| IED ID | IndEnz0002014502 |
| Enzyme Type ID | protease014502 |
| 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 | Mus musculus (Mouse) |
| 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 Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGAASGQRGRWPLSPPLLMLSLLVLLLQPSPAPALDPGLQPGNFSPDEAGAQLFAESYNSSAEVVMFQSTVASWAHDTNITEENARRQEEAALVSQEFAEVWGKKAKELYESIWQNFTDSKLRRIIGSIRTLGPANLPLAQRQQYNSLLSNMSRIYSTGKVCFPNKTATCWSLDPELTNILASSRSYAKLLFAWEGWHDAVGIPLKPLYQDFTAISNEAYRQDDFSDTGAFWRSWYESPSFEESLEHIYHQLEPLYLNLHAYVRRALHRRYGDKYVNLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVSEEFFTSLGLSPMPPEFWAESMLEKPTDGREVVCHASAWDFYNRKDFRIKQCTRVTMEQLATVHHEMGHVQYYLQYKDLHVSLRRGANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDIESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVARNETHFDAGAKFHIPNVTPYIRYFVSFVLQFQFHQALCKEAGHQGPLHQCDIYQSAQAGAKLKQVLQAGCSRPWQEVLKDLVGSDALDAKALLEYFQPVSQWLEEQNQRNGEVLGWPENQWRPPLPDNYPEGIDLETDEAKADRFVEEYDRTAQVLLNEYAEANWQYNTNITIEGSKILLEKSTEVSNHTLKYGTRAKTFDVSNFQNSSIKRIIKKLQNLDRAVLPPKELEEYNQILLDMETTYSLSNICYTNGTCMPLEPDLTNMMATSRKYEELLWAWKSWRDKVGRAILPFFPKYVEFSNKIAKLNGYTDAGDSWRSLYESDNLEQDLEKLYQELQPLYLNLHAYVRRSLHRHYGSEYINLDGPIPAHLLGNMWAQTWSNIYDLVAPFPSAPNIDATEAMIKQGWTPRRIFKEADNFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHPSAWDFYNGKDFRIKQCTSVNMEDLVIAHHEMGHIQYFMQYKDLPVTFREGANPGFHEAIGDIMALSVSTPKHLYSLNLLSTEGSGYEYDINFLMKMALDKIAFIPFSYLIDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRSQGDFDPGSKFHVPANVPYVRYFVSFIIQFQFHEALCRAAGHTGPLHKCDIYQSKEAGKLLADAMKLGYSKPWPEAMKLITGQPNMSASAMMNYFKPLTEWLVTENRRHGETLGWPEYNWAPNTARAEGSTAESNRVNFLGLYLEPQQARVGQWVLLFLGVALLVATVGLAHRLYNIRNHHSLRRPHRGPQFGSEVELRHS |
| Enzyme Length | 1312 |
| Uniprot Accession Number | P09470 |
| Absorption | |
| Active Site | ACT_SITE 396; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 994; /note=2 |
| Activity Regulation | ACTIVITY REGULATION: Peptidase activity is specifically inhibited by lisinopril, captopril and enalaprilat. In contrast, GPIase activity is nearly insensitive to captopril. {ECO:0000269|PubMed:15665832}. |
| Binding Site | BINDING 236; /note=Chloride 1; /evidence=ECO:0000250; BINDING 534; /note=Chloride 1; /evidence=ECO:0000250; BINDING 796; /note=Chloride 2; /evidence=ECO:0000250; BINDING 834; /note=Chloride 3; /evidence=ECO:0000250; BINDING 1095; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1099; /note=Chloride 2; /evidence=ECO:0000250; BINDING 1132; /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. {ECO:0000269|PubMed:15665832, ECO:0000269|PubMed:7753170, ECO:0000269|PubMed:8642790}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Binding site (7); Chain (2); Disulfide bond (4); Glycosylation (13); Metal binding (6); Modified residue (1); Mutagenesis (3); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (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 | INDUCTION: Expression is thought to be subject to hormonal regulation by androgens. |
| Subcellular Location | SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237}; Single-pass type I membrane protein {ECO:0000269|PubMed:23535237}. Cytoplasm {ECO:0000269|PubMed:23535237}. Note=Detected in both cell membrane and cytoplasm in neurons. |
| Modified Residue | MOD_RES 1305; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | PTM: Phosphorylated by CK2 on Ser-1305; which allows membrane retention. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000269|PubMed:2835538 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10076178; 10187843; 10330057; 10405217; 10589702; 10720939; 10775573; 10831599; 11104792; 11217851; 11303049; 11687636; 11723129; 11786523; 11847186; 12003835; 12062093; 12075344; 12167603; 12204286; 12359984; 12372418; 12384478; 12444051; 12459519; 12466851; 12574101; 12620918; 12637363; 12646655; 12691672; 12777443; 1328889; 14525797; 14757757; 14769811; 14981053; 15031129; 15123520; 15151931; 15252021; 15331425; 15485659; 15494545; 15522949; 15569856; 15854741; 15947253; 16001071; 16141072; 16154999; 16215678; 16221869; 16270063; 16547111; 16585392; 16602821; 16804085; 16857898; 16870943; 16912050; 16926272; 17082641; 17135368; 17188239; 17307998; 17337599; 17525278; 17566078; 17634445; 17652370; 17656683; 17892857; 18032521; 18084722; 18158355; 18192335; 18212275; 18252713; 18263657; 18347228; 18356559; 18443281; 18483182; 18483625; 18554416; 19004932; 19075090; 19125280; 19258495; 19556720; 19673938; 19706421; 19710239; 19782130; 19846569; 19880118; 19930431; 20030584; 20116413; 20530543; 20614101; 20651228; 20667972; 20937811; 21115616; 21116821; 21148418; 21267068; 21386911; 2157425; 21622682; 21677750; 21964607; 22203735; 22580272; 22999937; 23055941; 23619363; 23633567; 23846498; 24194600; 24414175; 24475296; 24487585; 24501175; 24614194; 24800825; 24952961; 25012170; 25017399; 25249154; 25273883; 25924878; 26401072; 27055902; 27601681; 27879415; 27880904; 27988209; 28273875; 28390948; 28515091; 28665931; 28935757; 29101168; 29187372; 29549541; 29684311; 29750573; 29884907; 30088535; 30185469; 30670595; 31345929; 31455729; 31615657; 31794021; 31871049; 32238693; 32669323; 33480126; 33781839; 7671305; 8025157; 8391328; 8598926; 8952516; 9039095; 9153279; 9231832; 9316207; 9482924; 9664078; 9860346; 9876285; 9973259; |
| Motif | |
| Gene Encoded By | |
| Mass | 150,918 |
| Kinetics | |
| Metal Binding | METAL 395; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 399; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 423; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 993; /note=Zinc 2; catalytic; METAL 997; /note=Zinc 2; catalytic; METAL 1021; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.15.1; |