P01019 (ANGT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiotensinogen

Alternative name(s):
Serpin A8

Cleaved into the following 3 chains:

1. Angiotensin-1
   Alternative name(s):
   Angiotensin I
   Short name=Ang I
2. Angiotensin-2
   Alternative name(s):
   Angiotensin II
   Short name=Ang II
3. Angiotensin-3
   Alternative name(s):
   Angiotensin III
   Short name=Ang III
   Des-Asp[1]-angiotensin II

Gene names

Name:	AGT
Synonyms:	SERPINA8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. In response to lowered blood pressure, the enzyme renin cleaves angiotensinogen to produce angiotensin-1 (angiotensin 1-10). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2 (angiotensin 1-8). Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3 (angiotensin 2-8), angiotensin-4 (angiotensin 3-8). Angiotensin 1-7 is cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2. Ref.11 Ref.12 Ref.16 Angiotensin-2 acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. Ref.11 Ref.12 Ref.16 Angiotensin-3 stimulates aldosterone release. Ref.11 Ref.12 Ref.16 Angiotensin 1-7 is a ligand for the G-protein coupled receptor MAS1 By similarity. Has vasodilator and antidiuretic effects By similarity. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets By similarity. Ref.11 Ref.12 Ref.16
Subunit structure	During pregnancy, exists as a disulfide-linked 2:2 heterotetramer with the proform of PRG2 and as a complex (probably a 2:2:2 heterohexamer) with pro-PRG2 and C3dg. Ref.8
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Post-translational modification	Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear leukocytes produces alanine. The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor.
Involvement in disease	Genetic variations in AGT are a cause of susceptibility to essential hypertension (EHT) [MIM:145500]. Essential hypertension is a condition in which blood pressure is consistently higher than normal with no identifiable cause. Defects in AGT are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Ref.26
Sequence similarities	Belongs to the serpin family.
Caution	It is uncertain whether Met-1 or Met-10 is the initiator.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Vasoactive Vasoconstrictor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	G-protein signaling, coupled to cGMP nucleotide second messenger Traceable author statement. Source: BHF-UCL activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger Non-traceable author statement. Source: BHF-UCL blood vessel remodeling Traceable author statement. Source: BHF-UCL cell-cell signaling Traceable author statement. Source: ProtInc cellular lipid metabolic process Traceable author statement. Source: Reactome kidney development Inferred from mutant phenotype Ref.26. Source: BHF-UCL low-density lipoprotein particle remodeling Non-traceable author statement. Source: BHF-UCL negative regulation of nerve growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL nitric oxide mediated signal transduction Traceable author statement. Source: BHF-UCL positive regulation of NAD(P)H oxidase activity Traceable author statement. Source: BHF-UCL positive regulation of NF-kappaB transcription factor activity Traceable author statement. Source: BHF-UCL positive regulation of activation of JAK2 kinase activity Inferred from mutant phenotype. Source: UniProtKB positive regulation of branching involved in ureteric bud morphogenesis Inferred from direct assay. Source: UniProtKB positive regulation of cardiac muscle hypertrophy Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cholesterol esterification Inferred from direct assay. Source: BHF-UCL positive regulation of cytokine production Traceable author statement. Source: BHF-UCL positive regulation of endothelial cell migration Inferred from direct assay. Source: BHF-UCL positive regulation of epidermal growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of inflammatory response Traceable author statement. Source: BHF-UCL positive regulation of macrophage derived foam cell differentiation Inferred by curator. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay. Source: BHF-UCL positive regulation of protein tyrosine kinase activity Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of renal output by angiotensin Non-traceable author statement. Source: BHF-UCL regulation of vasoconstriction Non-traceable author statement. Source: BHF-UCL renin-angiotensin regulation of aldosterone production Non-traceable author statement. Source: BHF-UCL response to muscle activity involved in regulation of muscle adaptation Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL soluble fraction Traceable author statement. Source: ProtInc
Molecular function	acetyltransferase activator activity Inferred from direct assay. Source: BHF-UCL growth factor activity Traceable author statement. Source: BHF-UCL hormone activity Inferred from sequence or structural similarity. Source: BHF-UCL serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome type 1 angiotensin receptor binding Inferred from physical interaction. Source: BHF-UCL type 2 angiotensin receptor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Ref.7 Ref.8 Ref.9

