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Protein

Angiotensinogen

Gene

Agt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.
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.By similarity
Angiotensin-3: stimulates aldosterone release.By similarity
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.

GO - Molecular functioni

GO - Biological processi

  • activation of NF-kappaB-inducing kinase activity Source: MGI
  • angiotensin-activated signaling pathway Source: MGI
  • angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure Source: MGI
  • astrocyte activation Source: MGI
  • blood vessel development Source: MGI
  • brain renin-angiotensin system Source: MGI
  • branching involved in ureteric bud morphogenesis Source: MGI
  • cell-matrix adhesion Source: MGI
  • drinking behavior Source: MGI
  • establishment of blood-nerve barrier Source: MGI
  • excretion Source: MGI
  • extracellular matrix organization Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • hormone metabolic process Source: MGI
  • kidney development Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of neurotrophin TRK receptor signaling pathway Source: MGI
  • ovarian follicle rupture Source: MGI
  • peristalsis Source: MGI
  • positive regulation of activation of JAK2 kinase activity Source: MGI
  • positive regulation of branching involved in ureteric bud morphogenesis Source: MGI
  • positive regulation of cellular protein metabolic process Source: MGI
  • positive regulation of cholesterol esterification Source: MGI
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of endothelial cell migration Source: MGI
  • positive regulation of epidermal growth factor receptor signaling pathway Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of fatty acid biosynthetic process Source: MGI
  • positive regulation of gap junction assembly Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of membrane hyperpolarization Source: MGI
  • positive regulation of multicellular organism growth Source: MGI
  • positive regulation of organ growth Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • positive regulation of protein kinase C activity Source: MGI
  • positive regulation of protein tyrosine kinase activity Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • regulation of apoptotic process Source: MGI
  • regulation of blood pressure Source: MGI
  • regulation of cardiac conduction Source: MGI
  • regulation of extracellular matrix assembly Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of inflammatory response Source: MGI
  • regulation of renal output by angiotensin Source: MGI
  • regulation of systemic arterial blood pressure by circulatory renin-angiotensin Source: MGI
  • renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure Source: MGI
  • renal system process Source: MGI
  • renin-angiotensin regulation of aldosterone production Source: MGI
  • response to cold Source: MGI
  • response to salt stress Source: MGI
  • smooth muscle cell differentiation Source: MGI
  • smooth muscle cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Vasoactive, Vasoconstrictor

Protein family/group databases

MEROPSiI04.953.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensinogen
Alternative name(s):
Serpin A8
Cleaved into the following 8 chains:
Alternative name(s):
Angiotensin 1-10
Angiotensin I
Short name:
Ang I
Alternative name(s):
Angiotensin 1-8
Angiotensin II
Short name:
Ang II
Alternative name(s):
Angiotensin 2-8
Angiotensin III
Short name:
Ang III
Des-Asp[1]-angiotensin II
Alternative name(s):
Angiotensin 3-8
Angiotensin IV
Short name:
Ang IV
Gene namesi
Name:Agt
Synonyms:Serpina8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87963. Agt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 477453AngiotensinogenPRO_0000032460Add
BLAST
Peptidei25 – 3410Angiotensin-1PRO_0000032461
Peptidei25 – 339Angiotensin 1-9PRO_0000420664
Peptidei25 – 328Angiotensin-2PRO_0000032462
Peptidei25 – 317Angiotensin 1-7PRO_0000420665
Peptidei25 – 295Angiotensin 1-5PRO_0000420666
Peptidei25 – 284Angiotensin 1-4PRO_0000420667
Peptidei26 – 327Angiotensin-3PRO_0000032463
Peptidei27 – 326Angiotensin-4PRO_0000420668

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi42 ↔ 1611 Publication
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

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).By similarity
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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP11859.
MaxQBiP11859.
PaxDbiP11859.
PeptideAtlasiP11859.
PRIDEiP11859.

PTM databases

iPTMnetiP11859.
PhosphoSiteiP11859.
SwissPalmiP11859.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

