ID AGTR1_HUMAN Reviewed; 359 AA.
AC P30556; Q13725; Q8TBK4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 02-OCT-2024, entry version 217.
DE RecName: Full=Type-1 angiotensin II receptor {ECO:0000303|PubMed:1550596};
DE AltName: Full=AT1AR {ECO:0000303|PubMed:1378723};
DE AltName: Full=AT1BR;
DE AltName: Full=Angiotensin II type-1 receptor {ECO:0000303|PubMed:1378723};
DE Short=AT1 receptor {ECO:0000303|PubMed:1543512};
GN Name=AGTR1 {ECO:0000312|HGNC:HGNC:336};
GN Synonyms=AGTR1A, AGTR1B, AT2R1, AT2R1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1378723; DOI=10.1016/s0006-291x(05)80804-6;
RA Mauzy C.A., Hwang O., Egloff A.M., Wu L.H., Chung F.-Z.;
RT "Cloning, expression, and characterization of a gene encoding the human
RT angiotensin II type 1A receptor.";
RL Biochem. Biophys. Res. Commun. 186:277-284(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=1543512; DOI=10.1016/0006-291x(92)91600-u;
RA Furuta H., Guo D.F., Inagami T.;
RT "Molecular cloning and sequencing of the gene encoding human angiotensin II
RT type 1 receptor.";
RL Biochem. Biophys. Res. Commun. 183:8-13(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=1567413; DOI=10.1016/s0006-291x(05)80288-8;
RA Bergsma D.J., Ellis C., Kumar C., Nuthalaganti P., Kersten H.,
RA Elshourbagy N.A., Griffin E., Stadel J.M., Aiyar N.;
RT "Cloning and characterization of a human angiotensin II type 1 receptor.";
RL Biochem. Biophys. Res. Commun. 183:989-995(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1550596; DOI=10.1016/0006-291x(92)90570-b;
RA Takayanagi R., Ohnaka K., Sakai Y., Nakao R., Yanase T., Haji M.,
RA Inagami T., Furuta H., Gou D.F., Nakamuta M., Nawata H.;
RT "Molecular cloning, sequence analysis and expression of a cDNA encoding
RT human type-1 angiotensin II receptor.";
RL Biochem. Biophys. Res. Commun. 183:910-916(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1508224; DOI=10.1210/mend.6.7.1508224;
RA Curnow K.M., Pascoe L., White P.C.;
RT "Genetic analysis of the human type-1 angiotensin II receptor.";
RL Mol. Endocrinol. 6:1113-1118(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TRP-289.
RC TISSUE=Placenta;
RX PubMed=8135787; DOI=10.1006/bbrc.1994.1252;
RA Konishi H., Kuroda S., Inada Y., Fujisawa Y.;
RT "Novel subtype of human angiotensin II type 1 receptor: cDNA cloning and
RT expression.";
RL Biochem. Biophys. Res. Commun. 199:467-474(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7792812; DOI=10.1016/0039-128x(94)00022-5;
RA Nawata H., Takayanagi R., Ohnaka K., Sakai Y., Imasaki K., Yanase T.,
RA Ikuyama S., Tanaka S., Ohe K.;
RT "Type 1 angiotensin II receptors of adrenal tumors.";
RL Steroids 60:28-34(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Ostermann E., Castanon M.J.;
RT "Cloning and sequencing of a human cDNA encoding the angiotensin II
RT receptor type 1.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Antonellis A., Rogus J.J., Pezzolesi M.G., Makita Y., Nam M., Doria A.,
RA Warram J.H., Krolewski A.S.;
RT "Rapid identification of polymorphisms in genomic DNA: a high density SNP
RT map of the type I angiotensin II receptor gene locus on chromosome 3q.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-222 AND HIS-341.
RC TISSUE=Brain;
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 [12]
RP FUNCTION, AND MUTAGENESIS OF ASN-111.
RX PubMed=8987975; DOI=10.1021/bi961593m;
RA Noda K., Feng Y.H., Liu X.P., Saad Y., Husain A., Karnik S.S.;
RT "The active state of the AT1 angiotensin receptor is generated by
RT angiotensin II induction.";
RL Biochemistry 35:16435-16442(1996).
RN [13]
RP INTERACTION WITH MAS1.
