ANGT_HUMAN
ID ANGT_HUMAN Reviewed; 485 AA.
AC P01019; Q16358; Q16359; Q96F91;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 3.
DT 03-AUG-2022, entry version 243.
DE RecName: Full=Angiotensinogen;
DE AltName: Full=Serpin A8;
DE Contains:
DE RecName: Full=Angiotensin-1;
DE AltName: Full=Angiotensin 1-10;
DE AltName: Full=Angiotensin I;
DE Short=Ang I;
DE Contains:
DE RecName: Full=Angiotensin-2;
DE AltName: Full=Angiotensin 1-8;
DE AltName: Full=Angiotensin II;
DE Short=Ang II;
DE Contains:
DE RecName: Full=Angiotensin-3;
DE AltName: Full=Angiotensin 2-8;
DE AltName: Full=Angiotensin III;
DE Short=Ang III;
DE AltName: Full=Des-Asp[1]-angiotensin II;
DE Contains:
DE RecName: Full=Angiotensin-4;
DE AltName: Full=Angiotensin 3-8;
DE AltName: Full=Angiotensin IV;
DE Short=Ang IV;
DE Contains:
DE RecName: Full=Angiotensin 1-9;
DE Contains:
DE RecName: Full=Angiotensin 1-7;
DE Contains:
DE RecName: Full=Angiotensin 1-5;
DE Contains:
DE RecName: Full=Angiotensin 1-4;
DE Flags: Precursor;
GN Name=AGT; Synonyms=SERPINA8;
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 [MRNA].
RX PubMed=6089875; DOI=10.1021/bi00311a006;
RA Kageyama R., Ohkubo H., Nakanishi S.;
RT "Primary structure of human preangiotensinogen deduced from the cloned cDNA
RT sequence.";
RL Biochemistry 23:3603-3609(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2924688; DOI=10.1089/dna.1.1989.8.87;
RA Gaillard I., Clauser E., Corvol P.;
RT "Structure of human angiotensinogen gene.";
RL DNA 8:87-99(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1692023; DOI=10.1016/s0021-9258(19)39153-7;
RA Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S.,
RA Murakami K.;
RT "Structure and expression of the human angiotensinogen gene. Identification
RT of a unique and highly active promoter.";
RL J. Biol. Chem. 265:7576-7582(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-335.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-338.
RX PubMed=2885106; DOI=10.1161/01.res.60.5.786;
RA Kunapuli S.P., Kumar A.;
RT "Molecular cloning of human angiotensinogen cDNA and evidence for the
RT presence of its mRNA in rat heart.";
RL Circ. Res. 60:786-790(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-184.
RX PubMed=3579322; DOI=10.1016/0003-9861(87)90148-2;
RA Kunapuli S.P., Benedict C.R., Kumar A.;
RT "Tissue specific hormonal regulation of the rat angiotensinogen gene
RT expression.";
RL Arch. Biochem. Biophys. 254:642-646(1987).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-242; ARG-244
RP AND CYS-281.
RX PubMed=7607642; DOI=10.1007/bf00214197;
RA Hixson J.E., Powers P.K.;
RT "Detection and characterization of new mutations in the human
RT angiotensinogen gene (AGT).";
RL Hum. Genet. 96:110-112(1995).
RN [8]
RP PROTEIN SEQUENCE OF 34-58.
RX PubMed=7259779; DOI=10.1016/0006-291x(81)90762-2;
RA Tewksbury D.A., Dart R.A., Travis J.;
RT "The amino terminal amino acid sequence of human angiotensinogen.";
RL Biochem. Biophys. Res. Commun. 99:1311-1315(1981).
RN [9]
RP PROTEIN SEQUENCE OF 34-45, AND SUBUNIT.
RC TISSUE=Serum;
RX PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T.,
RA Gleich G.J., Sottrup-Jensen L.;
RT "Identification of angiotensinogen and complement C3dg as novel proteins
RT binding the proform of eosinophil major basic protein in human pregnancy
RT serum and plasma.";
RL J. Biol. Chem. 270:13645-13651(1995).
RN [10]
RP PROTEIN SEQUENCE OF 34-43.
RX PubMed=4300938; DOI=10.1016/0005-2795(68)90239-0;
RA Arakawa K., Minohara A., Yamada J., Nakamura M.;
RT "Enzymatic degradation and electrophoresis of human angiotensin I.";
RL Biochim. Biophys. Acta 168:106-112(1968).
RN [11]
RP CLEAVAGE.
RX PubMed=4322742; DOI=10.1016/0005-2795(70)90017-6;
RA Yang H.Y., Erdoes E.G., Levin Y.;
RT "A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates
RT bradykinin.";
RL Biochim. Biophys. Acta 214:374-376(1970).
RN [12]
RP GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328.
RX PubMed=3934016; DOI=10.1016/0303-7207(85)90039-5;
RA Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.;
RT "Processing of rat and human angiotensinogen precursors by microsomal
RT membranes.";
RL Mol. Cell. Endocrinol. 43:31-40(1985).
RN [13]
RP FUNCTION OF ANGIOTENSIN-3.
RX PubMed=1132082; DOI=10.1161/01.res.36.6.38;
RA Goodfriend T.L., Peach M.J.;
RT "Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and
RT speculation for its role as an important agonist in the renin - angiotensin
RT system.";
RL Circ. Res. 36:38-48(1975).
RN [14]
RP FUNCTION OF ANGIOTENSIN-2.
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 [15]
RP FUNCTION OF ANGIOTENSIN-2.
RX PubMed=8185599; DOI=10.1006/bbrc.1994.1613;
RA Tsuzuki S., Ichiki T., Nakakubo H., Kitami Y., Guo D.F., Shirai H.,
RA Inagami T.;
RT "Molecular cloning and expression of the gene encoding human angiotensin II
RT type 2 receptor.";
RL Biochem. Biophys. Res. Commun. 200:1449-1454(1994).
RN [16]
RP FUNCTION OF ANGIOTENSIN-2.
RX PubMed=10619573; DOI=10.1016/s0895-7061(99)00103-x;
RA Weir M.R., Dzau V.J.;
RT "The renin-angiotensin-aldosterone system: a specific target for
RT hypertension management.";
RL Am. J. Hypertens. 12:205S-213S(1999).
RN [17]
RP CLEAVAGE BY ACE AND ACE2.
RX PubMed=10969042; DOI=10.1161/01.res.87.5.e1;
RA Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N.,
RA Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.;
RT "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2)
RT converts angiotensin I to angiotensin 1-9.";
RL Circ. Res. 87:E1-E9(2000).
RN [18]
RP CLEAVAGE OF ANGIOTENSIN-1 AND ANGIOTENSIN-2 BY ACE2.
RX PubMed=11815627; DOI=10.1074/jbc.m200581200;
RA Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K.,
RA Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A.,
RA Tummino P.;
RT "Hydrolysis of biological peptides by human angiotensin-converting enzyme-
RT related carboxypeptidase.";
RL J. Biol. Chem. 277:14838-14843(2002).
RN [19]
RP CLEAVAGE BY RENIN.
RX PubMed=12045255; DOI=10.1172/jci14276;
RA Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.;
RT "Pivotal role of the renin/prorenin receptor in angiotensin II production
RT and cellular responses to renin.";
RL J. Clin. Invest. 109:1417-1427(2002).
RN [20]
RP CLEAVAGE.
RX PubMed=15283675; DOI=10.1042/bj20040634;
RA Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.;
RT "Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and
RT neprilysin in angiotensin peptide metabolism.";
RL Biochem. J. 383:45-51(2004).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [22]
RP DECARBOXYLATION AT ASP-34, FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17138938; DOI=10.1161/01.atv.0000253889.09765.5f;
RA Jankowski V., Vanholder R., van der Giet M., Tolle M., Karadogan S.,
RA Gobom J., Furkert J., Oksche A., Krause E., Tran T.N., Tepel M.,
RA Schuchardt M., Schluter H., Wiedon A., Beyermann M., Bader M., Todiras M.,
RA Zidek W., Jankowski J.;
RT "Mass-spectrometric identification of a novel angiotensin peptide in human
RT plasma.";
RL Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007).
RN [23]
RP REVIEW ON THE RENIN-ANGIOTENSIN SYSTEM.
RX PubMed=18793332; DOI=10.1111/j.1365-2796.2008.01981.x;
RA Fyhrquist F., Saijonmaa O.;
RT "Renin-angiotensin system revisited.";
RL J. Intern. Med. 264:224-236(2008).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP STRUCTURE BY NMR OF ANGIOTENSIN-2.
RX PubMed=9492317; DOI=10.1046/j.1432-1327.1998.2510448.x;
RA Carpenter K.A., Wilkes B.C., Schiller P.W.;
RT "The octapeptide angiotensin II adopts a well-defined structure in a
RT phospholipid environment.";
RL Eur. J. Biochem. 251:448-453(1998).
RN [28]
RP STRUCTURE BY NMR OF 34-43, AND STRUCTURE BY NMR OF 34-41.
RX PubMed=12752436; DOI=10.1046/j.1432-1033.2003.03573.x;
RA Spyroulias G.A., Nikolakopoulou P., Tzakos A., Gerothanassis I.P.,
RA Magafa V., Manessi-Zoupa E., Cordopatis P.;
RT "Comparison of the solution structures of angiotensin I & II. Implication
RT for structure-function relationship.";
RL Eur. J. Biochem. 270:2163-2173(2003).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 34-485 IN COMPLEX WITH RENIN, AND
RP DISULFIDE BOND.
RX PubMed=20927107; DOI=10.1038/nature09505;
RA Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L.,
RA Stein P.E., Broughton Pipkin F., Read R.J.;
RT "A redox switch in angiotensinogen modulates angiotensin release.";
RL Nature 468:108-111(2010).
RN [30]
RP VARIANTS MET-207; THR-268 AND CYS-281.
RX PubMed=1394429; DOI=10.1016/0092-8674(92)90275-h;
RA Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., Williams C.S.,
RA Charru A., Hunt S.C., Hopkins P.N., Williams R.R., Lalouel J.-M.,
RA Corvol P.;
RT "Molecular basis of human hypertension: role of angiotensinogen.";
RL Cell 71:169-180(1992).
RN [31]
RP VARIANT THR-268.
RX PubMed=8513325; DOI=10.1038/ng0593-59;
RA Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C.,
RA Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S.,
RA Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.;
RT "A molecular variant of angiotensinogen associated with preeclampsia.";
RL Nat. Genet. 4:59-61(1993).
RN [32]
RP VARIANT PHE-43.
RX PubMed=7744780; DOI=10.1074/jbc.270.19.11430;
RA Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P., Bohlender J.,
RA Lifton R.P., Corvol P., Ward K., Lalouel J.-M.;
RT "A mutation of angiotensinogen in a patient with preeclampsia leads to
RT altered kinetics of the renin-angiotensin system.";
RL J. Biol. Chem. 270:11430-11436(1995).
RN [33]
RP CHARACTERIZATION OF VARIANT CYS-281.
RX PubMed=8621667; DOI=10.1074/jbc.271.16.9838;
RA Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T.,
RA Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.;
RT "The natural mutation Y248C of human angiotensinogen leads to abnormal
RT glycosylation and altered immunological recognition of the protein.";
RL J. Biol. Chem. 271:9838-9844(1996).
RN [34]
RP VARIANT RTD GLN-375.
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: Essential component of the renin-angiotensin system (RAS), a
CC potent regulator of blood pressure, body fluid and electrolyte
CC homeostasis. {ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1132082,
CC ECO:0000269|PubMed:17138938}.
CC -!- FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a
CC potent vasoconstrictor, affects cardiac contractility and heart rate
CC through its action on the sympathetic nervous system, and alters renal
CC sodium and water absorption through its ability to stimulate the zona
CC glomerulosa cells of the adrenal cortex to synthesize and secrete
CC aldosterone (PubMed:10619573, PubMed:17138938). Acts by binding to
CC angiotensin receptors AGTR1 and AGTR2 (PubMed:1567413). Also binds the
CC DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P01015,
CC ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1567413,
CC ECO:0000269|PubMed:17138938}.
CC -!- FUNCTION: [Angiotensin-3]: Stimulates aldosterone release.
CC {ECO:0000269|PubMed:1132082}.
CC -!- FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled
CC receptor MAS1 (By similarity). Has vasodilator and antidiuretic
CC effects. Has an antithrombotic effect that involves MAS1-mediated
CC release of nitric oxide from platelets (By similarity).
CC {ECO:0000250|UniProtKB:P11859}.
CC -!- SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2
CC heterotetramer with the proform of PRG2 and as a complex (probably a
CC 2:2:2 heterohexamer) with pro-PRG2 and C3dg.
CC {ECO:0000269|PubMed:20927107, ECO:0000269|PubMed:7539791}.
CC -!- INTERACTION:
CC P01019; Q8TAB7: CCDC26; NbExp=3; IntAct=EBI-751728, EBI-10271580;
CC P01019; Q9UI10: EIF2B4; NbExp=3; IntAct=EBI-751728, EBI-2340132;
CC P01019; O00746: NME4; NbExp=3; IntAct=EBI-751728, EBI-744871;
CC P01019; C9J082: NPHP1; NbExp=3; IntAct=EBI-751728, EBI-25830675;
CC P01019; O14744: PRMT5; NbExp=3; IntAct=EBI-751728, EBI-351098;
CC P01019; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-751728, EBI-10272071;
CC P01019; P00797: REN; NbExp=2; IntAct=EBI-751728, EBI-715794;
CC P01019; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-751728, EBI-2822550;
CC P01019; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-751728, EBI-1752602;
CC P01019; O43493-5: TGOLN2; NbExp=3; IntAct=EBI-751728, EBI-25830716;
CC P01019; Q8NFB2: TMEM185A; NbExp=3; IntAct=EBI-751728, EBI-21757569;
CC P01019; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-751728, EBI-11337915;
CC P01019; P25095: Agtr1; Xeno; NbExp=10; IntAct=EBI-751728, EBI-764979;
CC P01019; Q10714: Ance; Xeno; NbExp=2; IntAct=EBI-751728, EBI-115736;
CC PRO_0000032457; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-25493366, EBI-7730807;
CC PRO_0000032458; Q9BYF1: ACE2; NbExp=5; IntAct=EBI-6622938, EBI-7730807;
CC PRO_0000032458; P30556: AGTR1; NbExp=2; IntAct=EBI-6622938, EBI-6623016;
CC PRO_0000032459; P50052: AGTR2; NbExp=2; IntAct=EBI-2927577, EBI-1748067;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:4300938,
CC ECO:0000305|PubMed:7259779, ECO:0000305|PubMed:7539791}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC {ECO:0000269|PubMed:1692023}.
CC -!- PTM: Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear
CC leukocytes produces alanine (PubMed:17138938). The resulting peptide
CC form, angiotensin-A, has the same affinity for the AT1 receptor as
CC angiotensin-2, but a higher affinity for the AT2 receptor
CC (PubMed:17138938). {ECO:0000269|PubMed:17138938}.
CC -!- PTM: In response to low blood pressure, the enzyme renin/REN cleaves
CC angiotensinogen to produce angiotensin-1 (PubMed:12045255).
