A0A7I2V4H0 · A0A7I2V4H0_HUMAN
- ProteinAngiotensin-converting enzyme
- GeneACE2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids786 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Catalytic activity
- angiotensin I + H2O = angiotensin-(1-9) + L-leucineThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 zinc ion per subunit.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 375 | Proton acceptor 1 | ||||
Sequence: E | ||||||
Active site | 375 | Proton acceptor 2 | ||||
Sequence: E | ||||||
Active site | 505 | Proton donor 1 | ||||
Sequence: H | ||||||
Active site | 505 | Proton donor 2 | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | cilium | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
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
Names & Taxonomy
Protein names
- Recommended nameAngiotensin-converting enzyme
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A7I2V4H0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 739-762 | Helical | ||||
Sequence: VSIWLIVFGVVMGVIVVGIVILIF |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 442 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-17 | UniProt | |||||
Sequence: MSSSSWLLLSLVAVTAA | |||||||
Chain | PRO_5029780446 | 18-786 | UniProt | Angiotensin-converting enzyme | |||
Sequence: QSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKPTPLLGKSWLTAILKD | |||||||
Glycosylation | 53 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 90 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 90 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 133↔141 | UniProt | |||||
Sequence: CNPDNPQEC | |||||||
Disulfide bond | 344↔361 | UniProt | |||||
Sequence: CHPTAWDLGKGDFRILMC | |||||||
Modified residue (large scale data) | 425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 530↔542 | UniProt | |||||
Sequence: CQAAKHEGPLHKC | |||||||
Glycosylation | 578 | UniProt | N-linked (GlcNAc...) asparagine; partial | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 614-786 | Collectrin-like | ||||
Sequence: ADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKPTPLLGKSWLTAILKD |
Sequence similarities
Belongs to the peptidase M2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length786
- Mass (Da)90,386
- Last updated2021-04-07 v1
- ChecksumD2FB49B6FBFBB959
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q9BYF1 | ACE2_HUMAN | ACE2 | 805 | ||
A0A7I2V2E9 | A0A7I2V2E9_HUMAN | ACE2 | 771 | ||
A0A7I2V3N4 | A0A7I2V3N4_HUMAN | ACE2 | 772 | ||
A0A7I2V3X6 | A0A7I2V3X6_HUMAN | ACE2 | 786 | ||
A0A7I2V5W5 | A0A7I2V5W5_HUMAN | ACE2 | 112 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC097625 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |