AGTR1_PIG
ID AGTR1_PIG Reviewed; 359 AA.
AC P30555;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Type-1 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-1 receptor;
DE Short=AT1 receptor;
GN Name=AGTR1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Aortic smooth muscle;
RX PubMed=8491254; DOI=10.1016/0922-4106(93)90122-p;
RA Itazaki K., Shigeri Y., Fujimoto M.;
RT "Molecular cloning and characterization of the angiotensin receptor subtype
RT in porcine aortic smooth muscle.";
RL Eur. J. Pharmacol. 245:147-156(1993).
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:8491254). 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 (By similarity). {ECO:0000250|UniProtKB:P30556,
CC ECO:0000269|PubMed:8491254}.
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 -!- 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; D11340; BAA01952.1; -; mRNA.
DR RefSeq; XP_003132517.1; XM_003132469.3.
DR AlphaFoldDB; P30555; -.
DR SMR; P30555; -.
DR IntAct; P30555; 1.
DR STRING; 9823.ENSSSCP00000030853; -.
DR BindingDB; P30555; -.
DR ChEMBL; CHEMBL5743; -.
DR PaxDb; P30555; -.
DR PRIDE; P30555; -.
DR Ensembl; ENSSSCT00000034453; ENSSSCP00000030853; ENSSSCG00000011695.
DR Ensembl; ENSSSCT00005034302; ENSSSCP00005020902; ENSSSCG00005021724.
DR Ensembl; ENSSSCT00015071980; ENSSSCP00015028872; ENSSSCG00015053993.
DR Ensembl; ENSSSCT00025038974; ENSSSCP00025016487; ENSSSCG00025028692.
DR Ensembl; ENSSSCT00030061647; ENSSSCP00030028191; ENSSSCG00030044196.
DR Ensembl; ENSSSCT00035009753; ENSSSCP00035003286; ENSSSCG00035007839.
DR Ensembl; ENSSSCT00040096595; ENSSSCP00040042920; ENSSSCG00040070419.
DR Ensembl; ENSSSCT00045055743; ENSSSCP00045038876; ENSSSCG00045032665.
DR Ensembl; ENSSSCT00050077460; ENSSSCP00050033335; ENSSSCG00050056820.
DR Ensembl; ENSSSCT00055042939; ENSSSCP00055034160; ENSSSCG00055021872.
DR Ensembl; ENSSSCT00060086211; ENSSSCP00060037272; ENSSSCG00060063200.
DR Ensembl; ENSSSCT00065097576; ENSSSCP00065042773; ENSSSCG00065071012.
DR Ensembl; ENSSSCT00070011447; ENSSSCP00070009438; ENSSSCG00070006005.
DR GeneID; 100519976; -.
DR KEGG; ssc:100519976; -.
DR CTD; 185; -.
DR VGNC; VGNC:85191; AGTR1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P30555; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR TreeFam; TF330024; -.
DR Reactome; R-SSC-375276; Peptide ligand-binding receptors.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Reactome; R-SSC-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SSC-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P30555; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Bgee; ENSSSCG00000011695; Expressed in liver and 35 other tissues.
DR Genevisible; P30555; SS.
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_0000069158"
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 326..359
FT /note="Disordered"
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; 40907 MW; D5B93968CC57ABF0 CRC64;
MILNSSTEDS IKRIQDDCPK AGRHNYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNYL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLLAGLAS LPTIIHRNVF FIENTNITVC
AFHYESQNST LPVGLGLTKN ILGFLFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFK
IIMAIVLFFF FSWVPHQIFT FLDVLIQLGI IHDCKIADIV DTAMPITICL AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPKAKSHSSL STKMSTLSYR PSENGSSSTK KSAPCTEVE