CC Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme)
CC that removes a dipeptide to yield the physiologically active peptide
CC angiotensin-2 (PubMed:4322742, PubMed:10969042). Angiotensin-1 and
CC angiotensin-2 can be further processed to generate angiotensin-3,
CC angiotensin-4 (PubMed:10969042, PubMed:11815627). Angiotensin 1-9 is
CC cleaved from angiotensin-1 by ACE2 and can be further processed by ACE
CC to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4
CC (PubMed:10969042, PubMed:11815627). Angiotensin 1-7 has also been
CC proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1
CC by MME (neprilysin) (PubMed:15283675). {ECO:0000269|PubMed:10969042,
CC ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:12045255,
CC ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:4322742}.
CC -!- PTM: The disulfide bond is labile. Angiotensinogen is present in the
CC circulation in a near 40:60 ratio with the oxidized disulfide-bonded
CC form, which preferentially interacts with receptor-bound renin.
CC {ECO:0000269|PubMed:20927107}.
CC -!- DISEASE: Essential hypertension (EHT) [MIM:145500]: A condition in
CC which blood pressure is consistently higher than normal with no
CC identifiable cause. {ECO:0000269|PubMed:1394429,
CC ECO:0000269|PubMed:8513325}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
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 serpin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51679.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA51731.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA52282.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH11519.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA33385.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Angiotensin entry;
CC URL="https://en.wikipedia.org/wiki/Angiotensin";
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DR EMBL; K02215; AAA51731.1; ALT_INIT; mRNA.
DR EMBL; M24689; AAA51679.1; ALT_INIT; Genomic_DNA.
DR EMBL; M24686; AAA51679.1; JOINED; Genomic_DNA.
DR EMBL; M24687; AAA51679.1; JOINED; Genomic_DNA.
DR EMBL; M24688; AAA51679.1; JOINED; Genomic_DNA.
DR EMBL; X15324; CAA33385.1; ALT_INIT; Genomic_DNA.
DR EMBL; X15325; CAA33385.1; JOINED; Genomic_DNA.
DR EMBL; X15326; CAA33385.1; JOINED; Genomic_DNA.
DR EMBL; X15327; CAA33385.1; JOINED; Genomic_DNA.
DR EMBL; BC011519; AAH11519.1; ALT_INIT; mRNA.
DR EMBL; M69110; AAA52282.1; ALT_INIT; mRNA.
DR EMBL; S78529; AAD14287.1; -; Genomic_DNA.
DR EMBL; S78530; AAD14288.1; -; Genomic_DNA.
DR CCDS; CCDS1585.1; -.
DR PIR; A35203; ANHU.
DR RefSeq; NP_000020.1; NM_000029.3.
DR PDB; 1N9U; NMR; -; A=34-43.
DR PDB; 1N9V; NMR; -; A=34-41.
DR PDB; 2JP8; NMR; -; P=34-40.
DR PDB; 2WXW; X-ray; 3.30 A; A=34-485.
DR PDB; 2X0B; X-ray; 4.33 A; B/D/F/H=34-485.
DR PDB; 3CK0; X-ray; 3.00 A; P=34-41.
DR PDB; 3WOO; X-ray; 1.80 A; C/D=36-41.
DR PDB; 3WOR; X-ray; 2.10 A; C/D=34-41.
DR PDB; 4AA1; X-ray; 1.99 A; P=34-41.
DR PDB; 4APH; X-ray; 1.99 A; P=34-41.
DR PDB; 4FYS; X-ray; 2.01 A; C=36-41.
DR PDB; 5E2Q; X-ray; 2.40 A; B=34-41.
DR PDB; 5M3X; X-ray; 2.63 A; A/B=44-485.
DR PDB; 5M3Y; X-ray; 2.30 A; A=34-485.
DR PDB; 5XJM; X-ray; 3.20 A; B=35-40.
DR PDB; 6I3F; X-ray; 2.55 A; A=34-485.
DR PDB; 6I3I; X-ray; 2.97 A; A=34-485.
DR PDB; 6JOD; X-ray; 3.20 A; B=34-41.
DR PDB; 6OS0; X-ray; 2.90 A; B=34-41.
DR PDB; 7C6A; X-ray; 3.40 A; B=35-40.
DR PDBsum; 1N9U; -.
DR PDBsum; 1N9V; -.
DR PDBsum; 2JP8; -.
DR PDBsum; 2WXW; -.
DR PDBsum; 2X0B; -.
DR PDBsum; 3CK0; -.
DR PDBsum; 3WOO; -.
DR PDBsum; 3WOR; -.
DR PDBsum; 4AA1; -.
DR PDBsum; 4APH; -.
DR PDBsum; 4FYS; -.
DR PDBsum; 5E2Q; -.
DR PDBsum; 5M3X; -.
DR PDBsum; 5M3Y; -.
DR PDBsum; 5XJM; -.
DR PDBsum; 6I3F; -.
DR PDBsum; 6I3I; -.
DR PDBsum; 6JOD; -.
DR PDBsum; 6OS0; -.
DR PDBsum; 7C6A; -.
DR AlphaFoldDB; P01019; -.
DR SMR; P01019; -.
DR BioGRID; 106690; 32.
DR CORUM; P01019; -.
DR DIP; DIP-309N; -.
DR IntAct; P01019; 26.
DR MINT; P01019; -.
DR STRING; 9606.ENSP00000355627; -.
DR ChEMBL; CHEMBL3596085; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12548; Sparsentan.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR MEROPS; I04.953; -.
DR CarbonylDB; P01019; -.
DR GlyConnect; 703; 12 N-Linked glycans (3 sites).
DR GlyGen; P01019; 5 sites, 20 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P01019; -.
DR PhosphoSitePlus; P01019; -.
DR BioMuta; AGT; -.
DR DMDM; 113880; -.
DR SWISS-2DPAGE; P01019; -.
DR EPD; P01019; -.
DR jPOST; P01019; -.
DR MassIVE; P01019; -.
DR MaxQB; P01019; -.
DR PaxDb; P01019; -.
DR PeptideAtlas; P01019; -.
DR PRIDE; P01019; -.
DR ProteomicsDB; 51306; -.
DR ABCD; P01019; 5 sequenced antibodies.
DR Antibodypedia; 866; 1067 antibodies from 42 providers.
DR DNASU; 183; -.
DR Ensembl; ENST00000366667.6; ENSP00000355627.5; ENSG00000135744.9.
DR Ensembl; ENST00000679738.1; ENSP00000505063.1; ENSG00000135744.9.
DR Ensembl; ENST00000680041.1; ENSP00000504866.1; ENSG00000135744.9.
DR Ensembl; ENST00000681269.1; ENSP00000505985.1; ENSG00000135744.9.
DR Ensembl; ENST00000681514.1; ENSP00000505963.1; ENSG00000135744.9.
DR GeneID; 183; -.
DR MANE-Select; ENST00000366667.6; ENSP00000355627.5; NM_001384479.1; NP_001371408.1.
DR UCSC; uc001hty.6; human.
DR CTD; 183; -.
DR DisGeNET; 183; -.
DR GeneCards; AGT; -.
DR HGNC; HGNC:333; AGT.
DR HPA; ENSG00000135744; Tissue enriched (liver).
DR MalaCards; AGT; -.
DR MIM; 106150; gene.
DR MIM; 145500; phenotype.
DR MIM; 267430; phenotype.
DR neXtProt; NX_P01019; -.
DR OpenTargets; ENSG00000135744; -.
DR Orphanet; 243761; NON RARE IN EUROPE: Essential hypertension.
DR Orphanet; 97369; Renal tubular dysgenesis of genetic origin.
DR PharmGKB; PA42; -.
DR VEuPathDB; HostDB:ENSG00000135744; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00890000139531; -.
DR HOGENOM; CLU_045267_1_0_1; -.
DR InParanoid; P01019; -.
DR OMA; FMGFRMY; -.
DR OrthoDB; 450590at2759; -.
DR PhylomeDB; P01019; -.
DR TreeFam; TF343201; -.
DR PathwayCommons; P01019; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P01019; -.
DR SIGNOR; P01019; -.