Chain

34 – 485

452

Angiotensinogen

PRO_0000032456

Peptide

34 – 43

10

Angiotensin-1 Ref.9

PRO_0000032457

Peptide

34 – 41

8

Angiotensin-2

PRO_0000032458

Peptide

35 – 41

7

Angiotensin-3

PRO_0000032459

Amino acid modifications

Modified residue

34

1

Beta-decarboxylated aspartate; in form angiotensin-A

Glycosylation

47

1

N-linked (GlcNAc...) Ref.10 Ref.15 Ref.18

Glycosylation

170

1

N-linked (GlcNAc...) Ref.10

Glycosylation

304

1

N-linked (GlcNAc...) Ref.10

Glycosylation

328

1

N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant

43

1

L → F Associated with susceptibility to pre-eclampsia; alters the reactions with renin and angiotensin-converting enzyme. Ref.24
Corresponds to variant rs41271499 [ dbSNP | Ensembl ].

VAR_022933

Natural variant

98

1

E → K.
Corresponds to variant rs11568032 [ dbSNP | Ensembl ].

VAR_029166

Natural variant

114

1

G → C.
Corresponds to variant rs2229389 [ dbSNP | Ensembl ].

VAR_051939

Natural variant

137

1

T → M.
Corresponds to variant rs34829218 [ dbSNP | Ensembl ].

VAR_035431

Natural variant

207

1

T → M Associated with hypertension. Ref.21
Corresponds to variant rs4762 [ dbSNP | Ensembl ].

VAR_007093

Natural variant

242

1

T → I Associated with susceptibility to hypertension. Ref.23

VAR_007094

Natural variant

244

1

L → R Associated with susceptibility to hypertension. Ref.23
Corresponds to variant rs5041 [ dbSNP | Ensembl ].

VAR_007095

Natural variant

268

1

M → I.
Corresponds to variant rs11568053 [ dbSNP | Ensembl ].

VAR_029167

Natural variant

268

1

M → T Associated with essential hypertension and pre-eclampsia. Ref.21 Ref.22
Corresponds to variant rs699 [ dbSNP | Ensembl ].

VAR_007096

Natural variant

281

1

Y → C Associated with susceptibility to hypertension; alters the structure, glycosylation and secretion of angiotensinogen. Ref.21 Ref.23 Ref.25
Corresponds to variant rs56073403 [ dbSNP | Ensembl ].

VAR_007097

Natural variant

335

1

P → S. Ref.4
Corresponds to variant rs17856352 [ dbSNP | Ensembl ].

VAR_035432

Natural variant

375

1

R → Q in RTD. Ref.26

VAR_035433

Natural variant

392

1

L → M.
Corresponds to variant rs1805090 [ dbSNP | Ensembl ].

VAR_014573

Experimental info

Sequence conflict

51

1

C → S AA sequence Ref.7

Sequence conflict

58

1

N → D AA sequence Ref.7

Sequence conflict

333

1

Q → E in AAA51679. Ref.2

Secondary structure

1

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485

Helix Strand Turn

Details...

