA01045.1; -; mRNA.
DR PIR; A41632; A41632.
DR AlphaFoldDB; P30546; -.
DR SMR; P30546; -.
DR STRING; 9913.ENSBTAP00000001896; -.
DR BindingDB; P30546; -.
DR ChEMBL; CHEMBL3573; -.
DR PaxDb; P30546; -.
DR PRIDE; P30546; -.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; P30546; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0071420; P:cellular response to histamine; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048245; P:eosinophil chemotaxis; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069673"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 54..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..102
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 166..190
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 212..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 421..442
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 443..454
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 455..474
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 475..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 108..113
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT REGION 246..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..432
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 445..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 491 AA; 55957 MW; DAA349E52218CE28 CRC64;
MTCPNSSCVF EDKMCQGNKT APANDAQLTP LVVVLSTISL VTVGLNLLVL YAVRSERKLH
TVGNLYIVSL SVADLIVGVV VMPMNILYLL MSRWSLGRPL CLFWLSMDYV ASTASIFSVF
ILCIDRYRSV QQPLKYLRYR TKTRASITIL AAWFLSFLWI IPILGWRHFQ PKTPEPREDK
CETDFYNVTW FKVMTAIINF YLPTLLMLWF YAKIYKAVRQ HCQHRELING SFPSFSDMKM
KPENLQVGAK KPGKESPWEV LKRKPKDTGG GPVLKPPSQE PKEVTSPGVF SQEKEEKDGE
LGKFYCFPLD TVQAQPEAEG SGRGYATINQ SQNQLEMGEQ GLSMPGAKEA LEDQILGDSQ
SFSRTDSDTP AEPAPAKGKS RSESSTGLEY IKFTWKRLRS HSRQYVSGLH MNRERKAAKQ
LGFIMAAFII CWIPYFIFFM VIAFCESCCN QHVHMFTIWL GYINSTLNPL IYPLCNENFK
KTFKKILHIR S
