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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_MOUSE              Reviewed;         477 AA.
P11859;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 132.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3397061; DOI=10.1016/0888-7543(88)90008-0;
Clouston W.M., Evans B.A., Haralambidis J., Richards R.I.;
"Molecular cloning of the mouse angiotensinogen gene.";
Genomics 2:240-248(1988).
[2]
FUNCTION OF ANGIOTENSIN 1-7 AS LIGAND FOR MAS1.
PubMed=12829792; DOI=10.1073/pnas.1432869100;
Santos R.A.S., Simoes e Silva A.C., Maric C., Silva D.M.R.,
Machado R.P., de Buhr I., Heringer-Walther S., Pinheiro S.V.B.,
Lopes M.T., Bader M., Mendes E.P., Lemos V.S., Campagnole-Santos M.J.,
Schultheiss H.-P., Speth R., Walther T.;
"Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled
receptor Mas.";
Proc. Natl. Acad. Sci. U.S.A. 100:8258-8263(2003).
[3]
FUNCTION OF ANGIOTENSIN 1-7.
PubMed=18026570; DOI=10.2119/2007-00073.Fraga-Silva;
Fraga-Silva R.A., Pinheiro S.V.B., Goncalves A.C., Alenina N.,
Bader M., Santos R.A.S.;
"The antithrombotic effect of angiotensin-(1-7) involves mas-mediated
NO release from platelets.";
Mol. Med. 14:28-35(2008).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-477, 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).
-!- 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. {ECO:0000250}.
-!- FUNCTION: Angiotensin-3: stimulates aldosterone release.
{ECO:0000250}.
-!- 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.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- 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 (By similarity). Angiotensin
1-9 is cleaved from angiotensin-1 by ACE2 (By similarity) 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) (By similarity). {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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EMBL; AF045887; AAC01765.1; -; Genomic_DNA.
EMBL; AF045886; AAC01765.1; JOINED; Genomic_DNA.
EMBL; AF045885; AAC01765.1; JOINED; Genomic_DNA.
EMBL; AF045884; AAC01765.1; JOINED; Genomic_DNA.
PIR; A29978; A29978.
UniGene; Mm.301626; -.
PDB; 2WXX; X-ray; 2.95 A; A/B/C/D=25-477.
PDB; 2WXY; X-ray; 2.10 A; C=25-477.
PDB; 2WY0; X-ray; 2.38 A; C=25-477.
PDBsum; 2WXX; -.
PDBsum; 2WXY; -.
PDBsum; 2WY0; -.
ProteinModelPortal; P11859; -.
SMR; P11859; -.
STRING; 10090.ENSMUSP00000066488; -.
MEROPS; I04.953; -.
iPTMnet; P11859; -.
PhosphoSitePlus; P11859; -.
SwissPalm; P11859; -.
MaxQB; P11859; -.
PaxDb; P11859; -.
PeptideAtlas; P11859; -.
PRIDE; P11859; -.
MGI; MGI:87963; Agt.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
HOVERGEN; HBG004233; -.
InParanoid; P11859; -.
PhylomeDB; P11859; -.
EvolutionaryTrace; P11859; -.
PRO; PR:P11859; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IDA:MGI.
GO; GO:0031703; F:type 2 angiotensin receptor binding; IPI:MGI.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI.
GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IDA:MGI.
GO; GO:0048143; P:astrocyte activation; IMP:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0002035; P:brain renin-angiotensin system; IDA:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0042756; P:drinking behavior; IMP:MGI.
GO; GO:0008065; P:establishment of blood-nerve barrier; IMP:MGI.
GO; GO:0007588; P:excretion; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
GO; GO:0001543; P:ovarian follicle rupture; IMP:MGI.
GO; GO:0030432; P:peristalsis; IMP:MGI.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; ISO:MGI.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:MGI.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:MGI.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:MGI.
GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0046622; P:positive regulation of organ growth; IDA:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:MGI.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:1903779; P:regulation of cardiac conduction; ISO:MGI.
GO; GO:1901201; P:regulation of extracellular matrix assembly; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IDA:MGI.
GO; GO:0002019; P:regulation of renal output by angiotensin; IMP:MGI.
GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IMP:MGI.
GO; GO:0001999; P:renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0003014; P:renal system process; ISO:MGI.
GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IMP:MGI.
GO; GO:0009409; P:response to cold; IMP:MGI.
GO; GO:0009651; P:response to salt stress; IMP:MGI.
GO; GO:0051145; P:smooth muscle cell differentiation; IDA:MGI.
GO; GO:0048659; P:smooth muscle cell proliferation; IDA:MGI.
