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Protein Page:
angiotensin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
angiotensin Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. In response to lowered blood pressure, the enzyme renin cleaves angiotensinogen to produce angiotensin-1 (angiotensin 1-10). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2 (angiotensin 1- 8). Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3 (angiotensin 2-8), angiotensin-4 (angiotensin 3-8). Angiotensin 1-7 is cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2. Genetic variations in AGT are a cause of susceptibility to essential hypertension (EHT). Essential hypertension is a condition in which blood pressure is consistently higher than normal with no identifiable cause. Defects in AGT are a cause of renal tubular dysgenesis (RTD). RTD is an 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). Belongs to the serpin family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: 1q42.2
Cellular Component: extracellular region; extracellular space
Molecular Function: growth factor activity; hormone activity; protein binding; serine-type endopeptidase inhibitor activity; type 1 angiotensin receptor binding; type 2 angiotensin receptor binding
Biological Process: activation of NF-kappaB transcription factor; angiotensin maturation; blood vessel remodeling; cell-cell signaling; G-protein coupled receptor protein signaling pathway; G-protein signaling, coupled to cGMP nucleotide second messenger; kidney development; negative regulation of nerve growth factor receptor signaling pathway; nitric oxide mediated signal transduction; positive regulation of cellular protein metabolic process; positive regulation of cytokine production; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of fibroblast proliferation; positive regulation of inflammatory response; positive regulation of NAD(P)H oxidase activity; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of transcription, DNA-dependent; regulation of blood pressure; renal system process; renin-angiotensin regulation of blood vessel size; response to muscle activity involved in regulation of muscle adaptation
Disease: Hypertension, Essential; Renal Tubular Dysgenesis
Reference #:  P01019 (UniProtKB)
Alt. Names/Synonyms: AGT; alpha-1 antiproteinase, antitrypsin; Ang I; Ang II; Ang III; Angiotensin I; Angiotensin II; Angiotensin III; Angiotensin-1; Angiotensin-2; Angiotensin-3; Angiotensinogen; angiotensinogen (serpin peptidase inhibitor, clade A, member 8); ANGT; ANHU; Des-Asp[1]-angiotensin II; FLJ92595; FLJ97926; pre-angiotensinogen; serine (or cysteine) proteinase inhibitor; Serpin A8; SERPINA8
Gene Symbols: AGT
Molecular weight: 53,154 Da
Basal Isoelectric point: 5.87  Predict pI for various phosphorylation states
Select Structure to View Below

angiotensin

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T20 AGVSLRATILCLLAW
0 2 Y37 LAAGDRVYIHPFHLV
0 1 I45 IHPFHLVIHNESTCE
0 1 H46 HPFHLVIHNESTCEQ
0 1 N47 PFHLVIHNESTCEQL
0 1 K287‑ac TYVHFQGkMKGFSLL
  mouse

 
T11 TGAGLKATIFCILTW
Y28‑p LTAGDRVyIHPFHLL
Y36 IHPFHLLYHNKSTCA
H37 HPFHLLYHNKSTCAQ
N38 PFHLLYHNKSTCAQL
T278 TYVHFQGTMRGFSQL
  rat

 
T11‑p TGAGLKAtIFCILTW
Y28‑p LTAGDRVyIHPFHLL
Y36‑p IHPFHLLyysKSTCA
Y37‑p HPFHLLyysKSTCAQ
S38‑p PFHLLyysKSTCAQL
K278 TYVHFQGKMRGFSQL
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