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MGP005699

UniProt Annotations

Entry Information
Gene Nameangiotensin I converting enzyme 2
Protein EntryACE2_HUMAN
UniProt IDQ9BYF1
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9BYF1-1; Sequence=Displayed; Name=2; IsoId=Q9BYF1-2; Sequence=VSP_014901, VSP_014902; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=6.9 uM for angiotensin I {ECO:0000269|PubMed:11815627}; KM=2 uM for angiotensin II {ECO:0000269|PubMed:11815627}; KM=6.8 uM for apelin-13 {ECO:0000269|PubMed:11815627}; KM=5.5 uM for dynorphin-13 {ECO:0000269|PubMed:11815627}; pH dependence: Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9. {ECO:0000269|PubMed:11815627};
Catalytic ActivityAngiotensin II + H(2)O = angiotensin-(1-7) + L-phenylalanine.
CofactorName=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11815627}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11815627};
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11815627}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11815627};
Enzyme RegulationActivated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril and enalaprilat. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:15231706}.
FunctionCarboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- 13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:24227843}.
InductionUp-regulated in failing heart. {ECO:0000269|PubMed:15151696, ECO:0000269|PubMed:15671045}.
PtmN-glycosylation on Asn-90 may limit SARS infectivity. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19159218}.
PtmProteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1. {ECO:0000269|PubMed:15983030, ECO:0000269|PubMed:21068237, ECO:0000269|PubMed:21563828, ECO:0000269|PubMed:24227843}.
SimilarityBelongs to the peptidase M2 family. {ECO:0000305}.
Subcellular LocationCell membrane; Single-pass type I membrane protein. Cytoplasm {ECO:0000250}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250}.
Subcellular LocationProcessed angiotensin-converting enzyme 2: Secreted.
SubunitInteracts with ITGB1. Interacts with SARS-CoV and HCoV- NL63 spike glycoprotein. Interacts with the catalytically active form of TMPRSS2. {ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15276642, ECO:0000269|PubMed:15452268, ECO:0000269|PubMed:15791205, ECO:0000269|PubMed:15897467, ECO:0000269|PubMed:21068237}.
Tissue SpecificityExpressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15141377, ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:15671045}.
Web ResourceName=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ace2/";
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