InterPro; IPR000227; Angiotensinogen.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
PANTHER; PTHR11461:SF13; PTHR11461:SF13; 1.
Pfam; PF00079; Serpin; 1.
PRINTS; PR00654; ANGIOTENSNGN.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
SIGNAL 1 24
CHAIN 25 477 Angiotensinogen.
/FTId=PRO_0000032460.
PEPTIDE 25 34 Angiotensin-1.
/FTId=PRO_0000032461.
PEPTIDE 25 33 Angiotensin 1-9.
/FTId=PRO_0000420664.
PEPTIDE 25 32 Angiotensin-2.
/FTId=PRO_0000032462.
PEPTIDE 25 31 Angiotensin 1-7.
/FTId=PRO_0000420665.
PEPTIDE 25 29 Angiotensin 1-5.
/FTId=PRO_0000420666.
PEPTIDE 25 28 Angiotensin 1-4.
/FTId=PRO_0000420667.
PEPTIDE 26 32 Angiotensin-3.
/FTId=PRO_0000032463.
PEPTIDE 27 32 Angiotensin-4.
/FTId=PRO_0000420668.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 161 {ECO:0000269|PubMed:20927107}.
HELIX 32 34 {ECO:0000244|PDB:2WXY}.
TURN 39 41 {ECO:0000244|PDB:2WY0}.
HELIX 72 84 {ECO:0000244|PDB:2WXY}.
HELIX 88 115 {ECO:0000244|PDB:2WXY}.
STRAND 119 124 {ECO:0000244|PDB:2WXY}.
HELIX 126 138 {ECO:0000244|PDB:2WXY}.
HELIX 144 151 {ECO:0000244|PDB:2WXY}.
HELIX 161 163 {ECO:0000244|PDB:2WXY}.
HELIX 167 182 {ECO:0000244|PDB:2WXY}.
STRAND 193 203 {ECO:0000244|PDB:2WXY}.
HELIX 211 218 {ECO:0000244|PDB:2WXY}.
STRAND 224 228 {ECO:0000244|PDB:2WXY}.
HELIX 235 250 {ECO:0000244|PDB:2WXY}.
STRAND 267 284 {ECO:0000244|PDB:2WXY}.
STRAND 289 294 {ECO:0000244|PDB:2WXY}.
STRAND 297 301 {ECO:0000244|PDB:2WXY}.
STRAND 303 315 {ECO:0000244|PDB:2WXY}.
TURN 316 319 {ECO:0000244|PDB:2WXY}.
STRAND 320 340 {ECO:0000244|PDB:2WXY}.
HELIX 341 343 {ECO:0000244|PDB:2WXY}.
HELIX 344 351 {ECO:0000244|PDB:2WXY}.
STRAND 366 373 {ECO:0000244|PDB:2WXY}.
STRAND 375 382 {ECO:0000244|PDB:2WXY}.
HELIX 383 389 {ECO:0000244|PDB:2WXY}.
TURN 393 396 {ECO:0000244|PDB:2WXY}.
STRAND 405 408 {ECO:0000244|PDB:2WXY}.
STRAND 416 427 {ECO:0000244|PDB:2WXY}.
STRAND 444 447 {ECO:0000244|PDB:2WXY}.
STRAND 452 458 {ECO:0000244|PDB:2WXY}.
TURN 459 461 {ECO:0000244|PDB:2WXY}.
STRAND 464 471 {ECO:0000244|PDB:2WXY}.
SEQUENCE 477 AA; 51990 MW; A877F4029F338607 CRC64;
MTPTGAGLKA TIFCILTWVS LTAGDRVYIH PFHLLYHNKS TCAQLENPSV ETLPESTFEP
VPIQAKTSPV NEKTLHDQLV LAAEKLEDED RKRAAQVAMI ANFVGFRMYK MLNEAGSGAS
GAILSPPALF GTLVSFYLGS LDPTASQLQT LLDVPVKEGD CTSRLDGHKV LAALRAVQGL
LVTQGGSSSQ TPLLQSIMVG LFTAPGFRLK HSFVQSLALF TPALFPRSLD LSTDPVLATE
KINRFIKAVT GWKMNLPLEG VSTDSTLLFN TYVHFQGTMR GFSQLPGVHE FWVDNSISVS
VPMISGTGNF QHWSDAQNNF SVTCVPLGER ATLLLIQPHC TSDLDRVEAL IFRNDLLTWI
ENPPPRAIRL TLPQLEIRGS YNLQDLLAED KLPTLLGAEA NLSNIGDTNP RVGEVLNSIL
LELKAGEEEQ PTTSVQQPGS PEALDVTLSS PFLFAIYEQD SGTLHFLGRV NNPQSVV


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