DR BioGRID-ORCS; 183; 15 hits in 1072 CRISPR screens.
DR ChiTaRS; AGT; human.
DR EvolutionaryTrace; P01019; -.
DR GeneWiki; Angiotensin; -.
DR GenomeRNAi; 183; -.
DR Pharos; P01019; Tbio.
DR PRO; PR:P01019; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P01019; protein.
DR Bgee; ENSG00000135744; Expressed in liver and 179 other tissues.
DR Genevisible; P01019; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0008083; F:growth factor activity; TAS:BHF-UCL.
DR GO; GO:0005179; F:hormone activity; ISS:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; TAS:BHF-UCL.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IPI:BHF-UCL.
DR GO; GO:0031703; F:type 2 angiotensin receptor binding; IPI:BHF-UCL.
DR GO; GO:0007202; P:activation of phospholipase C activity; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; IEA:Ensembl.
DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; TAS:BHF-UCL.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; TAS:BHF-UCL.
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; TAS:BHF-UCL.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:CACAO.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; TAS:BHF-UCL.
DR GO; GO:0034104; P:negative regulation of tissue remodeling; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:BHF-UCL.
DR GO; GO:0035106; P:operant conditioning; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; NAS:BHF-UCL.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IMP:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IDA:UniProtKB.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IDA:BHF-UCL.
DR GO; GO:0001819; P:positive regulation of cytokine production; TAS:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:BHF-UCL.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IGI:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; TAS:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; IEA:Ensembl.
DR GO; GO:1905010; P:positive regulation of L-lysine import across plasma membrane; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
DR GO; GO:1902632; P:positive regulation of membrane hyperpolarization; IMP:BHF-UCL.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; TAS:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:BHF-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:BHF-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; TAS:BHF-UCL.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IGI:BHF-UCL.
DR GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; NAS:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:1903779; P:regulation of cardiac conduction; IGI: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:1901201; P:regulation of extracellular matrix assembly; IGI:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; IEA:Ensembl.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; NAS:BHF-UCL.
DR GO; GO:0035813; P:regulation of renal sodium excretion; NAS:BHF-UCL.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; NAS:BHF-UCL.
DR GO; GO:0003014; P:renal system process; IDA:UniProtKB.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; NAS:BHF-UCL.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:BHF-UCL.
DR GO; GO:0048659; P:smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0070471; P:uterine smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR CDD; cd02054; serpinA8_AGT; 1.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR000227; Angiotensinogen.
DR InterPro; IPR033834; Angiotensinogen_serpin_dom.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF331; PTHR11461:SF331; 1.
DR Pfam; PF00079; Serpin; 1.
DR PRINTS; PR00654; ANGIOTENSNGN.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal; Vasoactive;
KW Vasoconstrictor.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:4300938,
FT ECO:0000269|PubMed:7259779, ECO:0000269|PubMed:7539791"
FT CHAIN 34..485
FT /note="Angiotensinogen"
FT /id="PRO_0000032456"
FT PEPTIDE 34..43
FT /note="Angiotensin-1"
FT /evidence="ECO:0000269|PubMed:4300938"
FT /id="PRO_0000032457"
FT PEPTIDE 34..42
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000305|PubMed:10969042"
FT /id="PRO_0000420659"
FT PEPTIDE 34..41
FT /note="Angiotensin-2"
FT /evidence="ECO:0000305|PubMed:11815627,
FT ECO:0000305|PubMed:9492317"
FT /id="PRO_0000032458"
FT PEPTIDE 34..40
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000305|PubMed:15283675"
FT /id="PRO_0000420660"
FT PEPTIDE 34..38
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000305|PubMed:10969042,