Turn

42 – 44

3

Helix

48 – 57

10

Beta strand

66 – 68

3

Helix

81 – 93

13

Helix

97 – 105

9

Helix

109 – 112

4

Helix

136 – 139

4

Helix

143 – 147

5

Helix

154 – 161

8

Turn

171 – 173

3

Helix

177 – 187

11

Beta strand

204 – 209

6

Helix

221 – 224

4

Turn

228 – 230

3

Helix

244 – 258

15

Beta strand

280 – 285

6

Beta strand

302 – 305

4

Beta strand

319 – 322

4

Turn

325 – 328

4

Beta strand

329 – 333

5

Turn

337 – 339

3

Beta strand

340 – 349

10

Helix

353 – 356

4

Helix

365 – 368

4

Beta strand

377 – 381

5

Helix

392 – 395

4

Helix

402 – 406

5

Beta strand

407 – 409

3

Beta strand

425 – 431

7

Beta strand

452 – 455

4

Beta strand

460 – 466

7

Turn

467 – 470

4

Sequences

	Sequence		Length	Mass (Da)
	P01019 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 5026C2DFB2DD236E	FASTA	485	53,154
	10 20 30 40 50 60 MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG 70 80 90 100 110 120 KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM 130 140 150 160 170 180 HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV 190 200 210 220 230 240 LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD 250 260 270 280 290 300 FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF 310 320 330 340 350 360 WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT 370 380 390 400 410 420 FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR 430 440 450 460 470 480 VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN PLSTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence." Kageyama R., Ohkubo H., Nakanishi S. Biochemistry 23:3603-3609(1984) [PubMed: 6089875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of human angiotensinogen gene." Gaillard I., Clauser E., Corvol P. DNA 8:87-99(1989) [PubMed: 2924688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter." Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., Murakami K. J. Biol. Chem. 265:7576-7582(1990) [PubMed: 1692023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-335. Tissue: Brain.
[5]	"Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart." Kunapuli S.P., Kumar A. Circ. Res. 60:786-790(1987) [PubMed: 2885106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-338.
[6]	"Tissue specific hormonal regulation of the rat angiotensinogen gene expression." Kunapuli S.P., Benedict C.R., Kumar A. Arch. Biochem. Biophys. 254:642-646(1987) [PubMed: 3579322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-184.
[7]	"The amino terminal amino acid sequence of human angiotensinogen." Tewksbury D.A., Dart R.A., Travis J. Biochem. Biophys. Res. Commun. 99:1311-1315(1981) [PubMed: 7259779] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-58.
[8]	"Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma." Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L. J. Biol. Chem. 270:13645-13651(1995) [PubMed: 7539791] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-45, SUBUNIT. Tissue: Serum.
[9]	"Enzymatic degradation and electrophoresis of human angiotensin I." Arakawa K., Minohara A., Yamada J., Nakamura M. Biochim. Biophys. Acta 168:106-112(1968) [PubMed: 4300938] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-43.
[10]	"Processing of rat and human angiotensinogen precursors by microsomal membranes." Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P. Mol. Cell. Endocrinol. 43:31-40(1985) [PubMed: 3934016] [Abstract] Cited for: GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328.
[11]	"Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system." Goodfriend T.L., Peach M.J. Circ. Res. 36:38-48(1975) [PubMed: 1132082] [Abstract] Cited for: FUNCTION OF ANGIOTENSIN-3.
[12]	"The renin-angiotensin-aldosterone system: a specific target for hypertension management." Weir M.R., Dzau V.J. Am. J. Hypertens. 12:205S-213S(1999) [PubMed: 10619573] [Abstract] Cited for: FUNCTION OF ANGIOTENSIN-2.
[13]	"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase." Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P. J. Biol. Chem. 277:14838-14843(2002) [PubMed: 11815627] [Abstract] Cited for: CLEAVAGE OF ANGIOTENSIN-1 AND ANGIOTENSIN-2 BY ACE2.
[14]	"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism." Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M. Biochem. J. 383:45-51(2004) [PubMed: 15283675] [Abstract] Cited for: ANGIOTENSIN PEPTIDES METABOLISM.
[15]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, MASS SPECTROMETRY. Tissue: Plasma.
[16]	"Mass-spectrometric identification of a novel angiotensin peptide in human plasma." Jankowski V., Vanholder R., van der Giet M., Tolle M., Karadogan S., Gobom J., Furkert J., Oksche A., Krause E., Tran T.N., Tepel M., Schuchardt M., Schluter H., Wiedon A., Beyermann M., Bader M., Todiras M., Zidek W., Jankowski J. Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007) [PubMed: 17138938] [Abstract] Cited for: DECARBOXYLATION AT ASP-34, FUNCTION, MASS SPECTROMETRY.
[17]	"Renin-angiotensin system revisited." Fyhrquist F., Saijonmaa O. J. Intern. Med. 264:224-236(2008) [PubMed: 18793332] [Abstract] Cited for: REVIEW ON THE RENIN-ANGIOTENSIN SYSTEM.
[18]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, MASS SPECTROMETRY. Tissue: Liver.
[19]	"The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment." Carpenter K.A., Wilkes B.C., Schiller P.W. Eur. J. Biochem. 251:448-453(1998) [PubMed: 9492317] [Abstract] Cited for: STRUCTURE BY NMR OF ANGIOTENSIN-2.
[20]	"Comparison of the solution structures of angiotensin I & II. Implication for structure-function relationship." Spyroulias G.A., Nikolakopoulou P., Tzakos A., Gerothanassis I.P., Magafa V., Manessi-Zoupa E., Cordopatis P. Eur. J. Biochem. 270:2163-2173(2003) [PubMed: 12752436] [Abstract] Cited for: STRUCTURE BY NMR OF 34-43, STRUCTURE BY NMR OF 34-41.
[21]	"Molecular basis of human hypertension: role of angiotensinogen." Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., Lalouel J.-M., Corvol P. Cell 71:169-180(1992) [PubMed: 1394429] [Abstract] Cited for: VARIANTS MET-207; THR-268 AND CYS-281.
[22]	"A molecular variant of angiotensinogen associated with preeclampsia." Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M. Nat. Genet. 4:59-61(1993) [PubMed: 8513325] [Abstract] Cited for: VARIANT THR-268.
[23]	"Detection and characterization of new mutations in the human angiotensinogen gene (AGT)." Hixson J.E., Powers P.K. Hum. Genet. 96:110-112(1995) [PubMed: 7607642] [Abstract] Cited for: VARIANTS ILE-242; ARG-244 AND CYS-281.
[24]	"A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system." Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P., Bohlender J., Lifton R.P., Corvol P., Ward K., Lalouel J.-M. J. Biol. Chem. 270:11430-11436(1995) [PubMed: 7744780] [Abstract] Cited for: VARIANT PHE-43.
[25]	"The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein." Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X. J. Biol. Chem. 271:9838-9844(1996) [PubMed: 8621667] [Abstract] Cited for: CHARACTERIZATION OF VARIANT CYS-281.
[26]	"Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis." Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C. Nat. Genet. 37:964-968(2005) [PubMed: 16116425] [Abstract] Cited for: VARIANT RTD GLN-375.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Angiotensin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02215 mRNA. Translation: AAA51731.1.
M24689 , M24686, M24687, M24688 Genomic DNA. Translation: AAA51679.1.
X15324 , X15325, X15326, X15327 Genomic DNA. Translation: CAA33385.1.
BC011519 mRNA. Translation: AAH11519.1.
M69110 mRNA. Translation: AAA52282.1.
S78529 Genomic DNA. Translation: AAD14287.1.
S78530 Genomic DNA. Translation: AAD14288.1.

