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Protein Page:
angiotensin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
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
Cellular Component: extracellular space; extracellular region
Molecular Function: serine-type endopeptidase inhibitor activity; protein binding; growth factor activity; hormone activity; type 2 angiotensin receptor binding; type 1 angiotensin receptor binding
Biological Process: renal system process; extracellular matrix organization and biogenesis; establishment of blood-nerve barrier; negative regulation of nerve growth factor receptor signaling pathway; positive regulation of transcription, DNA-dependent; stress-activated MAPK cascade; positive regulation of multicellular organism growth; activation of NF-kappaB transcription factor; ovarian follicle rupture; positive regulation of fibroblast proliferation; cell-cell signaling; positive regulation of superoxide release; negative regulation of neuron apoptosis; kidney development; positive regulation of NAD(P)H oxidase activity; positive regulation of cytokine production; angiotensin mediated regulation of renal output; response to muscle activity involved in regulation of muscle adaptation; regulation of calcium ion transport; regulation of norepinephrine secretion; positive regulation of phosphoinositide 3-kinase cascade; negative regulation of tissue remodeling; positive regulation of peptidyl-tyrosine phosphorylation; phospholipase C activation; angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure; regulation of vasoconstriction; regulation of proteolysis; G-protein signaling, coupled to IP3 second messenger (phospholipase C activating); smooth muscle cell differentiation; nitric oxide mediated signal transduction; cytokine secretion; regulation of long-term neuronal synaptic plasticity; peristalsis; cell-matrix adhesion; renin-angiotensin regulation of aldosterone production; positive regulation of cellular protein metabolic process; smooth muscle cell proliferation; cellular lipid metabolic process; angiotensin maturation; excretion; vasodilation; response to salt stress; negative regulation of cell proliferation; positive regulation of MAPKKK cascade; fibroblast proliferation; renin-angiotensin regulation of blood vessel size; positive regulation of epidermal growth factor receptor signaling pathway; renin-angiotensin regulation of blood volume; regulation of cell growth; angiotensin mediated drinking behavior; artery smooth muscle contraction; aging; positive regulation of fatty acid biosynthetic process; blood vessel development; cellular sodium ion homeostasis; renal response to blood flow during renin-angiotensin regulation of systemic arterial blood pressure; activation of NF-kappaB-inducing kinase; positive regulation of organ growth; regulation of cell proliferation; G-protein coupled receptor protein signaling pathway; negative regulation of angiogenesis; cellular protein metabolic process; ureteric bud branching; G-protein signaling, coupled to cGMP nucleotide second messenger; blood vessel remodeling; response to cold; negative regulation of cell growth; astrocyte activation; positive regulation of inflammatory response
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


 SS 

SS: 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.


 MS 

MS: 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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