3.4.17.23	cell membrane	-	-	708649	
3.4.17.23	cell surface	-	9986	707074	
3.4.17.23	cell surface	cell-surface non-raft protein with the extracellular N-terminal and intracellular C-terminal domains. Binding to SARS-CoV-2 protein S induces the ACE2 internalization	9986	762787	
3.4.17.23	cytoplasm	-	5737	710171	
3.4.17.23	cytoplasm	ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17	5737	694170	
3.4.17.23	membrane	-	16020	658459, 659147, 679300, 679706, 679708, 680388, 710171	
3.4.17.23	membrane	ACE 2 is shedded	16020	707074	
3.4.17.23	membrane	ACE2 also undergoes phorbol-12-myristate-13-acetate-inducible ectodomain shedding from the membrane	16020	679705	
3.4.17.23	membrane	ACE2 exists as bothmembrane bound and soluble forms, the latter being generated by proteolytic cleavage of the ectodomain by the tumor necrosis factor convertase ADAM17	16020	694170	
3.4.17.23	membrane	ACE2 is a type I membrane-anchored protein with a catalytically active ectodomain, that undergoes shedding	16020	707055	
3.4.17.23	membrane	enzyme possesses a transmembrane domain, posttranslational cleavage for secretion of the protein in vivo and in cell culture	16020	658455	
3.4.17.23	membrane	integral membrane protein	16020	692972	
3.4.17.23	membrane	the larger form of ACE2 is a type I membrane-anchored protein with a catalytically active ectodomain, that undergoes shedding resulting in the smaller soluble enzyme form	16020	707055	
3.4.17.23	membrane	the monomer of homodimeric ACE2 is a type 1 transmembrane protein with a single transmembrane alpha-helix in the C-terminal region similar to the collectrin domain	16020	762898	
3.4.17.23	membrane	transmembrane enzyme	16020	678102	
3.4.17.23	membrane	type I transmembrane metallocarboxypeptidase	16020	763160	
3.4.17.23	additional information	transmembrane domain	-	658963	
3.4.17.23	plasma membrane	evenly distributed to detergent-soluble regions of the plasma membrane in non-polarized CHO cells, in polarized Madin-Darby canine kidney epithelial cells ACE is localized predominantly to the apical surface (92%) where it is proteolytically cleaved within the ectodomain to release a soluble form, recombinantly expressed enzymes	5886	669404	
3.4.17.23	plasma membrane	the ACE2 ectodomain can be cleaved from the cell membrane and released into the extracellular milieu	5886	679876	
3.4.17.23	plasma membrane	the full-length enzyme (ACE2) contains a structural transmembrane domain, which anchors its extracellular domain to the plasma membrane	5886	753315	
3.4.17.23	soluble	ACE 2 is shedded	-	707074	
3.4.17.23	soluble	smaller enzyme form without ectodomain	-	707055	
3.4.17.23	soluble	the soluble form of angiotensin-converting enzyme 2 lacks the membrane anchor and circulates in small amounts in the blood	-	753315