HRH1_PONPY
ID HRH1_PONPY Reviewed; 487 AA.
AC Q9N2B0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Histamine H1 receptor;
DE Short=H1R;
DE Short=HH1R;
GN Name=HRH1;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate oran-Po13;
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: 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AB041383; BAA94468.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N2B0; -.
DR SMR; Q9N2B0; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004969; F:histamine receptor activity; ISS:UniProtKB.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
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: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; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..487
FT /note="Histamine H1 receptor"
FT /id="PRO_0000069679"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 30..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 53..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..101
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 124..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 417..438
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 439..450
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 451..470
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 471..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 107..112
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT REGION 238..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..428
FT /note="Important for agonist binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 240..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70174"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35367"
FT MOD_RES 398
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 100..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 441..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 487 AA; 55588 MW; 67331ABBFD7D6299 CRC64;
MSLPNSSCLL EDKMCEGNKT TMASPQLMPL VVVLSTISLV TVGLNLLVLY AVRSERKLHT
VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC LFWLSMDYVA STASIFSVFI
LCIDRYRSVQ QPLRYLKYRT KTRASATILG AWFLSFLWVI PILGWNHFRQ QISVRREDKC
ETDFYDVTWF KVMTAIINFY LPTLLMLWFY AKIYKAVQKH CQHRELINGS LPSFSEIKLR
PENPKGDAKK PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDGEVDKL
HCFPLDIVQM QTVAEGSSRD YVAINQSHGQ LKTDEQGLNT HGASEISEDQ MLGDSQSFSR
TDSDTTTETA PGKGKLRSGS NTGLDYIKFT WKRLRSHSRQ YVSGLHMNRE RKAAKQLGFI
MAAFILCWIP YFIFFMVIAF CKNCCNEHLH MFTIWLGYIN STLNPLIYPL CNENFKKTFK
RILHIRS
