ID ANGT_HUMAN Reviewed; 476 AA. AC P01019; Q16358; Q16359; Q96F91; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 4. DT 02-SEP-2026, entry version 262. DE RecName: Full=Angiotensinogen {ECO:0000305}; 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 {ECO:0000312|HGNC:HGNC:333}; 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-326. 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 1-329. 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 23-175. 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-233; ARG-235 RP AND CYS-272. 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 25-49. 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 25-36, 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 25-34. 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-38; ASN-161; ASN-295 AND ASN-319. 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-38. 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-25, 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-38. 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] {ECO:0007744|PDB:1N9U, ECO:0007744|PDB:1N9V} RP STRUCTURE BY NMR OF 25-34, AND STRUCTURE BY NMR OF 25-32. 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] {ECO:0007744|PDB:2WXW, ECO:0007744|PDB:2X0B} RP X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 25-476 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-198; THR-259 AND CYS-272. 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-259. 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-34. 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-272. 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-366. 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; 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-25 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:10969042, PubMed:4322742). 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 -!- 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"; 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; 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; CCDS1585.2; -. DR PIR; A35203; ANHU. DR RefSeq; NP_001369746.2; NM_001382817.3. DR RefSeq; NP_001371408.1; NM_001384479.1. DR PDB; 1N9U; NMR; -; A=25-34. DR PDB; 1N9V; NMR; -; A=25-32. DR PDB; 2JP8; NMR; -; P=25-31. DR PDB; 2WXW; X-ray; 3.30 A; A=25-476. DR PDB; 2X0B; X-ray; 4.33 A; B/D/F/H=25-476. DR PDB; 3CK0; X-ray; 3.00 A; P=25-32. DR PDB; 3WOO; X-ray; 1.80 A; C/D=27-32. DR PDB; 3WOR; X-ray; 2.10 A; C/D=25-32. DR PDB; 4AA1; X-ray; 1.99 A; P=25-32. DR PDB; 4APH; X-ray; 1.99 A; P=25-32. DR PDB; 4FYS; X-ray; 2.01 A; C=27-32. DR PDB; 5E2Q; X-ray; 2.40 A; B=25-32. DR PDB; 5M3X; X-ray; 2.63 A; A/B=35-476. DR PDB; 5M3Y; X-ray; 2.30 A; A=25-476. DR PDB; 5NJ9; X-ray; 1.25 A; E/F=25-28. DR PDB; 5XJM; X-ray; 3.20 A; B=26-31. DR PDB; 6I3F; X-ray; 2.55 A; A=25-476. DR PDB; 6I3I; X-ray; 2.97 A; A=25-476. DR PDB; 6JOD; X-ray; 3.20 A; B=25-32. DR PDB; 6OS0; X-ray; 2.90 A; B=25-32. DR PDB; 7C6A; X-ray; 3.40 A; B=26-31. DR AlphaFoldDB; P01019; -. DR MDposit; P01019; -. DR MDRepo; P01019; -. DR SMR; P01019; -. DR BioGRID; 106690; 40. DR CORUM; P01019; -. DR DIP; DIP-309N; -. DR FunCoup; P01019; 902. DR IntAct; P01019; 32. DR MINT; P01019; -. DR NDEx; IQUERY-CP-AGT; 24 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000355627; -. DR BindingDB; P01019; -. DR ChEMBL; CHEMBL3596085; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR MEROPS; I04.953; -. DR CarbonylDB; P01019; -. DR GlyConnect; P01019; 65 N-Linked glycans (3 sites). DR GlyCosmos; P01019; 5 sites, 21 glycans. DR GlyGen; P01019; 4 sites, 1 N-linked glycan (1 site). DR iPTMnet; P01019; -. DR PhosphoSitePlus; P01019; -. DR SwissPalm; P01019; -. DR BioMuta; AGT; -. DR DMDM; 113880; -. DR jPOST; P01019; -. DR MassIVE; P01019; -. DR PaxDb; 9606-ENSP00000355627; -. DR PeptideAtlas; P01019; -. DR ProteomicsDB; 51306; -. DR ABCD; P01019; 6 sequenced antibodies. DR Antibodypedia; 866; 1052 antibodies from 46 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 KEGG; hsa:183; -. DR MANE-Select; ENST00000366667.6; ENSP00000355627.5; NM_001384479.1; NP_001371408.1. DR UCSC; uc001hty.6; human. DR AGR; HGNC:333; -. DR ClinPGx; PA42; -. 