F7F5D8 · F7F5D8_MACMU
- ProteinAngiotensin-converting enzyme
- GeneACE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1266 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.
Catalytic activity
- Leu-enkephalin + H2O = L-tyrosylglycylglycine + L-phenylalanyl-L-leucineThis reaction proceeds in the forward direction.
- Met-enkephalin + H2O = L-phenylalanyl-L-methionine + L-tyrosylglycylglycineThis reaction proceeds in the forward direction.
- Met-enkephalin-Arg-Phe + H2O = L-arginyl-L-phenylalanine + Met-enkephalinThis reaction proceeds in the forward direction.
- neurotensin + H2O = neurotensin(1-11) + L-isoleucyl-L-leucineThis reaction proceeds in the forward direction.
- substance P + H2O = substance P(1-8) + Gly-L-Leu-L-Met-NH2This reaction proceeds in the forward direction.
- substance P + H2O = substance P(1-9) + L-Leu-L-Met-NH2This reaction proceeds in the forward direction.
- substance P + H2O = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-6)This reaction proceeds in the forward direction.
- bradykinin + H2O = L-Phe-L-Arg + bradykinin(1-7)This reaction proceeds in the forward direction.
- goralatide + H2O = N-acetyl-L-seryl-L-aspartate + L-lysyl-L-prolineThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 392 | Proton acceptor 1 | ||||
Sequence: E | ||||||
Active site | 521 | Proton donor 1 | ||||
Sequence: H | ||||||
Active site | 990 | Proton acceptor 2 | ||||
Sequence: E | ||||||
Active site | 1119 | Proton donor 2 | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallopeptidase activity | |
Molecular Function | peptidyl-dipeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAngiotensin-converting enzyme
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionF7F5D8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1217-1236 | Helical | ||||
Sequence: VGQWLLLFLGIALLVATLGL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MGAASGRQGPGPLLQPLLLLLLLPPQPALA | ||||||
Chain | PRO_5023844228 | 31-1266 | Angiotensin-converting enzyme | |||
Sequence: LDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPELRKIIGAVGTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRGGANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFNGRTPPSHYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYQSTKAGAKLRKVLQAGSSRPWQEVLKDMVGSDALDAQPLLNYFQPVTQWLQEQNRQNGEVLGWPEYQWRPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARRFDVNHFQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHTNGSCLQLEPDLTNVMATSRKYEELLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDPTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSHEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHVPSSVPYIRTAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHQSLHQHPQGPQFGSEVELRHS | ||||||
Glycosylation | 39 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 55 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 112 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 147 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 158↔166 | |||||
Sequence: CLPNKTATC | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 319 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 360↔378 | |||||
Sequence: CHASAWDFYNRKDFRIKQC | ||||||
Glycosylation | 446 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 510 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 546↔558 | |||||
Sequence: CKEAGYEGPLHQC | ||||||
Glycosylation | 678 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 696 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 715 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 761 | N-linked (GlcNAc...) asparagine; partial | ||||
Sequence: N | ||||||
Glycosylation | 943 | N-linked (GlcNAc...) asparagine; partial | ||||
Sequence: N | ||||||
Disulfide bond | 958↔976 | |||||
Sequence: CHASAWDFYNGKDFRIKQC | ||||||
Glycosylation | 1151 | N-linked (GlcNAc...) asparagine; partial | ||||
Sequence: N |
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Monomer and homodimer; homodimerizes following binding to an inhibitor. Interacts with calmodulin (CALM1, CALM2 or CALM3); interaction takes place in the cytoplasmic region and regulates phosphorylation and proteolytic cleavage.
Structure
Sequence
- Sequence statusComplete
- Length1,266
- Mass (Da)144,901
- Last updated2019-12-11 v3
- Checksum4B36590B6FBEDAEF
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1D5R9B8 | A0A1D5R9B8_MACMU | ACE | 1307 | ||
G7NJ76 | G7NJ76_MACMU | ACE | 342 | ||
A0A5K1VF83 | A0A5K1VF83_MACMU | ACE | 349 | ||
A0A5F8ANI1 | A0A5F8ANI1_MACMU | ACE | 452 |
Keywords
- Technical term