AGTRA_RAT
ID AGTRA_RAT Reviewed; 359 AA.
AC P25095; Q9QVS5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Type-1 angiotensin II receptor A {ECO:0000303|PubMed:2041570};
DE AltName: Full=Angiotensin II type-1 receptor A {ECO:0000303|PubMed:2043116};
DE Short=AT1 receptor A {ECO:0000303|PubMed:1533121};
GN Name=Agtr1; Synonyms=Agtr1a, At1a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Vascular smooth muscle;
RX PubMed=2041570; DOI=10.1038/351233a0;
RA Murphy T.J., Alexander R.W., Griendling K.K., Runge M.S., Bernstein K.E.;
RT "Isolation of a cDNA encoding the vascular type-1 angiotensin II
RT receptor.";
RL Nature 351:233-236(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2043116; DOI=10.1016/0006-291x(91)91982-i;
RA Iwai N., Yamano Y., Chaki S., Konishi F., Bardhan S., Tibbetts C.,
RA Sasaki K., Hasegawa M., Matsuda Y., Inagami T.;
RT "Rat angiotensin II receptor: cDNA sequence and regulation of the gene
RT expression.";
RL Biochem. Biophys. Res. Commun. 177:299-304(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1533121; DOI=10.1016/s0006-291x(05)80293-1;
RA Langford K.G., Frenzel K., Martin B.M., Bernstein K.E.;
RT "The genomic organization of the rat AT1 angiotensin receptor.";
RL Biochem. Biophys. Res. Commun. 183:1025-1032(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=1544458; DOI=10.1016/0014-5793(92)80071-n;
RA Iwai N., Inagami T.;
RT "Identification of two subtypes in the rat type I angiotensin II
RT receptor.";
RL FEBS Lett. 298:257-260(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7713098; DOI=10.1093/eurheartj/15.suppl_d.104;
RA Inagami T., Iwai N., Sasaki K., Yamano Y., Bardhan S., Chaki S., Guo D.F.,
RA Furuta H., Ohyama K., Kambayashi Y., Takahashi K., Ichiki T.;
RT "Cloning, expression and regulation of angiotensin II receptors.";
RL Eur. Heart J. 15:104-107(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-259.
RC TISSUE=Kidney;
RX PubMed=1599457; DOI=10.1016/s0006-291x(05)80976-3;
RA Ye M.Q., Healy D.P.;
RT "Characterization of an angiotensin type-1 receptor partial cDNA from rat
RT kidney: evidence for a novel AT1B receptor subtype.";
RL Biochem. Biophys. Res. Commun. 185:204-210(1992).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ILE-238 AND PHE-239.
RX PubMed=10747880; DOI=10.1074/jbc.m000198200;
RA Zhang M., Zhao X., Chen H.C., Catt K.J., Hunyady L.;
RT "Activation of the AT1 angiotensin receptor is dependent on adjacent apolar
RT residues in the carboxyl terminus of the third cytoplasmic loop.";
RL J. Biol. Chem. 275:15782-15788(2000).
RN [9]
RP INTERACTION WITH ARRB1.
RX PubMed=11579203; DOI=10.1210/mend.15.10.0714;
RA Qian H., Pipolo L., Thomas W.G.;
RT "Association of beta-Arrestin 1 with the type 1A angiotensin II receptor
RT involves phosphorylation of the receptor carboxyl terminus and correlates
RT with receptor internalization.";
RL Mol. Endocrinol. 15:1706-1719(2001).
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:2041570, PubMed:10747880). The activated receptor in
CC turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and
CC thus activates phospholipase C and increases the cytosolic Ca(2+)
CC concentrations, which in turn triggers cellular responses such as
CC stimulation of protein kinase C (PubMed:10747880).
CC {ECO:0000269|PubMed:10747880, ECO:0000269|PubMed:2041570}.
CC -!- SUBUNIT: Interacts with MAS1 (By similarity). Interacts with ARRB1
CC (PubMed:11579203). Interacts with FLNA (via filamin repeat 21);
CC increases PKA-mediated phosphorylation of FLNA (By similarity).
CC {ECO:0000250|UniProtKB:P30556, ECO:0000269|PubMed:11579203}.
