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Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4]

 ANGT_HUMAN              Reviewed;         485 AA.
P01019; Q16358; Q16359; Q96F91;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 209.
RecName: Full=Angiotensinogen;
AltName: Full=Serpin A8;
Contains:
RecName: Full=Angiotensin-1;
AltName: Full=Angiotensin 1-10;
AltName: Full=Angiotensin I;
Short=Ang I;
Contains:
RecName: Full=Angiotensin-2;
AltName: Full=Angiotensin 1-8;
AltName: Full=Angiotensin II;
Short=Ang II;
Contains:
RecName: Full=Angiotensin-3;
AltName: Full=Angiotensin 2-8;
AltName: Full=Angiotensin III;
Short=Ang III;
AltName: Full=Des-Asp[1]-angiotensin II;
Contains:
RecName: Full=Angiotensin-4;
AltName: Full=Angiotensin 3-8;
AltName: Full=Angiotensin IV;
Short=Ang IV;
Contains:
RecName: Full=Angiotensin 1-9;
Contains:
RecName: Full=Angiotensin 1-7;
Contains:
RecName: Full=Angiotensin 1-5;
Contains:
RecName: Full=Angiotensin 1-4;
Flags: Precursor;
Name=AGT; Synonyms=SERPINA8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6089875; DOI=10.1021/bi00311a006;
Kageyama R., Ohkubo H., Nakanishi S.;
"Primary structure of human preangiotensinogen deduced from the cloned
cDNA sequence.";
Biochemistry 23:3603-3609(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2924688; DOI=10.1089/dna.1.1989.8.87;
Gaillard I., Clauser E., Corvol P.;
"Structure of human angiotensinogen gene.";
DNA 8:87-99(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1692023;
Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S.,
Murakami K.;
"Structure and expression of the human angiotensinogen gene.
Identification of a unique and highly active promoter.";
J. Biol. Chem. 265:7576-7582(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-335.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-338.
PubMed=2885106; DOI=10.1161/01.RES.60.5.786;
Kunapuli S.P., Kumar A.;
"Molecular cloning of human angiotensinogen cDNA and evidence for the
presence of its mRNA in rat heart.";
Circ. Res. 60:786-790(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-184.
PubMed=3579322; DOI=10.1016/0003-9861(87)90148-2;
Kunapuli S.P., Benedict C.R., Kumar A.;
"Tissue specific hormonal regulation of the rat angiotensinogen gene
expression.";
Arch. Biochem. Biophys. 254:642-646(1987).
[7]
PROTEIN SEQUENCE OF 34-58.
PubMed=7259779; DOI=10.1016/0006-291X(81)90762-2;
Tewksbury D.A., Dart R.A., Travis J.;
"The amino terminal amino acid sequence of human angiotensinogen.";
Biochem. Biophys. Res. Commun. 99:1311-1315(1981).
[8]
PROTEIN SEQUENCE OF 34-45, AND SUBUNIT.
TISSUE=Serum;
PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I.,
Stigbrand T., Gleich G.J., Sottrup-Jensen L.;
"Identification of angiotensinogen and complement C3dg as novel
proteins binding the proform of eosinophil major basic protein in
human pregnancy serum and plasma.";
J. Biol. Chem. 270:13645-13651(1995).
[9]
PROTEIN SEQUENCE OF 34-43.
PubMed=4300938;
Arakawa K., Minohara A., Yamada J., Nakamura M.;
"Enzymatic degradation and electrophoresis of human angiotensin I.";
Biochim. Biophys. Acta 168:106-112(1968).
[10]
GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328.
PubMed=3934016; DOI=10.1016/0303-7207(85)90039-5;
Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.;
"Processing of rat and human angiotensinogen precursors by microsomal
membranes.";
Mol. Cell. Endocrinol. 43:31-40(1985).
[11]
FUNCTION OF ANGIOTENSIN-3.
PubMed=1132082; DOI=10.1161/01.RES.36.6.38;
Goodfriend T.L., Peach M.J.;
"Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and
speculation for its role as an important agonist in the renin
- angiotensin system.";
Circ. Res. 36:38-48(1975).
[12]
FUNCTION OF ANGIOTENSIN-2.