RX PubMed=15809376; DOI=10.1161/01.cir.0000160867.23556.7d;
RA Kostenis E., Milligan G., Christopoulos A., Sanchez-Ferrer C.F.,
RA Heringer-Walther S., Sexton P.M., Gembardt F., Kellett E., Martini L.,
RA Vanderheyden P., Schultheiss H.P., Walther T.;
RT "G-protein-coupled receptor Mas is a physiological antagonist of the
RT angiotensin II type 1 receptor.";
RL Circulation 111:1806-1813(2005).
RN [14]
RP FUNCTION.
RX PubMed=15611106; DOI=10.1074/jbc.m412924200;
RA Barnes W.G., Reiter E., Violin J.D., Ren X.-R., Milligan G.,
RA Lefkowitz R.J.;
RT "beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber
RT formation following receptor stimulation.";
RL J. Biol. Chem. 280:8041-8050(2005).
RN [15]
RP GLYCOSYLATION AT ASN-4.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP INTERACTION WITH FLNA.
RX PubMed=26460884; DOI=10.1021/acs.biochem.5b00975;
RA Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J.,
RA Karnik S.S.;
RT "G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and
RT Promote Filamin Phosphorylation.";
RL Biochemistry 54:6673-6683(2015).
RN [17]
RP FUNCTION (MICROBIAL FUNCTION), AND SUBCELLULAR LOCATION.
RX PubMed=33713620; DOI=10.1016/j.cell.2021.02.053;
RA Yeung M.L., Teng J.L.L., Jia L., Zhang C., Huang C., Cai J.P., Zhou R.,
RA Chan K.H., Zhao H., Zhu L., Siu K.L., Fung S.Y., Yung S., Chan T.M.,
RA To K.K., Chan J.F., Cai Z., Lau S.K.P., Chen Z., Jin D.Y., Woo P.C.Y.,
RA Yuen K.Y.;
RT "Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with
RT proteins related to the renin-angiotensin system.";
RL Cell 0:0-0(2021).
RN [18] {ECO:0007744|PDB:4YAY}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 15-319, FUNCTION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BONDS, AND
RP MUTAGENESIS OF TRP-84; TYR-92; LYS-135; ARG-167; MET-284; PRO-285 AND
RP ILE-288.
RX PubMed=25913193; DOI=10.1016/j.cell.2015.04.011;
RA Zhang H., Unal H., Gati C., Han G.W., Liu W., Zatsepin N.A., James D.,
RA Wang D., Nelson G., Weierstall U., Sawaya M.R., Xu Q., Messerschmidt M.,
RA Williams G.J., Boutet S., Yefanov O.M., White T.A., Wang C., Ishchenko A.,
RA Tirupula K.C., Desnoyer R., Coe J., Conrad C.E., Fromme P., Stevens R.C.,
RA Katritch V., Karnik S.S., Cherezov V.;
RT "Structure of the Angiotensin receptor revealed by serial femtosecond
RT crystallography.";
RL Cell 161:833-844(2015).
RN [19] {ECO:0007744|PDB:4ZUD}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 15-315, FUNCTION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BONDS, AND
RP MUTAGENESIS OF TYR-35; TRP-84; ARG-167; PHE-182; LYS-199; ILE-288 AND
RP TYR-292.
RX PubMed=26420482; DOI=10.1074/jbc.m115.689000;
RA Zhang H., Unal H., Desnoyer R., Han G.W., Patel N., Katritch V.,
RA Karnik S.S., Cherezov V., Stevens R.C.;
RT "Structural Basis for Ligand Recognition and Functional Selectivity at
RT Angiotensin Receptor.";
RL J. Biol. Chem. 290:29127-29139(2015).
RN [20] {ECO:0007744|PDB:6DO1}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-319 IN COMPLEX WITH ANGIOTENSIN
RP II ANALOG, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-176.
RX PubMed=30639100; DOI=10.1016/j.cell.2018.12.006;
RA Wingler L.M., McMahon C., Staus D.P., Lefkowitz R.J., Kruse A.C.;
RT "Distinctive Activation Mechanism for Angiotensin Receptor Revealed by a
RT Synthetic Nanobody.";
RL Cell 176:479-490(2019).
RN [21] {ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-319 IN COMPLEX WITH ANGIOTENSIN
RP II, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-176, AND MUTAGENESIS OF LEU-112 AND TYR-292.