CC -!- INTERACTION:
CC P25095; P01019: AGT; Xeno; NbExp=10; IntAct=EBI-764979, EBI-751728;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- TISSUE SPECIFICITY: Is expressed in the liver, kidney, aorta, lung,
CC uterus, ovary, spleen, heart, adrenal gland, and vascular smooth muscle
CC cell. {ECO:0000269|PubMed:2041570}.
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; X62295; CAA44183.1; -; mRNA.
DR EMBL; M74054; AAA40738.1; -; mRNA.
DR EMBL; BC078810; AAH78810.1; -; mRNA.
DR EMBL; M86912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC2134; JC2134.
DR RefSeq; NP_112247.2; NM_030985.4.
DR RefSeq; XP_006253944.1; XM_006253882.3.
DR RefSeq; XP_008769816.1; XM_008771594.2.
DR AlphaFoldDB; P25095; -.
DR SMR; P25095; -.
DR BioGRID; 246370; 6.
DR IntAct; P25095; 6.
DR MINT; P25095; -.
DR STRING; 10116.ENSRNOP00000034687; -.
DR BindingDB; P25095; -.
DR ChEMBL; CHEMBL329; -.
DR DrugCentral; P25095; -.
DR GuidetoPHARMACOLOGY; 34; -.
DR GlyGen; P25095; 3 sites.
DR iPTMnet; P25095; -.
DR PhosphoSitePlus; P25095; -.
DR PaxDb; P25095; -.
DR PRIDE; P25095; -.
DR Ensembl; ENSRNOT00000038532; ENSRNOP00000034687; ENSRNOG00000018346.
DR Ensembl; ENSRNOT00000102465; ENSRNOP00000091615; ENSRNOG00000018346.
DR GeneID; 24180; -.
DR KEGG; rno:24180; -.
DR UCSC; RGD:2070; rat.
DR CTD; 11607; -.
DR RGD; 2070; Agtr1a.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P25095; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR PhylomeDB; P25095; -.
DR TreeFam; TF330024; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P25095; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018346; Expressed in liver and 16 other tissues.
DR Genevisible; P25095; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0012505; C:endomembrane system; IDA:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031968; C:organelle outer membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0001596; F:angiotensin type I receptor activity; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; ISO:RGD.
DR GO; GO:0031711; F:bradykinin receptor binding; ISO:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0042976; P:activation of Janus kinase activity; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0002035; P:brain renin-angiotensin system; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR GO; GO:0042416; P:dopamine biosynthetic process; IMP:RGD.
DR GO; GO:0042756; P:drinking behavior; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:BHF-UCL.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:RGD.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0006885; P:regulation of pH; IDA:RGD.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; ISO:RGD.
DR GO; GO:0034391; P:regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; ISO:RGD.
DR GO; GO:1905459; P:regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0002001; P:renin secretion into blood stream; ISO:RGD.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:1990776; P:response to angiotensin; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0009651; P:response to salt stress; IEP:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; IMP:RGD.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
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 1: Evidence at protein 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 A"
FT /id="PRO_0000069160"
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 337..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..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"
FT MUTAGEN 238
FT /note="I->A,S,K: Decreased angiotensin II-induced inositol
FT phosphate response."
FT /evidence="ECO:0000269|PubMed:10747880"
FT MUTAGEN 238
FT /note="I->D: Abolished angiotensin II-induced inositol
FT phosphate response."
FT /evidence="ECO:0000269|PubMed:10747880"
FT MUTAGEN 239
FT /note="F->D: Reduced angiotensin II-induced inositol
FT phosphate response."
FT /evidence="ECO:0000269|PubMed:10747880"
FT MUTAGEN 239
FT /note="F->R,K: Increased angiotensin II-induced inositol
FT phosphate response."
FT /evidence="ECO:0000269|PubMed:10747880"
FT CONFLICT 81
FT /note="L -> C (in Ref. 2; AAA40738)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="S -> T (in Ref. 2; AAA40738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40890 MW; 200EAE56DB4DA678 CRC64;
MALNSSAEDG IKRIQDDCPK AGRHSYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNHL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLMAGLAS LPAVIHRNVY FIENTNITVC
AFHYESRNST LPIGLGLTKN ILGFLFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFR
IIMAIVLFFF FSWVPHQIFT FLDVLIQLGV IHDCKISDIV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPKAKSHSSL STKMSTLSYR PSDNMSSSAK KPASCFEVE
