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Protein Page:
ACE (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ACE Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Defects in ACE 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). Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH). A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. Belongs to the peptidase M2 family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.2.1.-; Protease; Membrane protein, integral; EC 3.4.15.1
Cellular Component: extracellular space; extracellular region; plasma membrane; integral to membrane; endosome; external side of plasma membrane
Molecular Function: peptidyl-dipeptidase activity; protein binding; carboxypeptidase activity; metallopeptidase activity; zinc ion binding; bradykinin receptor binding; endopeptidase activity; drug binding; chloride ion binding; actin binding
Biological Process: mononuclear cell proliferation; regulation of vasodilation; angiotensin mediated regulation of renal output; angiotensin maturation; arachidonic acid secretion; regulation of systemic arterial blood pressure by renin-angiotensin; regulation of smooth muscle cell migration; cellular protein metabolic process; peptide catabolic process; regulation of blood pressure; regulation of vasoconstriction; angiotensin catabolic process in blood; hormone catabolic process; blood vessel remodeling; kidney development
Reference #:  P12821 (UniProtKB)
Alt. Names/Synonyms: ACE; ACE1; angiotensin converting enzyme, somatic isoform; angiotensin I converting enzyme (peptidyl-dipeptidase A) 1; angiotensin I converting enzyme 1; Angiotensin-converting enzyme; Angiotensin-converting enzyme, soluble form; carboxycathepsin; CD143; CD143 antigen; DCP; DCP1; dipeptidyl carboxypeptidase 1; Dipeptidyl carboxypeptidase I; Kininase II; MGC26566; MVCD3; peptidase P; testicular ECA
Gene Symbols: ACE
Molecular weight: 149,715 Da
Basal Isoelectric point: 5.95  Predict pI for various phosphorylation states
Select Structure to View Below

ACE

Protein Structure Not Found.


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Sites Implicated In
exocytosis, altered: S1299‑p
intracellular localization: S1299‑p
molecular association, regulation: S1299‑p
protein degradation: S1299‑p

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

► Hide Isoforms
 
0 1 K718-u QLQNTTIkRIIKKVQ
0 1 - gap
7 25 S1299-p SHGPQFGsEVELRHS
0 1 S1306 sEVELRHS_______
  ACE iso2  
K144 QLQNTTIKRIIKKVQ
Y700-p GTREAPVyMSKRAAS
- gap
- gap
  mouse

 
K723 NFQNSSIKRIIKKLQ
- gap
S1305-p HRGPQFGsEVELRHs
S1312-p sEVELRHs_______
  rat

 
K724 NFQNSTIKRIIKKVQ
- gap
S1306 HRGPQFGSEVELRHS
S1313 SEVELRHS_______
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