RX PubMed=32079768; DOI=10.1126/science.aay9813;
RA Wingler L.M., Skiba M.A., McMahon C., Staus D.P., Kleinhenz A.L.W.,
RA Suomivuori C.M., Latorraca N.R., Dror R.O., Lefkowitz R.J., Kruse A.C.;
RT "Angiotensin and biased analogs induce structurally distinct active
RT conformations within a GPCR.";
RL Science 367:888-892(2020).
RN [22]
RP VARIANT RTD MET-282.
RX PubMed=16116425; DOI=10.1038/ng1623;
RA Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N.,
RA Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L.,
RA Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M.,
RA Antignac C., Gubler M.-C.;
RT "Mutations in genes in the renin-angiotensin system are associated with
RT autosomal recessive renal tubular dysgenesis.";
RL Nat. Genet. 37:964-968(2005).
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:15611106, PubMed:1567413, PubMed:25913193,
CC PubMed:26420482, PubMed:30639100, PubMed:32079768, PubMed:8987975). The
CC activated receptor in turn couples to G-alpha proteins G(q) (GNAQ,
CC GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases
CC the cytosolic Ca(2+) concentrations, which in turn triggers cellular
CC responses such as stimulation of protein kinase C (PubMed:15611106).
CC {ECO:0000269|PubMed:15611106, ECO:0000269|PubMed:1567413,
CC ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482,
CC ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768,
CC ECO:0000269|PubMed:8987975}.
CC -!- FUNCTION: (Microbial infection) During SARS coronavirus-2/SARS-CoV-2
CC infection, it is able to recognize and internalize the complex formed
CC by secreted ACE2 and SARS-CoV-2 spike protein through DNM2/dynamin 2-
CC dependent endocytosis. {ECO:0000269|PubMed:33713620}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by anti-hypertensive drugs
CC losartan, candesartan, valsartan, irbesartan, telmisartan, eprosartan,
CC olmesartan and azilsartan, most of which share a common biphenyl-
CC tetrazole scaffold. {ECO:0000269|PubMed:25913193,
CC ECO:0000269|PubMed:26420482}.
CC -!- SUBUNIT: Interacts with MAS1 (PubMed:15809376). Interacts with ARRB1
CC (By similarity). Interacts with FLNA (via filamin repeat 21); increases
CC PKA-mediated phosphorylation of FLNA (PubMed:26460884).
CC {ECO:0000250|UniProtKB:P25095, ECO:0000269|PubMed:15809376,
CC ECO:0000269|PubMed:26460884, ECO:0000305}.
CC -!- INTERACTION:
CC P30556; PRO_0000032458 [P01019]: AGT; NbExp=2; IntAct=EBI-6623016, EBI-6622938;
CC P30556; P35414: APLNR; NbExp=14; IntAct=EBI-6623016, EBI-2875891;
CC P30556; P05026: ATP1B1; NbExp=2; IntAct=EBI-6623016, EBI-714630;
CC P30556; Q6ZMG9: CERS6; NbExp=2; IntAct=EBI-6623016, EBI-20794243;
CC P30556; O75937: DNAJC8; NbExp=2; IntAct=EBI-6623016, EBI-1045911;
CC P30556; P54368: OAZ1; NbExp=2; IntAct=EBI-6623016, EBI-948441;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33713620};
CC Multi-pass membrane protein {ECO:0000269|PubMed:25913193,
CC ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
CC ECO:0000269|PubMed:32079768}.
CC -!- TISSUE SPECIFICITY: Liver, lung, adrenal and adrenocortical adenomas.
CC {ECO:0000269|PubMed:1378723}.
CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC {ECO:0000303|PubMed:1378723}.
CC -!- DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal
CC recessive severe disorder of renal tubular development characterized by
CC persistent fetal anuria and perinatal death, probably due to pulmonary
CC hypoplasia from early-onset oligohydramnios (the Potter phenotype).
CC {ECO:0000269|PubMed:16116425}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Angiotensin receptor entry;
CC URL="https://en.wikipedia.org/wiki/Angiotensin_receptor";
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DR EMBL; M91464; AAA35569.1; -; Genomic_DNA.
DR EMBL; Z11162; CAA77513.1; -; Genomic_DNA.