PubMed=10619573; DOI=10.1016/S0895-7061(99)00103-X;
Weir M.R., Dzau V.J.;
"The renin-angiotensin-aldosterone system: a specific target for
hypertension management.";
Am. J. Hypertens. 12:205S-213S(1999).
[13]
CLEAVAGE BY ACE AND ACE2.
PubMed=10969042; DOI=10.1161/01.RES.87.5.e1;
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M.,
Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R.,
Breitbart R.E., Acton S.;
"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2)
converts angiotensin I to angiotensin 1-9.";
Circ. Res. 87:E1-E9(2000).
[14]
CLEAVAGE OF ANGIOTENSIN-1 AND ANGIOTENSIN-2 BY ACE2.
PubMed=11815627; DOI=10.1074/jbc.M200581200;
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.;
"Hydrolysis of biological peptides by human angiotensin-converting
enzyme-related carboxypeptidase.";
J. Biol. Chem. 277:14838-14843(2002).
[15]
ANGIOTENSIN PEPTIDES METABOLISM.
PubMed=15283675; DOI=10.1042/BJ20040634;
Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.;
"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2
and neprilysin in angiotensin peptide metabolism.";
Biochem. J. 383:45-51(2004).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
DECARBOXYLATION AT ASP-34, FUNCTION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17138938; DOI=10.1161/01.ATV.0000253889.09765.5f;
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.;
"Mass-spectrometric identification of a novel angiotensin peptide in
human plasma.";
Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007).
[18]
REVIEW ON THE RENIN-ANGIOTENSIN SYSTEM.
PubMed=18793332; DOI=10.1111/j.1365-2796.2008.01981.x;
Fyhrquist F., Saijonmaa O.;
"Renin-angiotensin system revisited.";
J. Intern. Med. 264:224-236(2008).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
STRUCTURE BY NMR OF ANGIOTENSIN-2.
PubMed=9492317; DOI=10.1046/j.1432-1327.1998.2510448.x;
Carpenter K.A., Wilkes B.C., Schiller P.W.;
"The octapeptide angiotensin II adopts a well-defined structure in a
phospholipid environment.";
Eur. J. Biochem. 251:448-453(1998).
[23]
STRUCTURE BY NMR OF 34-43, AND STRUCTURE BY NMR OF 34-41.
PubMed=12752436; DOI=10.1046/j.1432-1033.2003.03573.x;
Spyroulias G.A., Nikolakopoulou P., Tzakos A., Gerothanassis I.P.,
Magafa V., Manessi-Zoupa E., Cordopatis P.;
"Comparison of the solution structures of angiotensin I & II.
Implication for structure-function relationship.";
Eur. J. Biochem. 270:2163-2173(2003).
[24]
X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 34-485 IN COMPLEX WITH
RENIN, AND DISULFIDE BOND.
PubMed=20927107; DOI=10.1038/nature09505;
Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L.,
Stein P.E., Broughton Pipkin F., Read R.J.;
"A redox switch in angiotensinogen modulates angiotensin release.";
Nature 468:108-111(2010).
[25]
VARIANTS MET-207; THR-268 AND CYS-281.
PubMed=1394429; DOI=10.1016/0092-8674(92)90275-H;
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.;
"Molecular basis of human hypertension: role of angiotensinogen.";
Cell 71:169-180(1992).
[26]
VARIANT THR-268.
PubMed=8513325; DOI=10.1038/ng0593-59;
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.;
"A molecular variant of angiotensinogen associated with
preeclampsia.";
Nat. Genet. 4:59-61(1993).
[27]
VARIANTS ILE-242; ARG-244 AND CYS-281.
PubMed=7607642; DOI=10.1007/BF00214197;
Hixson J.E., Powers P.K.;
"Detection and characterization of new mutations in the human
angiotensinogen gene (AGT).";
Hum. Genet. 96:110-112(1995).
[28]
VARIANT PHE-43.
PubMed=7744780; DOI=10.1074/jbc.270.19.11430;
Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P.,
Bohlender J., Lifton R.P., Corvol P., Ward K., Lalouel J.-M.;
"A mutation of angiotensinogen in a patient with preeclampsia leads to
altered kinetics of the renin-angiotensin system.";
J. Biol. Chem. 270:11430-11436(1995).
[29]
CHARACTERIZATION OF VARIANT CYS-281.