FT ECO:0000305|PubMed:11815627"
FT /id="PRO_0000420661"
FT PEPTIDE 34..37
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000305|PubMed:10969042,
FT ECO:0000305|PubMed:11815627"
FT /id="PRO_0000420662"
FT PEPTIDE 35..41
FT /note="Angiotensin-3"
FT /evidence="ECO:0000305|PubMed:10969042,
FT ECO:0000305|PubMed:1132082, ECO:0000305|PubMed:11815627"
FT /id="PRO_0000032459"
FT PEPTIDE 36..41
FT /note="Angiotensin-4"
FT /evidence="ECO:0000305|PubMed:10969042,
FT ECO:0000305|PubMed:11815627"
FT /id="PRO_0000420663"
FT MOD_RES 34
FT /note="Beta-decarboxylated aspartate; in form angiotensin-
FT A"
FT /evidence="ECO:0000269|PubMed:17138938"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3934016"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3934016"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3934016"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3934016"
FT DISULFID 51..171
FT /evidence="ECO:0000269|PubMed:20927107"
FT VARIANT 43
FT /note="L -> F (associated with susceptibility to pre-
FT eclampsia; alters the reactions with renin and angiotensin-
FT converting enzyme; dbSNP:rs41271499)"
FT /evidence="ECO:0000269|PubMed:7744780"
FT /id="VAR_022933"
FT VARIANT 98
FT /note="E -> K (in dbSNP:rs11568032)"
FT /id="VAR_029166"
FT VARIANT 114
FT /note="G -> C (in dbSNP:rs2229389)"
FT /id="VAR_051939"
FT VARIANT 137
FT /note="T -> M (in dbSNP:rs34829218)"
FT /id="VAR_035431"
FT VARIANT 207
FT /note="T -> M (associated with hypertension; dbSNP:rs4762)"
FT /evidence="ECO:0000269|PubMed:1394429"
FT /id="VAR_007093"
FT VARIANT 242
FT /note="T -> I (associated with susceptibility to
FT hypertension; dbSNP:rs765678426)"
FT /evidence="ECO:0000269|PubMed:7607642"
FT /id="VAR_007094"
FT VARIANT 244
FT /note="L -> R (associated with susceptibility to
FT hypertension; dbSNP:rs5041)"
FT /evidence="ECO:0000269|PubMed:7607642"
FT /id="VAR_007095"
FT VARIANT 268
FT /note="M -> I (in dbSNP:rs11568053)"
FT /id="VAR_029167"
FT VARIANT 268
FT /note="M -> T (associated with essential hypertension and
FT pre-eclampsia; dbSNP:rs699)"
FT /evidence="ECO:0000269|PubMed:1394429,
FT ECO:0000269|PubMed:8513325"
FT /id="VAR_007096"
FT VARIANT 281
FT /note="Y -> C (associated with susceptibility to
FT hypertension; alters the structure, glycosylation and
FT secretion of angiotensinogen; dbSNP:rs56073403)"
FT /evidence="ECO:0000269|PubMed:1394429,
FT ECO:0000269|PubMed:7607642, ECO:0000269|PubMed:8621667"
FT /id="VAR_007097"
FT VARIANT 335
FT /note="P -> S (in dbSNP:rs17856352)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035432"
FT VARIANT 375
FT /note="R -> Q (in RTD; dbSNP:rs74315283)"
FT /evidence="ECO:0000269|PubMed:16116425"
FT /id="VAR_035433"
FT VARIANT 392
FT /note="L -> M (in dbSNP:rs1805090)"
FT /id="VAR_014573"
FT CONFLICT 51
FT /note="C -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="N -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Q -> E (in Ref. 2; AAA51679)"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6OS0"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6I3I"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2WXW"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 88..110
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2WXW"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6I3F"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6I3F"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6I3F"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 303..315
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 320..340
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 387..391
FT /evidence="ECO:0007829|PDB:5M3Y"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2WXW"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 412..424
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:5M3Y"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:5M3Y"
FT STRAND 462..470
FT /evidence="ECO:0007829|PDB:5M3Y"
SQ SEQUENCE 485 AA; 53154 MW; 5026C2DFB2DD236E CRC64;
MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG
KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM
HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV
LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD
FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF
WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT
FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR
VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN
PLSTA