DR EMBL; M87290; AAA35535.1; -; mRNA.
DR EMBL; S77410; AAB34644.1; -; mRNA.
DR EMBL; M93394; AAA58370.1; -; mRNA.
DR EMBL; D13814; BAA02968.1; -; mRNA.
DR EMBL; X65699; CAA46621.1; -; mRNA.
DR EMBL; AF245699; AAF70464.1; -; Genomic_DNA.
DR EMBL; AY221090; AAO65968.1; -; Genomic_DNA.
DR EMBL; BC022447; AAH22447.1; -; mRNA.
DR CCDS; CCDS3137.1; -.
DR PIR; I39418; I39418.
DR PIR; JC1104; JC1104.
DR RefSeq; NP_000676.1; NM_000685.4.
DR RefSeq; NP_004826.5; NM_004835.4.
DR RefSeq; NP_033611.1; NM_009585.3.
DR RefSeq; NP_114038.4; NM_031850.3.
DR RefSeq; NP_114438.2; NM_032049.3.
DR PDB; 4YAY; X-ray; 2.90 A; A=2-319.
DR PDB; 4ZUD; X-ray; 2.80 A; A=2-315.
DR PDB; 6DO1; X-ray; 2.90 A; A/B=2-319.
DR PDB; 6OS0; X-ray; 2.90 A; A=2-319.
DR PDB; 6OS1; X-ray; 2.79 A; A=2-319.
DR PDB; 6OS2; X-ray; 2.70 A; A=2-319.
DR PDBsum; 4YAY; -.
DR PDBsum; 4ZUD; -.
DR PDBsum; 6DO1; -.
DR PDBsum; 6OS0; -.
DR PDBsum; 6OS1; -.
DR PDBsum; 6OS2; -.
DR AlphaFoldDB; P30556; -.
DR EMDB; EMD-41248; -.
DR EMDB; EMD-41249; -.
DR SMR; P30556; -.
DR BioGRID; 106691; 95.
DR IntAct; P30556; 75.
DR MINT; P30556; -.
DR STRING; 9606.ENSP00000398832; -.
DR BindingDB; P30556; -.
DR ChEMBL; CHEMBL227; -.
DR DrugBank; DB11842; Angiotensin II.
DR DrugBank; DB08822; Azilsartan medoxomil.
DR DrugBank; DB13919; Candesartan.
DR DrugBank; DB00796; Candesartan cilexetil.
DR DrugBank; DB05739; CYT006-AngQb.
DR DrugBank; DB00876; Eprosartan.
DR DrugBank; DB09279; Fimasartan.
DR DrugBank; DB01342; Forasartan.
DR DrugBank; DB01029; Irbesartan.
DR DrugBank; DB00678; Losartan.
DR DrugBank; DB00275; Olmesartan.
DR DrugBank; DB01347; Saprisartan.
DR DrugBank; DB01349; Tasosartan.
DR DrugBank; DB00966; Telmisartan.
DR DrugBank; DB00177; Valsartan.
DR DrugCentral; P30556; -.
DR GuidetoPHARMACOLOGY; 34; -.
DR TCDB; 9.A.14.13.1; the g-protein-coupled receptor (gpcr) family.
DR GlyCosmos; P30556; 3 sites, No reported glycans.
DR GlyGen; P30556; 3 sites.
DR iPTMnet; P30556; -.
DR PhosphoSitePlus; P30556; -.
DR BioMuta; AGTR1; -.
DR DMDM; 231519; -.
DR jPOST; P30556; -.
DR MassIVE; P30556; -.
DR PaxDb; 9606-ENSP00000419422; -.
DR PeptideAtlas; P30556; -.
DR ProteomicsDB; 54721; -.
DR ABCD; P30556; 3 sequenced antibodies.
DR Antibodypedia; 1002; 608 antibodies from 41 providers.
DR DNASU; 185; -.
DR Ensembl; ENST00000349243.8; ENSP00000273430.3; ENSG00000144891.19.
DR Ensembl; ENST00000402260.2; ENSP00000385641.3; ENSG00000144891.19.
DR Ensembl; ENST00000404754.2; ENSP00000385612.2; ENSG00000144891.19.
DR Ensembl; ENST00000418473.7; ENSP00000398832.4; ENSG00000144891.19.