PubMed=8621667; DOI=10.1074/jbc.271.16.9838;
Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T.,
Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.;
"The natural mutation Y248C of human angiotensinogen leads to abnormal
glycosylation and altered immunological recognition of the protein.";
J. Biol. Chem. 271:9838-9844(1996).
[30]
VARIANT RTD GLN-375.
PubMed=16116425; DOI=10.1038/ng1623;
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.;
"Mutations in genes in the renin-angiotensin system are associated
with autosomal recessive renal tubular dysgenesis.";
Nat. Genet. 37:964-968(2005).
-!- FUNCTION: Essential component of the renin-angiotensin system
(RAS), a potent regulator of blood pressure, body fluid and
electrolyte homeostasis.
-!- FUNCTION: 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.
-!- FUNCTION: Angiotensin-3: stimulates aldosterone release.
-!- FUNCTION: Angiotensin 1-7: is a ligand for the G-protein coupled
receptor MAS1. Has vasodilator and antidiuretic effects. Has an
antithrombotic effect that involves MAS1-mediated release of
nitric oxide from platelets. {ECO:0000250,
ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1132082,
ECO:0000269|PubMed:17138938}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:20927107, ECO:0000269|PubMed:7539791}.
-!- INTERACTION:
P30556:AGTR1; NbExp=2; IntAct=EBI-6622938, EBI-6623016;
P25095:Agtr1 (xeno); NbExp=10; IntAct=EBI-751728, EBI-764979;
P50052:AGTR2; NbExp=2; IntAct=EBI-2927577, EBI-1748067;
Q10714:Ance (xeno); NbExp=2; IntAct=EBI-751728, EBI-115736;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- PTM: 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.
{ECO:0000269|PubMed:17138938}.
-!- PTM: In response to low blood pressure, the enzyme renin/REN
cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is
a substrate of ACE (angiotensin converting enzyme) that removes a
dipeptide to yield the physiologically active peptide angiotensin-
2. Angiotensin-1 and angiotensin-2 can be further processed to
generate angiotensin-3, angiotensin-4. Angiotensin 1-9 is cleaved
from angiotensin-1 by ACE2 and can be further processed by ACE to
produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4.
Angiotensin 1-7 has also been proposed to be cleaved from
angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin).
{ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627}.
-!- PTM: The disulfide bond is labile. Angiotensinogen is present in
the circulation in a near 40:60 ratio with the oxidized disulfide-
bonded form, which preferentially interacts with receptor-bound
renin.
-!- DISEASE: Essential hypertension (EHT) [MIM:145500]: A condition in
which blood pressure is consistently higher than normal with no
identifiable cause. {ECO:0000269|PubMed:1394429,
ECO:0000269|PubMed:8513325}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: 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).
{ECO:0000269|PubMed:16116425}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=AGT";
-!- WEB RESOURCE: Name=Wikipedia; Note=Angiotensin entry;
URL="https://en.wikipedia.org/wiki/Angiotensin";
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EMBL; K02215; AAA51731.1; -; mRNA.
EMBL; M24689; AAA51679.1; -; Genomic_DNA.
EMBL; M24686; AAA51679.1; JOINED; Genomic_DNA.
EMBL; M24687; AAA51679.1; JOINED; Genomic_DNA.
EMBL; M24688; AAA51679.1; JOINED; Genomic_DNA.
EMBL; X15324; CAA33385.1; -; Genomic_DNA.
EMBL; X15325; CAA33385.1; JOINED; Genomic_DNA.
EMBL; X15326; CAA33385.1; JOINED; Genomic_DNA.
EMBL; X15327; CAA33385.1; JOINED; Genomic_DNA.
EMBL; BC011519; AAH11519.1; -; mRNA.
EMBL; M69110; AAA52282.1; -; mRNA.
EMBL; S78529; AAD14287.1; -; Genomic_DNA.
EMBL; S78530; AAD14288.1; -; Genomic_DNA.
CCDS; CCDS1585.1; -.
PIR; A35203; ANHU.
RefSeq; NP_000020.1; NM_000029.3.
UniGene; Hs.19383; -.
PDB; 1N9U; NMR; -; A=34-43.
PDB; 1N9V; NMR; -; A=34-41.
PDB; 2JP8; NMR; -; P=34-40.
PDB; 2WXW; X-ray; 3.30 A; A=34-485.
PDB; 2X0B; X-ray; 4.33 A; B/D/F/H=34-485.
PDB; 3CK0; X-ray; 3.00 A; P=34-41.
PDB; 3WOO; X-ray; 1.80 A; C/D=36-41.
PDB; 3WOR; X-ray; 2.10 A; C/D=34-41.
PDB; 4AA1; X-ray; 1.99 A; P=34-41.
PDB; 4APH; X-ray; 1.99 A; P=34-41.
PDB; 4FYS; X-ray; 2.01 A; C=36-41.
PDB; 5E2Q; X-ray; 2.40 A; B=34-41.
PDBsum; 1N9U; -.
PDBsum; 1N9V; -.
PDBsum; 2JP8; -.
PDBsum; 2WXW; -.
PDBsum; 2X0B; -.
PDBsum; 3CK0; -.
PDBsum; 3WOO; -.
PDBsum; 3WOR; -.
PDBsum; 4AA1; -.
PDBsum; 4APH; -.
PDBsum; 4FYS; -.
PDBsum; 5E2Q; -.
ProteinModelPortal; P01019; -.
SMR; P01019; -.
BioGrid; 106690; 15.
CORUM; P01019; -.
DIP; DIP-309N; -.
IntAct; P01019; 9.
MINT; MINT-1472115; -.
STRING; 9606.ENSP00000355627; -.
ChEMBL; CHEMBL3596085; -.
DrugBank; DB05206; PS433540.
MEROPS; I04.953; -.
iPTMnet; P01019; -.
PhosphoSitePlus; P01019; -.
BioMuta; AGT; -.
DMDM; 113880; -.
SWISS-2DPAGE; P01019; -.
EPD; P01019; -.
MaxQB; P01019; -.
PaxDb; P01019; -.
PeptideAtlas; P01019; -.
PRIDE; P01019; -.
DNASU; 183; -.
Ensembl; ENST00000366667; ENSP00000355627; ENSG00000135744.
GeneID; 183; -.
KEGG; hsa:183; -.
UCSC; uc001hty.6; human.
CTD; 183; -.
DisGeNET; 183; -.
EuPathDB; HostDB:ENSG00000135744.7; -.
GeneCards; AGT; -.
HGNC; HGNC:333; AGT.
HPA; CAB025798; -.
HPA; HPA001557; -.
MalaCards; AGT; -.
MIM; 106150; gene.
MIM; 145500; phenotype.
MIM; 267430; phenotype.
neXtProt; NX_P01019; -.
OpenTargets; ENSG00000135744; -.
Orphanet; 243761; Essential hypertension.
Orphanet; 97369; Renal tubular dysgenesis of genetic origin.
PharmGKB; PA42; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00890000139531; -.
HOVERGEN; HBG004233; -.
InParanoid; P01019; -.
KO; K09821; -.
OMA; RFMQAVT; -.
OrthoDB; EOG091G077M; -.
PhylomeDB; P01019; -.
TreeFam; TF343201; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; P01019; -.
ChiTaRS; AGT; human.
EvolutionaryTrace; P01019; -.
GeneWiki; Angiotensin; -.
GenomeRNAi; 183; -.
PMAP-CutDB; P01019; -.
PRO; PR:P01019; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000135744; -.
CleanEx; HS_AGT; -.
ExpressionAtlas; P01019; baseline and differential.
Genevisible; P01019; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; TAS:BHF-UCL.
GO; GO:0005179; F:hormone activity; ISS:BHF-UCL.
GO; GO:0048018; F:receptor agonist activity; IDA:BHF-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; TAS:BHF-UCL.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IPI:BHF-UCL.
GO; GO:0031703; F:type 2 angiotensin receptor binding; IPI:BHF-UCL.
GO; GO:0007202; P:activation of phospholipase C activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:BHF-UCL.
GO; GO:0003051; P:angiotensin-mediated drinking behavior; IEA:Ensembl.
GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
GO; GO:0001974; P:blood vessel remodeling; TAS:BHF-UCL.
GO; GO:0035411; P:catenin import into nucleus; IEA:Ensembl.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
GO; GO:0050663; P:cytokine secretion; IEA:Ensembl.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007199; P:G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; TAS:BHF-UCL.
GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; NAS:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IDA:BHF-UCL.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; TAS:BHF-UCL.
GO; GO:0034104; P:negative regulation of tissue remodeling; IEA:Ensembl.
GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:BHF-UCL.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; NAS:BHF-UCL.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IMP:UniProtKB.
GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IDA:UniProtKB.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IDA:BHF-UCL.
GO; GO:0001819; P:positive regulation of cytokine production; TAS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IEA:Ensembl.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:1903598; P:positive regulation of gap junction assembly; IGI:BHF-UCL.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; TAS:BHF-UCL.
GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; IEA:Ensembl.
GO; GO:1905010; P:positive regulation of L-lysine import across plasma membrane; IEA:Ensembl.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:1902632; P:positive regulation of membrane hyperpolarization; IMP:BHF-UCL.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; TAS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; TAS:BHF-UCL.
GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IGI:BHF-UCL.
GO; GO:0002034; P:regulation of blood vessel diameter by renin-angiotensin; TAS:BHF-UCL.
GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; NAS:BHF-UCL.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:1903779; P:regulation of cardiac conduction; IGI:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; NAS:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; NAS:BHF-UCL.
GO; GO:1901201; P:regulation of extracellular matrix assembly; IGI:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0014061; P:regulation of norepinephrine secretion; IEA:Ensembl.
GO; GO:0002019; P:regulation of renal output by angiotensin; NAS:BHF-UCL.
GO; GO:0035813; P:regulation of renal sodium excretion; NAS:BHF-UCL.
GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
GO; GO:0019229; P:regulation of vasoconstriction; NAS:BHF-UCL.
GO; GO:0003014; P:renal system process; IDA:UniProtKB.
GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; NAS:BHF-UCL.
GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:BHF-UCL.
GO; GO:0048659; P:smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
GO; GO:0070471; P:uterine smooth muscle contraction; IEA:Ensembl.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
CDD; cd02054; angiotensinogen; 1.
InterPro; IPR000227; Angiotensinogen.
InterPro; IPR033834; Angiotensinogen_serpin.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
PRINTS; PR00654; ANGIOTENSNGN.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
SIGNAL 1 33 {ECO:0000269|PubMed:4300938,
ECO:0000269|PubMed:7259779,
ECO:0000269|PubMed:7539791}.
CHAIN 34 485 Angiotensinogen.
/FTId=PRO_0000032456.
PEPTIDE 34 43 Angiotensin-1.
/FTId=PRO_0000032457.
PEPTIDE 34 42 Angiotensin 1-9.
/FTId=PRO_0000420659.
PEPTIDE 34 41 Angiotensin-2.
/FTId=PRO_0000032458.
PEPTIDE 34 40 Angiotensin 1-7.
/FTId=PRO_0000420660.
PEPTIDE 34 38 Angiotensin 1-5.
/FTId=PRO_0000420661.
PEPTIDE 34 37 Angiotensin 1-4.
/FTId=PRO_0000420662.
PEPTIDE 35 41 Angiotensin-3.
/FTId=PRO_0000032459.
PEPTIDE 36 41 Angiotensin-4.
/FTId=PRO_0000420663.
MOD_RES 34 34 Beta-decarboxylated aspartate; in form
angiotensin-A.
{ECO:0000269|PubMed:17138938}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3934016}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3934016}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3934016}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3934016}.
DISULFID 51 171 {ECO:0000269|PubMed:20927107}.
VARIANT 43 43 L -> F (associated with susceptibility to
pre-eclampsia; alters the reactions with
renin and angiotensin-converting enzyme;
dbSNP:rs41271499).
{ECO:0000269|PubMed:7744780}.
/FTId=VAR_022933.
VARIANT 98 98 E -> K (in dbSNP:rs11568032).
/FTId=VAR_029166.
VARIANT 114 114 G -> C (in dbSNP:rs2229389).
/FTId=VAR_051939.
VARIANT 137 137 T -> M (in dbSNP:rs34829218).
/FTId=VAR_035431.
VARIANT 207 207 T -> M (associated with hypertension;
dbSNP:rs4762).
{ECO:0000269|PubMed:1394429}.
/FTId=VAR_007093.
VARIANT 242 242 T -> I (associated with susceptibility to
hypertension; dbSNP:rs765678426).
{ECO:0000269|PubMed:7607642}.
/FTId=VAR_007094.
VARIANT 244 244 L -> R (associated with susceptibility to
hypertension; dbSNP:rs5041).
{ECO:0000269|PubMed:7607642}.
/FTId=VAR_007095.
VARIANT 268 268 M -> I (in dbSNP:rs11568053).
/FTId=VAR_029167.
VARIANT 268 268 M -> T (associated with essential
hypertension and pre-eclampsia;
dbSNP:rs699).
{ECO:0000269|PubMed:1394429,
ECO:0000269|PubMed:8513325}.
/FTId=VAR_007096.
VARIANT 281 281 Y -> C (associated with susceptibility to
hypertension; alters the structure,
glycosylation and secretion of
angiotensinogen; dbSNP:rs56073403).
{ECO:0000269|PubMed:1394429,
ECO:0000269|PubMed:7607642,
ECO:0000269|PubMed:8621667}.
/FTId=VAR_007097.
VARIANT 335 335 P -> S (in dbSNP:rs17856352).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_035432.
VARIANT 375 375 R -> Q (in RTD; dbSNP:rs74315283).
{ECO:0000269|PubMed:16116425}.
/FTId=VAR_035433.
VARIANT 392 392 L -> M (in dbSNP:rs1805090).
/FTId=VAR_014573.
CONFLICT 51 51 C -> S (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 58 58 N -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 333 333 Q -> E (in Ref. 2; AAA51679).
{ECO:0000305}.
TURN 42 44 {ECO:0000244|PDB:2WXW}.
HELIX 48 57 {ECO:0000244|PDB:2WXW}.
STRAND 59 62 {ECO:0000244|PDB:2WXW}.
HELIX 81 93 {ECO:0000244|PDB:2WXW}.
HELIX 97 117 {ECO:0000244|PDB:2WXW}.
HELIX 118 120 {ECO:0000244|PDB:2WXW}.
TURN 124 126 {ECO:0000244|PDB:2WXW}.
STRAND 129 134 {ECO:0000244|PDB:2WXW}.
HELIX 136 148 {ECO:0000244|PDB:2WXW}.
HELIX 154 162 {ECO:0000244|PDB:2WXW}.
TURN 171 173 {ECO:0000244|PDB:2WXW}.
HELIX 177 191 {ECO:0000244|PDB:2WXW}.
TURN 195 197 {ECO:0000244|PDB:2WXW}.
STRAND 203 212 {ECO:0000244|PDB:2WXW}.
HELIX 221 230 {ECO:0000244|PDB:2WXW}.
STRAND 234 236 {ECO:0000244|PDB:2WXW}.
HELIX 244 259 {ECO:0000244|PDB:2WXW}.
STRAND 277 288 {ECO:0000244|PDB:2WXW}.
STRAND 291 293 {ECO:0000244|PDB:2WXW}.
STRAND 302 305 {ECO:0000244|PDB:2WXW}.
STRAND 313 322 {ECO:0000244|PDB:2WXW}.
TURN 325 328 {ECO:0000244|PDB:2WXW}.
STRAND 329 333 {ECO:0000244|PDB:2WXW}.
TURN 337 339 {ECO:0000244|PDB:2WXW}.
STRAND 340 349 {ECO:0000244|PDB:2WXW}.
HELIX 353 358 {ECO:0000244|PDB:2WXW}.
HELIX 365 368 {ECO:0000244|PDB:2WXW}.
STRAND 374 381 {ECO:0000244|PDB:2WXW}.
STRAND 385 391 {ECO:0000244|PDB:2WXW}.
HELIX 392 395 {ECO:0000244|PDB:2WXW}.
HELIX 402 406 {ECO:0000244|PDB:2WXW}.
STRAND 407 409 {ECO:0000244|PDB:2WXW}.
STRAND 425 434 {ECO:0000244|PDB:2WXW}.
STRAND 452 455 {ECO:0000244|PDB:2WXW}.
STRAND 460 466 {ECO:0000244|PDB:2WXW}.
TURN 467 470 {ECO:0000244|PDB:2WXW}.
STRAND 475 479 {ECO:0000244|PDB:2WXW}.
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


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