| IED ID | IndEnz0002002739 |
| Enzyme Type ID | protease002739 |
| Protein Name |
Angiotensin-converting enzyme 2 EC 3.4.17.23 ACE-related carboxypeptidase EC 3.4.17.- Cleaved into: Processed angiotensin-converting enzyme 2 |
| Gene Name | ACE2 |
| Organism | Paguma larvata (Masked palm civet) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Feliformia Viverridae (civets) Paradoxurinae Paguma Paguma larvata (Masked palm civet) |
| Enzyme Sequence | MSGSFWLLLSFAALTAAQSTTEELAKTFLETFNYEAQELSYQSSVASWNYNTNITDENAKNMNEAGAKWSAYYEEQSKLAQTYPLAEIQDAKIKRQLQALQQSGSSVLSADKSQRLNTILNAMSTIYSTGKACNPNNPQECLLLEPGLDNIMENSKDYNERLWAWEGWRAEVGKQLRPLYEEYVALKNEMARANNYEDYGDYWRGDYEEEWTGGYNYSRNQLIQDVEDTFEQIKPLYQHLHAYVRAKLMDTYPSRISRTGCLPAHLLGDMWGRFWTNLYPLTVPFGQKPNIDVTDAMVNQNWDARRIFKEAEKFFVSVGLPNMTQGFWENSMLTEPGDGRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPNHLKTIGLLSPAFSEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGAIPKEQWMQKWWEMKRNIVGVVEPVPHDETYCDPASLFHVANDYSFIRYYTRTIYQFQFQEALCQIAKHEGPLHKCDISNSTEAGKKLLEMLSLGRSEPWTLALERVVGAKNMNVTPLLNYFEPLFTWLKEQNRNSFVGWDTDWRPYSDQSIKVRISLKSALGEKAYEWNDNEMYLFRSSIAYAMREYFSKVKNQTIPFVEDNVWVSDLKPRISFNFFVTFSNNVSDVIPRSEVEDAIRMSRSRINDAFRLDDNSLEFLGIEPTLSPPYRPPVTIWLIVFGVVMGAIVVGIVLLIVSGIRNRRKNDQAGSEENPYASVDLNKGENNPGFQHADDVQTSF |
| Enzyme Length | 805 |
| Uniprot Accession Number | Q56NL1 |
| Absorption | |
| Active Site | ACT_SITE 375; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q9BYF1; ACT_SITE 505; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q9BYF1 |
| Activity Regulation | |
| Binding Site | BINDING 169; /note=Chloride; /evidence=ECO:0000269|PubMed:22291007; BINDING 273; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9BYF1; BINDING 477; /note=Chloride; /evidence=ECO:0000269|PubMed:22291007; BINDING 481; /note=Chloride; /evidence=ECO:0000250|UniProtKB:Q9BYF1; BINDING 515; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9BYF1 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine; Xref=Rhea:RHEA:26554, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:58506, ChEBI:CHEBI:58922; EC=3.4.17.23; Evidence={ECO:0000250|UniProtKB:Q9BYF1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26555; Evidence={ECO:0000250|UniProtKB:Q9BYF1}; CATALYTIC ACTIVITY: Reaction=angiotensin I + H2O = angiotensin-(1-9) + L-leucine; Xref=Rhea:RHEA:63532, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427, ChEBI:CHEBI:147350, ChEBI:CHEBI:147351; Evidence={ECO:0000250|UniProtKB:Q9BYF1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63533; Evidence={ECO:0000250|UniProtKB:Q9BYF1}; |
| DNA Binding | |
| EC Number | 3.4.17.23; 3.4.17.- |
| Enzyme Function | FUNCTION: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity. {ECO:0000250|UniProtKB:Q9BYF1}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronavirus SARS. {ECO:0000269|PubMed:15791205}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (2); Compositional bias (1); Disulfide bond (3); Glycosylation (6); Helix (1); Metal binding (3); Modified residue (2); Motif (5); Region (8); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Carboxypeptidase;Cell membrane;Cell projection;Chloride;Cytoplasm;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | P59594 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Processed angiotensin-converting enzyme 2]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BYF1}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R0I0}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:Q8R0I0}. |
| Modified Residue | MOD_RES 781; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q9BYF1; MOD_RES 783; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9BYF1 |
| Post Translational Modification | PTM: Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By similarity). {ECO:0000250}.; PTM: Phosphorylated. Phosphorylation at Tyr-781 probably inhibits interaction with AP2M1 and enables interactions with proteins containing SH2 domains. {ECO:0000250|UniProtKB:Q9BYF1}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3D0G; 3D0H; 3D0I; 3SCK; 3SCL; |
| Mapped Pubmed ID | 18448527; |
| Motif | MOTIF 778..786; /note=LIR; /evidence=ECO:0000250|UniProtKB:Q9BYF1; MOTIF 781..785; /note=SH2-binding; /evidence=ECO:0000250|UniProtKB:Q9BYF1; MOTIF 781..784; /note=Endocytic sorting signal; /evidence=ECO:0000250|UniProtKB:Q9BYF1; MOTIF 792..795; /note=PTB; /evidence=ECO:0000250|UniProtKB:Q9BYF1; MOTIF 803..805; /note=PDZ-binding; /evidence=ECO:0000250|UniProtKB:Q9BYF1 |
| Gene Encoded By | |
| Mass | 92,611 |
| Kinetics | |
| Metal Binding | METAL 374; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22291007; METAL 378; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22291007; METAL 402; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:22291007 |
| Rhea ID | RHEA:26554; RHEA:26555; RHEA:63532; RHEA:63533 |
| Cross Reference Brenda | 3.4.17.23; |