DR Ensembl; ENST00000461609.1; ENSP00000418851.1; ENSG00000144891.19.
DR Ensembl; ENST00000474935.5; ENSP00000418084.1; ENSG00000144891.19.
DR Ensembl; ENST00000475347.5; ENSP00000419783.1; ENSG00000144891.19.
DR Ensembl; ENST00000497524.5; ENSP00000419422.1; ENSG00000144891.19.
DR GeneID; 185; -.
DR KEGG; hsa:185; -.
DR MANE-Select; ENST00000349243.8; ENSP00000273430.3; NM_000685.5; NP_000676.1.
DR AGR; HGNC:336; -.
DR CTD; 185; -.
DR DisGeNET; 185; -.
DR GeneCards; AGTR1; -.
DR HGNC; HGNC:336; AGTR1.
DR HPA; ENSG00000144891; Tissue enhanced (liver, placenta).
DR MalaCards; AGTR1; -.
DR MIM; 106165; gene.
DR MIM; 267430; phenotype.
DR neXtProt; NX_P30556; -.
DR OpenTargets; ENSG00000144891; -.
DR Orphanet; 97369; Renal tubular dysgenesis of genetic origin.
DR PharmGKB; PA43; -.
DR VEuPathDB; HostDB:ENSG00000144891; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01120000271868; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P30556; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 4179713at2759; -.
DR PhylomeDB; P30556; -.
DR TreeFam; TF330024; -.
DR PathwayCommons; P30556; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P30556; -.
DR SIGNOR; P30556; -.
DR BioGRID-ORCS; 185; 17 hits in 1153 CRISPR screens.
DR ChiTaRS; AGTR1; human.
DR EvolutionaryTrace; P30556; -.
DR GeneWiki; Angiotensin_II_receptor_type_1; -.
DR GenomeRNAi; 185; -.
DR Pharos; P30556; Tclin.
DR PRO; PR:P30556; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P30556; protein.
DR Bgee; ENSG00000144891; Expressed in skin of hip and 157 other cell types or tissues.
DR ExpressionAtlas; P30556; baseline and differential.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001596; F:angiotensin type I receptor activity; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IDA:BHF-UCL.
DR GO; GO:0031711; F:bradykinin receptor binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IC:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; NAS:BHF-UCL.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; IDA:UniProtKB.
DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; TAS:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; IMP:BHF-UCL.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:BHF-UCL.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; TAS:BHF-UCL.
DR GO; GO:0001558; P:regulation of cell growth; NAS:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; NAS:BHF-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0035813; P:regulation of renal sodium excretion; NAS:BHF-UCL.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IC:BHF-UCL.
DR GO; GO:0019229; P:regulation of vasoconstriction; IDA:BHF-UCL.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; NAS:BHF-UCL.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0046718; P:symbiont entry into host cell; IDA:UniProtKB.
DR CDD; cd15192; 7tmA_AT1R; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000190; ATII_AT1_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR050119; GPCR1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF951; APELIN RECEPTOR; 1.
DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 3D-structure; Cell membrane; Disease variant; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Host-virus interaction;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Proteomics identification; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor"
FT /id="PRO_0000069153"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TRANSMEM 26..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TOPO_DOM 56..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TRANSMEM 62..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TOPO_DOM 90..98
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TRANSMEM 99..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TOPO_DOM 126..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TRANSMEM 142..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TOPO_DOM 166..190
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TRANSMEM 191..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT TOPO_DOM 217..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD"
FT TRANSMEM 240..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD"
FT TOPO_DOM 269..278
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD"
FT TRANSMEM 279..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD"
FT TOPO_DOM 305..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..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:0000305|PubMed:30639100,
FT ECO:0007744|PDB:6DO1"
FT BINDING 17
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT BINDING 167
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT BINDING 182
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT BINDING 183
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT BINDING 184
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT BINDING 199
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:30639100,
FT ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT LIPID 355
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..274
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100,
FT ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY,
FT ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1,
FT ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1,
FT ECO:0007744|PDB:6OS2"
FT DISULFID 101..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482,
FT ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768,
FT ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD,
FT ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0,
FT ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2"
FT VARIANT 163
FT /note="A -> T (in dbSNP:rs12721226)"
FT /id="VAR_029206"
FT VARIANT 222
FT /note="L -> V (in dbSNP:rs17852013)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_070375"
FT VARIANT 244
FT /note="A -> S (in dbSNP:rs12721225)"
FT /id="VAR_029207"
FT VARIANT 282
FT /note="T -> M (in RTD; dbSNP:rs104893677)"
FT /evidence="ECO:0000269|PubMed:16116425"
FT /id="VAR_035086"
FT VARIANT 289
FT /note="C -> W (in dbSNP:rs1064533)"
FT /evidence="ECO:0000269|PubMed:8135787"
FT /id="VAR_011847"
FT VARIANT 336
FT /note="T -> P (in dbSNP:rs1801021)"
FT /id="VAR_011848"
FT VARIANT 341
FT /note="P -> H (in dbSNP:rs17852012)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_070376"
FT MUTAGEN 35
FT /note="Y->A,F: Abolished binding to angiotensin II;
FT abolished binding to olmesartan inhibitor."
