ACE-2 Products

Description

Angiotensin I Converting Enzyme 2 (ACE2), also known as ACEH (ACE homologue), is an integral membrane protein and a zinc metalloprotease of the ACE family (theoretical molecular weight 92 kDa). The predicted mouse ACE2 protein sequence consists of 798 amino acids, including an N-terminal signal peptide, a single catalytic domain, a C-terminal membrane anchor, and a short cytoplasmic tail. Mouse ACE2 is 40% homologous in amino acid identity to the N- and C-terminal domains of mouse somatic ACE. Enzymatically, ACE2 converts the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts Ang I to Ang II.

Genetic data from Drosophila, mice and rats show that the ACE2 protein is an essential regulator of heart function in vivo. ACE2 mRNA is found at high levels in testis, kidney and heart with moderate levels in colon, small intestine, and ovary. The ACE2 protein contributes to organ function through the renin-angiotensin system, playing a central role in vascular, renal, and myocardial physiology.

Virology research has demonstrated that the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein binds to its functional receptor, ACE2 (1). Vimentin is a type III intermediate filament protein expressed in mesenchymal cells that helps comprise the cytoskeleton in all animal cells. Studies have demonstrated that vimentin allows cell binding that allows the uptake of SARS-CoV spike protein into a host (2). This direct interaction of SARS-CoV with vimentin has been identified as an entry mechanism for the virus into a host, mediated by the SARS-CoV receptor ACE2 (1,2). It has been shown that ACE2 is the SARS-CoV-2 receptor required for cell entry and plays a physiological role in the replication of SARS-CoV in an infected host (1). Studies using human ACE2 antibody demonstrated a blockade of SARS-CoV-2 and ACE2 interaction, indicating an important physiological component of viral transmission and potential anti-viral therapeutic strategies (3).

References

1. Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., . . . Farzan, M. (2003). Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature, 426(6965), 450-454. doi:10.1038/nature02145

2. Yu YT, Chien SC, Chen IY, Lai CT, Tsay YG, Chang SC, Chang MF. (2016) Surface vimentin is critical for the cell entry of SARS-CoV. J Biomed Sci. doi: 10.1186/s12929-016-0234-7

3. Hoffmann, M., Kleine-Weber, H., Schroeder, S., Kruger, N., Herrler, T., Erichsen, S., . . . Pohlmann, S. (2020). SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. doi:10.1016/j.cell.2020.02.052

Bioinformatics

Entrez	59272 Human
Uniprot	NP_068576 Human Q9BYF1 Human
Product By Gene ID	59272
Alternate Names	ACEHangiotensin I converting enzyme 2 ACE-related carboxypeptidase angiotensin I converting enzyme (peptidyl-dipeptidase A) 2 angiotensin-converting enzyme 2 Angiotensin-converting enzyme homolog DKFZp434A014 EC 3.4.17 EC 3.4.17.23 Metalloprotease MPROT15

Diseases related to ACE-2

Discover more about diseases related to ACE-2.

Hypertensive Disease
Severe Acute Respiratory Syndrome
Kidney Diseases
Cardiovascular Diseases
Hypertrophy
Fibrosis
Diabetes Mellitus
Heart Failure
Diabetic Nephropathy
Inflammation
Injury To Kidney
Myocardial Infarction
Cardiac Hypertrophy
Infarction
Diabetes Mellitus, Experimental
Atherosclerosis
Pathologic Vasoconstriction
Infective Disorder
Proteinuria Of Undiagnosed Cause

Pathways for ACE-2

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Pathogenesis
Localization
Cell Cycle
Vasoconstriction
Mitosis
Cell Proliferation
Transport
Regulation Of Blood Pressure
Excretion
Membrane Fusion
Cell Division
Cytokinesis
Virulence
Cell Growth
Immune Response
Secretion
Mating
Glycosylation
Angiogenesis
Tropism

Research Areas for ACE-2

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Immunology
Virology, Bacteria and Parasites

PTMs for ACE-2

Learn more about PTMs related to ACE-2.

Cleavage
Phosphorylation
Glycosylation
Deglycosylation
Biotinylation
Oxidation
Carboxylation
Nitration
Reduction

Bioinformatics Tool for ACE-2

Discover related pathways, diseases and genes to ACE-2. Need help? Read the Bioinformatics Tool Guide for instructions on using this tool.
 

Related ACE-2 Blog Posts

Check out the latest blog posts on ACE-2.

Blocking SARS-CoV-2 Cell Entry: A potential Strategy Against COVID-19 Pandemic By Jamshed Arslan, Pharm. D., PhD. Coronaviruses are a family of enveloped RNA viruses. Some family members circulate in human populations, but others like severe acute respiratory syndrome coronavirus (SARS-CoV) ar...    Read more.

Tiny Antibodies (VHHs) from Llama Neutralize Respiratory Coronaviruses By Jamshed Arslan, Pharm. D., PhD. VHH Single Domain Antibodies vs Conventional AntibodiesThe immune system protects living organisms against harmful substances. B cells ward off infections by producing antibodies t...    Read more.

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COVID-19 and the Cardiovascular System: Observed complications and potential mechanisms By Victoria OsinskiThe outbreak of COVID-19 resulting from the transmission of the novel severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has resulted in many cases of illness typically manifesting in mi...    Read more.

COVID-19 and metabolic dysregulation: SARS-CoV-2 injures human exocrine and endocrine pancreas Jamshed Arslan, Pharm D, PhD Humans rely on the pancreas for digesting food and generating energy from it. SARS-CoV-2-mediated damage to the exocrine pancreas is evident from the pancreatitis, pancreatic enlargeme...    Read more.

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