AGTR1_BOVIN
ID AGTR1_BOVIN Reviewed; 359 AA.
AC P25104;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Type-1 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-1 receptor {ECO:0000303|PubMed:2041569};
DE Short=AT1 receptor {ECO:0000303|PubMed:2041569};
GN Name=AGTR1;
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, AND TISSUE SPECIFICITY.
RX PubMed=2041569; DOI=10.1038/351230a0;
RA Sasaki K., Yamano Y., Bardhan S., Iwai N., Murray J.J., Hasegawa M.,
RA Matsuda Y., Inagami T.;
RT "Cloning and expression of a complementary DNA encoding a bovine adrenal
RT angiotensin II type-1 receptor.";
RL Nature 351:230-233(1991).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide,
CC which acts as a key regulator of blood pressure and sodium retention by
CC the kidney (PubMed:2041569). The activated receptor in turn couples to
CC G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates
CC phospholipase C and increases the cytosolic Ca(2+) concentrations,
CC which in turn triggers cellular responses such as stimulation of
CC protein kinase C (PubMed:2041569). {ECO:0000269|PubMed:2041569}.
CC -!- SUBUNIT: Interacts with MAS1 (By similarity). Interacts with ARRB1 (By
CC similarity). Interacts with FLNA (via filamin repeat 21); increases
CC PKA-mediated phosphorylation of FLNA (By similarity).
CC {ECO:0000250|UniProtKB:P25095, ECO:0000250|UniProtKB:P30556}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- TISSUE SPECIFICITY: Adrenal medulla, cortex and kidney.
CC {ECO:0000269|PubMed:2041569}.
CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC {ECO:0000250|UniProtKB:P30556}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X62294; CAA44182.1; -; mRNA.
DR RefSeq; NP_776658.1; NM_174233.2.
DR AlphaFoldDB; P25104; -.
DR SMR; P25104; -.
DR STRING; 9913.ENSBTAP00000055053; -.
DR BindingDB; P25104; -.
DR ChEMBL; CHEMBL3374; -.
DR DrugCentral; P25104; -.
DR PaxDb; P25104; -.
DR Ensembl; ENSBTAT00000063575; ENSBTAP00000055053; ENSBTAG00000045633.
DR GeneID; 281607; -.
DR KEGG; bta:281607; -.
DR CTD; 185; -.
DR VEuPathDB; HostDB:ENSBTAG00000045633; -.
DR VGNC; VGNC:25745; AGTR1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P25104; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR TreeFam; TF330024; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:P25104; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000045633; Expressed in uterine cervix and 85 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001596; F:angiotensin type I receptor activity; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:Ensembl.
DR GO; GO:0031711; F:bradykinin receptor binding; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
DR InterPro; IPR000190; ATII_AT1_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00635; ANGIOTENSN1R.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor"
FT /id="PRO_0000069150"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 26..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 56..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 62..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 90..98
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 99..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 126..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 142..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 166..190
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 191..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 217..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 240..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 269..278
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 279..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 305..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 17
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 167
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 182
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 183
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 184
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 199
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT LIPID 355
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..274
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT DISULFID 101..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 359 AA; 41088 MW; B426BFFF6B61DFEA CRC64;
MILNSSTEDG IKRIQDDCPK AGRHNYIFIM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNYL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLLAGLAS LPTIIHRNVF FIENTNITVC
AFHYESQNST LPVGLGLTKN ILGFLFPFLI ILTSYTLIWK TLKKAYEIQK NKPRKDDIFK
IILAIVLFFF FSWVPHQIFT FMDVLIQLGL IRDCKIEDIV DTAMPITICL AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPKAKSHSNL STKMSTLSYR PSENGNSSTK KPAPCIEVE