FT /evidence="ECO:0000269|PubMed:26420482"
FT MUTAGEN 84
FT /note="W->A,I: Abolished binding to angiotensin II;
FT abolished binding to olmesartan inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482"
FT MUTAGEN 92
FT /note="Y->A: Decreased binding to telmisartan inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193"
FT MUTAGEN 111
FT /note="N->A,F,I: Reduced affinity for angiotensin II."
FT /evidence="ECO:0000269|PubMed:8987975"
FT MUTAGEN 111
FT /note="N->G: Induces a conformational change in the
FT angiotensin II-binding pocket, leading to constitutive
FT activation of the receptor."
FT /evidence="ECO:0000269|PubMed:8987975"
FT MUTAGEN 112
FT /note="L->A: Increased affinity for angiotensin II."
FT /evidence="ECO:0000269|PubMed:32079768"
FT MUTAGEN 135
FT /note="K->A: Abolished binding to angiotensin II."
FT /evidence="ECO:0000269|PubMed:25913193"
FT MUTAGEN 167
FT /note="R->A: Abolished binding to angiotensin II; abolished
FT binding to olmesartan inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482"
FT MUTAGEN 182
FT /note="F->A: Reduced binding to angiotensin II without
FT affecting binding to candesartan inhibitor."
FT /evidence="ECO:0000269|PubMed:26420482"
FT MUTAGEN 199
FT /note="K->R,Q: Abolished binding to angiotensin II."
FT /evidence="ECO:0000269|PubMed:26420482"
FT MUTAGEN 284
FT /note="M->A: Slightly affects binding to eprosartan
FT inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193"
FT MUTAGEN 285
FT /note="P->A: Decreased binding to eprosartan inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193"
FT MUTAGEN 288
FT /note="I->A: Decreased binding to eprosartan inhibitor."
FT /evidence="ECO:0000269|PubMed:25913193,
FT ECO:0000269|PubMed:26420482"
FT MUTAGEN 292
FT /note="Y->A: Mimics the disordered side chain induced by
FT angiotensin II-binding; increased affinity for G-protein
FT subunit alpha proteins. Decreased affinity for
FT telmisartan."
FT /evidence="ECO:0000269|PubMed:26420482,
FT ECO:0000269|PubMed:32079768"
FT CONFLICT 187
FT /note="Q -> R (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..205
FT /note="FL -> SC (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="K -> N (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="K -> R (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="L -> Q (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..313
FT /note="RYF -> KDI (in Ref. 6; BAA02968)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6OS2"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 25..56
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 97..131
FT /evidence="ECO:0007829|PDB:6OS2"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6OS2"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6OS2"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6OS2"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:6OS2"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:6OS2"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4ZUD"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6OS2"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 238..267
FT /evidence="ECO:0007829|PDB:6OS2"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4YAY"
FT HELIX 274..295
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:6OS2"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:6OS2"
SQ SEQUENCE 359 AA; 41061 MW; 35FC856F53E911A6 CRC64;
MILNSSTEDG IKRIQDDCPK AGRHNYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNYL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLLAGLAS LPAIIHRNVF FIENTNITVC
AFHYESQNST LPIGLGLTKN ILGFLFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFK
IIMAIVLFFF FSWIPHQIFT FLDVLIQLGI IRDCRIADIV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK RYFLQLLKYI PPKAKSHSNL STKMSTLSYR PSDNVSSSTK KPAPCFEVE
//