| IED ID | IndEnz0002014499 |
| Enzyme Type ID | protease014499 |
| 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 | Mesocricetus auratus (Golden hamster) |
| 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) Rodentia Myomorpha (mice and others) Muroidea Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
| Enzyme Sequence | MGAASGQRGQGPPSPLLLLWLSLLLLLLPPSPAPALDPGLQPGNFSADEIGAHLFAESYNSSAEQVIFQSTVASWAYDTNMTEENARLQEEAELIWQEFAEVWGKKAKELFDAIRQNFTDSKLRRVIETIRTLGPANLPLARRQQYNSLQNNMNRIYSTSKVCLPNKTATCWSLEPELTNILASSRSYAKLLFAWESWHDVVGIPLKPLYQDFTALSNEAYKQDGFSDTGAYWRSAYDSPSFEETLEHLYHQLEPLYLNLHAYVRRALHRRYGDKYINLRGPIPAHLLGDMWAQSWDNIYDMVVPFPNKPNLDVTNTMVQKGWNVTHMFRVAEEFFTSMGLSPMPPEFWAESMLEKPTDGREVVCHASAWDFFNRKDFRIKQCTRITMEQLSTVHHEMGHVQYYLQYKDLTVPLRRGANPGFHEAIGDVLALSVSTPAHLHKIGLLDRVANDLESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGHTPPSRYNFDWWYFRTKYQGICPPVVRNETHFDAGAKFHIPSGTPYIRYFVSFILQFQFHQALCKEAGHQGPLHQCDIYQSTQAGAKLQRVLQAGYSRPWQEVLKEMVGSDTLDAQALLEYFQPVIRWLQEQNQRNGEVLGWPEYQWRPPLPDNYPEGIDLVTDETEAERFVEEYDRTARVLWNEYAEANWQYNTNITLEASKILLQKNKKVANHTLKYGTLAKKFDVSNFQNYTIKRIIKKVQNMDRAVLPPKELEEYNQILMDMETTYSIANVCYLNGTCLHLEPDLTNVMATSRKYEELLWVWKSWRDKVGRAILPLFPKYVELSNKIAHLNGYADGGDSWRSSYESKSLEQDLEQLYQELQPLYLNLHAYVRRSLHRHYGSQHINLDGPIPAHLLGNMWAQTWSNIYDLVAPFPSAPNLDATEAMIKQGWTPRRIFKEADDFFTSLGLLPVSEEFWNKSMLEKPGDGREVVCHASAWDFYNGKDFRIKQCTSVNMEDLVIAHHEMGHIQYFMQYKDLPVTFREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGGYEHDINFLMKMALDKIAFIPFSYLIDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRSQDDFDPGSKFHVPANVPYIRYFVSFIIQFQFHEALCRAAGHTGPLHKCDIYQSKEAGKLLADTMKMGYSKPWPEAMKLITGQPNMSASAMMNYFKPLTEWLVTENRRHGETLGWPEYNWTPNTARSEGPFPESGRVNFLGMYLEPQQARVGQWVLLFLGVSLLVATLGLTHRLFSIRQHGHSLHRPHRGPQFGSEVELRHS |
| Enzyme Length | 1314 |
| Uniprot Accession Number | Q50JE5 |
| Absorption | |
| Active Site | ACT_SITE 397; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 995; /note=2; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 237; /note=Chloride 1; /evidence=ECO:0000250; BINDING 535; /note=Chloride 1; /evidence=ECO:0000250; BINDING 797; /note=Chloride 2; /evidence=ECO:0000250; BINDING 835; /note=Chloride 3; /evidence=ECO:0000250; BINDING 1096; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1100; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1133; /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. This GPIase activity seems to be crucial for the egg-binding ability of the sperm (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (2); Disulfide bond (4); Glycosylation (13); Metal binding (6); Modified residue (1); Propeptide (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Cell membrane;Cytoplasm;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 1307; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P12821 |
| Post Translational Modification | PTM: Phosphorylated by CK2 on Ser-1307; which allows membrane retention. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..35; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 151,595 |
| Kinetics | |
| Metal Binding | METAL 396; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 400; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 424; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 994; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 998; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 1022; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.15.1; |