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 OpenTargets; ENSG00000135744; -. DR Orphanet; 97369; Renal tubular dysgenesis of genetic origin. DR VEuPathDB; HostDB:ENSG00000135744; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00890000139531; -. DR HOGENOM; CLU_045267_1_0_1; -. DR InParanoid; P01019; -. DR OrthoDB; 7817921at2759; -. DR PAN-GO; P01019; 4 GO annotations based on evolutionary models. DR PhylomeDB; P01019; -. 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 Agora; ENSG00000135744; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 183; 18 hits in 1150 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 cell types or tissues. DR ExpressionAtlas; P01019; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL. DR GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL. DR GO; GO:0005179; F:hormone activity; IDA:UniProt. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central. 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:0038166; P:angiotensin-activated signaling pathway; IDA:BHF-UCL. DR GO; GO:0001974; P:blood vessel remodeling; TAS:BHF-UCL. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. 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; IDA:UniProt. 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:0038060; P:nitric oxide-cGMP-mediated signaling; TAS:BHF-UCL. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; NAS:BHF-UCL. DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IDA:UniProtKB. DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:BHF-UCL. DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IDA:BHF-UCL. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. 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:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB. DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IDA:BHF-UCL. 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; IDA:BHF-UCL. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:BHF-UCL. 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: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: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: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:1990776; P:response to angiotensin; IDA:BHF-UCL. DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:BHF-UCL. DR CDD; cd02054; serpinA8_AGT; 1. DR DisProt; DP03155; -. DR FunFam; 2.30.39.10:FF:000018; Angiotensinogen; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF13; ANGIOTENSINOGEN; 1. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR Pfam; PF00079; Serpin; 1. DR PRINTS; PR00654; ANGIOTENSNGN. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. 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; 5NJ9; -. DR PDBsum; 5XJM; -. DR PDBsum; 6I3F; -. DR PDBsum; 6I3I; -. DR PDBsum; 6JOD; -. DR PDBsum; 6OS0; -. DR PDBsum; 7C6A; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; KW Glycoprotein; Proteomics identification; Reference proteome; Secreted; KW Signal; Vasoactive; Vasoconstrictor. FT SIGNAL 1..24 FT /evidence="ECO:0000269|PubMed:4300938, FT ECO:0000269|PubMed:7259779, ECO:0000269|PubMed:7539791" FT CHAIN 25..476 FT /note="Angiotensinogen" FT /id="PRO_0000032456" FT PEPTIDE 25..34 FT /note="Angiotensin-1" FT /evidence="ECO:0000269|PubMed:4300938" FT /id="PRO_0000032457" FT PEPTIDE 25..33 FT /note="Angiotensin 1-9" FT /evidence="ECO:0000305|PubMed:10969042" FT /id="PRO_0000420659" FT PEPTIDE 25..32 FT /note="Angiotensin-2" FT /evidence="ECO:0000305|PubMed:11815627, FT ECO:0000305|PubMed:9492317" FT /id="PRO_0000032458" FT PEPTIDE 25..31 FT /note="Angiotensin 1-7" FT /evidence="ECO:0000305|PubMed:15283675" FT /id="PRO_0000420660" FT PEPTIDE 25..29 FT /note="Angiotensin 1-5" FT /evidence="ECO:0000305|PubMed:10969042, FT ECO:0000305|PubMed:11815627" FT /id="PRO_0000420661" FT PEPTIDE 25..28 FT /note="Angiotensin 1-4" FT /evidence="ECO:0000305|PubMed:10969042, FT ECO:0000305|PubMed:11815627" FT /id="PRO_0000420662" FT PEPTIDE 26..32 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 27..32 FT /note="Angiotensin-4" FT /evidence="ECO:0000305|PubMed:10969042, FT ECO:0000305|PubMed:11815627" FT /id="PRO_0000420663" FT MOD_RES 25 FT /note="Beta-decarboxylated aspartate; in form angiotensin- FT A" FT /evidence="ECO:0000269|PubMed:17138938" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3934016" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:3934016" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:3934016" FT CARBOHYD 319 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:3934016" FT DISULFID 42..162 FT /evidence="ECO:0000269|PubMed:20927107" FT VARIANT 34 FT /note="L -> F (risk factor for pre-eclampsia; alters the FT reactions with renin and angiotensin-converting enzyme; FT dbSNP:rs41271499)" FT /evidence="ECO:0000269|PubMed:7744780" FT /id="VAR_022933" FT VARIANT 89 FT /note="E -> K (in dbSNP:rs11568032)" FT /id="VAR_029166" FT VARIANT 105 FT /note="G -> C (in dbSNP:rs2229389)" FT /id="VAR_051939" FT VARIANT 128 FT /note="T -> M (in dbSNP:rs34829218)" FT /id="VAR_035431" FT VARIANT 198 FT /note="T -> M (risk factor for hypertension; dbSNP:rs4762)" FT /evidence="ECO:0000269|PubMed:1394429" FT /id="VAR_007093" FT VARIANT 233 FT /note="T -> I (risk factor for hypertension; FT dbSNP:rs765678426)" FT /evidence="ECO:0000269|PubMed:7607642" FT /id="VAR_007094" FT VARIANT 235 FT /note="L -> R (risk factor for hypertension; dbSNP:rs5041)" FT /evidence="ECO:0000269|PubMed:7607642" FT /id="VAR_007095" FT VARIANT 259 FT /note="M -> I (in dbSNP:rs11568053)" FT /id="VAR_029167" FT VARIANT 259 FT /note="M -> T (risk factor for 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 272 FT /note="Y -> C (risk factor for hypertension; alters the FT structure, glycosylation and secretion of angiotensinogen; FT dbSNP:rs56073403)" FT /evidence="ECO:0000269|PubMed:1394429, FT ECO:0000269|PubMed:7607642, ECO:0000269|PubMed:8621667" FT /id="VAR_007097" FT VARIANT 326 FT /note="P -> S (in dbSNP:rs17856352)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035432" FT VARIANT 366 FT /note="R -> Q (in RTD; dbSNP:rs74315283)" FT /evidence="ECO:0000269|PubMed:16116425" FT /id="VAR_035433" FT VARIANT 383 FT /note="L -> M (in dbSNP:rs1805090)" FT /id="VAR_014573" FT CONFLICT 42 FT /note="C -> S (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 49 FT /note="N -> D (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 324 FT /note="Q -> E (in Ref. 2; AAA51679)" FT /evidence="ECO:0000305" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:4APH" 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 59..61 FT /evidence="ECO:0007829|PDB:5M3Y" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:5M3Y" 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 476 AA; 52070 MW; EF44870358ABAD90 CRC64; MAPAGVSLRA TILCLLAWAG LAAGDRVYIH PFHLVIHNES TCEQLAKANA GKPKDPTFIP APIQAKTSPV DEKALQDQLV LVAAKLDTED KLRAAMVGML ANFLGFRIYG MHSELWGVVH GATVLSPTAV FGTLASLYLG ALDHTADRLQ AILGVPWKDK NCTSRLDAHK VLSALQAVQG LLVAQGRADS QAQLLLSTVV GVFTAPGLHL KQPFVQGLAL YTPVVLPRSL DFTELDVAAE KIDRFMQAVT GWKTGCSLMG ASVDSTLAFN TYVHFQGKMK GFSLLAEPQE FWVDNSTSVS VPMLSGMGTF QHWSDIQDNF SVTQVPFTES ACLLLIQPHY ASDLDKVEGL TFQQNSLNWM KKLSPRTIHL TMPQLVLQGS YDLQDLLAQA ELPAILHTEL NLQKLSNDRI RVGEVLNSIF FELEADEREP TESTQQLNKP EVLEVTLNRP FLFAVYDQSA TALHFLGRVA NPLSTA //