IPI

IPI00032220.

PIR

ANHU. A35203.

RefSeq

NP_000020.1. NM_000029.3.

UniGene

Hs.19383.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N9U	NMR	-	A	34-43	[»]
1N9V	NMR	-	A	34-41	[»]
2JP8	NMR	-	P	34-40	[»]
2WXW	X-ray	3.30	A	34-485	[»]
2X0B	X-ray	4.33	B/D/F/H	34-485	[»]

ProteinModelPortal

P01019.

SMR

P01019. Positions 34-482.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-309N.

IntAct

P01019. 4 interactions.

MINT

MINT-1472115.

STRING

P01019.

Protein family/group databases

MEROPS

I04.953.

PTM databases

PhosphoSite

P01019.

Polymorphism databases

DMDM

113880.

2D gel databases

SWISS-2DPAGE

P01019.

Proteomic databases

PeptideAtlas

P01019.

PRIDE

P01019.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366667; ENSP00000355627; ENSG00000135744.

GeneID

183.

KEGG

hsa:183.

UCSC

uc001hty.2. human.

Organism-specific databases

CTD

183.

GeneCards

GC01M230838.

H-InvDB

HIX0001686.

HGNC

HGNC:333. AGT.

HPA

HPA001557.

MIM

106150. gene.
145500. phenotype.
267430. phenotype.

neXtProt

NX_P01019.

Orphanet

243761. Essential hypertension.
97369. Renal tubular dysgenesis of genetic origin.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11287.

HOVERGEN

HBG004233.

InParanoid

P01019.

OMA

TYVHFQG.

OrthoDB

EOG44TP89.

PhylomeDB

P01019.

Enzyme and pathway databases

Pathway_Interaction_DB

prlsignalingeventspathway. Signaling events mediated by PRL.

Reactome

REACT_111102. Signal Transduction.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P01019.

Bgee

P01019.

CleanEx

HS_AGT.

Genevestigator

P01019.

GermOnline

ENSG00000135744. Homo sapiens.

Family and domain databases

InterPro

IPR000227. Angiotensngn.
IPR000215. Protease_inhib_I4_serpin.
IPR023795. Protease_inhib_I4_serpin_CS.
IPR023796. Sepin_dom.
[Graphical view]

KO

K09821.

PANTHER

PTHR11461. Prot_inh_serpin. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

PRINTS

PR00654. ANGIOTENSNGN.

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01258. Aliskiren.
DB01076. Atorvastatin.
DB01340. Cilazapril.
DB01029. Irbesartan.
DB00722. Lisinopril.
DB01092. Ouabain.
DB00641. Simvastatin.

NextBio

748.

PMAP-CutDB

P01019.

SOURCE

Search...

Entry information

Entry name

ANGT_HUMAN

Accession

Primary (citable) accession number: P01019
Secondary accession number(s): Q16358, Q16359, Q96F91

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.