Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Angiotensinogen

Gene

Agt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

  • hormone activity Source: MGI
  • serine-type endopeptidase inhibitor activity Source: GO_Central
  • type 1 angiotensin receptor binding Source: MGI
  • type 2 angiotensin receptor binding Source: MGI

GO - Biological processi

Keywordsi

Molecular functionVasoactive, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87963 Agt

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000003246025 – 477AngiotensinogenAdd BLAST453
PeptideiPRO_000003246125 – 34Angiotensin-110
PeptideiPRO_000042066425 – 33Angiotensin 1-99
PeptideiPRO_000003246225 – 32Angiotensin-28
PeptideiPRO_000042066525 – 31Angiotensin 1-77
PeptideiPRO_000042066625 – 29Angiotensin 1-55
PeptideiPRO_000042066725 – 28Angiotensin 1-44
PeptideiPRO_000003246326 – 32Angiotensin-37
PeptideiPRO_000042066827 – 32Angiotensin-46

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi42 ↔ 1611 Publication
Glycosylationi319N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1

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

MaxQBiP11859
PaxDbiP11859
PeptideAtlasiP11859
PRIDEiP11859

PTM databases

iPTMnetiP11859
PhosphoSitePlusiP11859
SwissPalmiP11859

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066488

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP11859
SMRiP11859
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

InterProiView protein in InterPro
IPR000227 Angiotensinogen
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PTHR11461:SF13 PTHR11461:SF13, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
PRINTSiPR00654 ANGIOTENSNGN
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3UTR7Q3UTR7_MOUSE
Angiotensinogen
Agt
482Annotation score:

Sequence databases

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

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WXXX-ray2.95A/B/C/D25-477[»]
2WXYX-ray2.10C25-477[»]
2WY0X-ray2.38C25-477[»]
ProteinModelPortaliP11859
SMRiP11859
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066488

Protein family/group databases

MEROPSiI04.953

PTM databases

iPTMnetiP11859
PhosphoSitePlusiP11859
SwissPalmiP11859

Proteomic databases

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

ChiTaRSiMgmt mouse
EvolutionaryTraceiP11859
PROiPR:P11859
SOURCEiSearch...

Family and domain databases

InterProiView protein in InterPro
IPR000227 Angiotensinogen
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PTHR11461:SF13 PTHR11461:SF13, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
PRINTSiPR00654 ANGIOTENSNGN
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiANGT_MOUSE
AccessioniPrimary (citable) accession number: P11859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 7, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again