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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

  • 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

  • activation of NF-kappaB-inducing kinase activity 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 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 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)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...)Sequence analysis1
Disulfide bondi42 ↔ 1611 Publication
Glycosylationi319N-linked (GlcNAc...)Sequence analysis1
Glycosylationi401N-linked (GlcNAc...)Sequence 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

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000066488.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 34Combined sources3
Turni39 – 41Combined sources3
Helixi72 – 84Combined sources13
Helixi88 – 115Combined sources28
Beta strandi119 – 124Combined sources6
Helixi126 – 138Combined sources13
Helixi144 – 151Combined sources8
Helixi161 – 163Combined sources3
Helixi167 – 182Combined sources16
Beta strandi193 – 203Combined sources11
Helixi211 – 218Combined sources8
Beta strandi224 – 228Combined sources5
Helixi235 – 250Combined sources16
Beta strandi267 – 284Combined sources18
Beta strandi289 – 294Combined sources6
Beta strandi297 – 301Combined sources5
Beta strandi303 – 315Combined sources13
Turni316 – 319Combined sources4
Beta strandi320 – 340Combined sources21
Helixi341 – 343Combined sources3
Helixi344 – 351Combined sources8
Beta strandi366 – 373Combined sources8
Beta strandi375 – 382Combined sources8
Helixi383 – 389Combined sources7
Turni393 – 396Combined sources4
Beta strandi405 – 408Combined sources4
Beta strandi416 – 427Combined sources12
Beta strandi444 – 447Combined sources4
Beta strandi452 – 458Combined sources7
Turni459 – 461Combined sources3
Beta strandi464 – 471Combined sources8

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...

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
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

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...

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: November 2, 2016
This is version 126 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.