| IED ID | IndEnz0002016530 |
| Enzyme Type ID | protease016530 |
| Protein Name |
Angiotensin-converting enzyme ACE EC 3.2.1.- EC 3.4.15.1 Dipeptidyl carboxypeptidase I Kininase II CD antigen CD143 Cleaved into: Angiotensin-converting enzyme, soluble form |
| Gene Name | ACE DCP1 |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MGAAPGRRGPRLLRPPPPLLLLLLLLRPPPAALTLDPGLLPGDFAADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPEDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQPVSLRRANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPSSRYNFDWWYLRTKYQGICPPVVRNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCMEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWLQEQNERNGEVLGWPEYQWRPPLPNNYPEGIDLVTDEAEASRFVEEYDRSFQAVWNEYAEANWNYNTNITTEASKILLQKNMQIANHTLTYGNWARRFDVSNFQNATSKRIIKKVQDLQRAVLPVKELEEYNQILLDMETIYSVANVCRVDGSCLQLEPDLTNLMATSRKYDELLWVWTSWRDKVGRAILPYFPKYVEFTNKAARLNGYVDAGDSWRSMYETPTLEQDLERLFQELQPLYLNLHAYVGRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVAPFPSASTMDATEAMIKQGWTPRRMFEEADKFFISLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNMEDLVVVHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSINLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLVDEWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPAPRSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCKAAGHTGPLHTCDIYQSKEAGKRLADAMKLGYSKPWPEAMKVITGQPNMSASAMMNYFKPLMDWLLTENGRHGEKLGWPQYTWTPNSARSEGSLPDSGRVNFLGMNLDAQQARVGQWVLLFLGVALLLASLGLTQRLFSIRYQSLRQPHHGPQFGSEVELRHS |
| Enzyme Length | 1310 |
| Uniprot Accession Number | P12822 |
| Absorption | |
| Active Site | ACT_SITE 396; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 993; /note=2; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Strongly activated by chloride. Specifically inhibited by lisinopril. {ECO:0000269|PubMed:7902354}. |
| Binding Site | BINDING 236; /note=Chloride 1; /evidence=ECO:0000250; BINDING 533; /note=Chloride 1; /evidence=ECO:0000250; BINDING 795; /note=Chloride 2; /evidence=ECO:0000250; BINDING 833; /note=Chloride 3; /evidence=ECO:0000250; BINDING 1094; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1098; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1131; /note=Chloride 3; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; |
| DNA Binding | |
| EC Number | 3.2.1.-; 3.4.15.1 |
| Enzyme Function | FUNCTION: Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Binding site (7); Chain (2); Disulfide bond (4); Glycosylation (11); Metal binding (6); Modified residue (1); Mutagenesis (2); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Cell membrane;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250}. |
| Modified Residue | MOD_RES 1303; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P12821 |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:1654880}.; PTM: Phosphorylated by CK2 on Ser-1303; which allows membrane retention. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..33; /evidence="ECO:0000269|PubMed:1654880, ECO:0000269|PubMed:6291514, ECO:0000269|PubMed:6314908" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 150,406 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for Hip-His-Leu {ECO:0000269|PubMed:7902354}; KM=0.09 mM for angiotensin I {ECO:0000269|PubMed:7902354}; |
| Metal Binding | METAL 395; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 399; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 422; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 992; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 996; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 1020; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.15.1; |