GO - Molecular functioni

  • receptor agonist activity Source: MGI
  • type 1 angiotensin receptor binding Source: MGI
  • type 2 angiotensin receptor binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066488.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343Combined sources
Turni39 – 413Combined sources
Helixi72 – 8413Combined sources
Helixi88 – 11528Combined sources
Beta strandi119 – 1246Combined sources
Helixi126 – 13813Combined sources
Helixi144 – 1518Combined sources
Helixi161 – 1633Combined sources
Helixi167 – 18216Combined sources
Beta strandi193 – 20311Combined sources
Helixi211 – 2188Combined sources
Beta strandi224 – 2285Combined sources
Helixi235 – 25016Combined sources
Beta strandi267 – 28418Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi303 – 31513Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 34021Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 3518Combined sources
Beta strandi366 – 3738Combined sources
Beta strandi375 – 3828Combined sources
Helixi383 – 3897Combined sources
Turni393 – 3964Combined sources
Beta strandi405 – 4084Combined sources
Beta strandi416 – 42712Combined sources
Beta strandi444 – 4474Combined sources
Beta strandi452 – 4587Combined sources
Turni459 – 4613Combined sources
Beta strandi464 – 4718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WXXX-ray2.95A/B/C/D25-477[»]
2WXYX-ray2.10C25-477[»]
2WY0X-ray2.38C25-477[»]
ProteinModelPortaliP11859.
SMRiP11859. Positions 25-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11859.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
HOVERGENiHBG004233.
InParanoidiP11859.
PhylomeDBiP11859.

Family and domain databases

InterProiIPR000227. Angiotensinogen.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 2 hits.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
PRINTSiPR00654. ANGIOTENSNGN.
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPTGAGLKA TIFCILTWVS LTAGDRVYIH PFHLLYHNKS TCAQLENPSV
60 70 80 90 100
ETLPESTFEP VPIQAKTSPV NEKTLHDQLV LAAEKLEDED RKRAAQVAMI
110 120 130 140 150
ANFVGFRMYK MLNEAGSGAS GAILSPPALF GTLVSFYLGS LDPTASQLQT
160 170 180 190 200
LLDVPVKEGD CTSRLDGHKV LAALRAVQGL LVTQGGSSSQ TPLLQSIMVG
210 220 230 240 250
LFTAPGFRLK HSFVQSLALF TPALFPRSLD LSTDPVLATE KINRFIKAVT
260 270 280 290 300
GWKMNLPLEG VSTDSTLLFN TYVHFQGTMR GFSQLPGVHE FWVDNSISVS
310 320 330 340 350
VPMISGTGNF QHWSDAQNNF SVTCVPLGER ATLLLIQPHC TSDLDRVEAL
360 370 380 390 400
IFRNDLLTWI ENPPPRAIRL TLPQLEIRGS YNLQDLLAED KLPTLLGAEA
410 420 430 440 450
NLSNIGDTNP RVGEVLNSIL LELKAGEEEQ PTTSVQQPGS PEALDVTLSS
460 470
PFLFAIYEQD SGTLHFLGRV NNPQSVV
Length:477
Mass (Da):51,990
Last modified:October 1, 1989 - v1
Checksum:iA877F4029F338607
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045887
, AF045886, AF045885, AF045884 Genomic DNA. Translation: AAC01765.1.
PIRiA29978.
UniGeneiMm.301626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045887
, AF045886, AF045885, AF045884 Genomic DNA. Translation: AAC01765.1.
PIRiA29978.
UniGeneiMm.301626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WXXX-ray2.95A/B/C/D25-477[»]
2WXYX-ray2.10C25-477[»]
2WY0X-ray2.38C25-477[»]
ProteinModelPortaliP11859.
SMRiP11859. Positions 25-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066488.

Protein family/group databases

MEROPSiI04.953.

PTM databases

iPTMnetiP11859.
PhosphoSiteiP11859.
SwissPalmiP11859.

Proteomic databases

EPDiP11859.
MaxQBiP11859.
PaxDbiP11859.
PeptideAtlasiP11859.
PRIDEiP11859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:87963. Agt.

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
HOVERGENiHBG004233.
InParanoidiP11859.
PhylomeDBiP11859.

Miscellaneous databases

EvolutionaryTraceiP11859.
PROiP11859.
SOURCEiSearch...

Family and domain databases

InterProiIPR000227. Angiotensinogen.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 2 hits.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
PRINTSiPR00654. ANGIOTENSNGN.
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the mouse angiotensinogen gene."
    Clouston W.M., Evans B.A., Haralambidis J., Richards R.I.
    Genomics 2:240-248(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: FUNCTION OF ANGIOTENSIN 1-7 AS LIGAND FOR MAS1.
  3. "The antithrombotic effect of angiotensin-(1-7) involves mas-mediated NO release from platelets."
    Fraga-Silva R.A., Pinheiro S.V.B., Goncalves A.C., Alenina N., Bader M., Santos R.A.S.
    Mol. Med. 14:28-35(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ANGIOTENSIN 1-7.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung and Testis.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-477, DISULFIDE BOND.

Entry informationi

Entry nameiANGT_MOUSE
AccessioniPrimary (citable) accession number: P11859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.