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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //