Detail Information for IndEnz0002018553
IED ID IndEnz0002018553
Enzyme Type ID protease018553
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 Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MGAASGQRGRWPLSPPLLMLSLLLLLLLPPSPAPALDPGLQPGNFSADEAGAQLFADSYNSSAEVVMFQSTAASWAHDTNITEENARLQEEAALINQEFAEVWGKKAKELYESIWQNFTDQKLRRIIGSVQTLGPANLPLTQRLQYNSLLSNMSRIYSTGKVCFPNKTATCWSLDPELTNILASSRNYAKVLFAWEGWHDAVGIPLRPLYQDFTALSNEAYRQDGFSDTGAYWRSWYESPSFEESLEHLYHQVEPLYLNLHAFVRRALHRRYGDKYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMVQKGWNATHMFRVAEEFFTSLGLSPMPPEFWAESMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHVQYYLQYKDLHVSLRRGANPGFHEAIGDVLALSVSTPAHLHKIGLLDRVANDIESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNYDWWYLRTKYQGICPPVARNETHFDAGAKFHIPSVTPYIRYFVSFVLQFQFHQALCKEAGHQGPLHQCDIYQSTKAGAKLQQVLQAGCSRPWQEVLKDLVGSDALDASALMEYFQPVSQWLQEQNQRNGEVLGWPEYQWRPPLPDNYPEGIDLETDEAKANRFVEEYDRTAKVLWNEYAEANWHYNTNITIEGSKILLQKNKEVSNHTLKYGTWAKTFDVSNFQNSTIKRIIKKVQNVDRAVLPPNELEEYNQILLDMETTYSVANVCYTNGTCLSLEPDLTNIMATSRKYEELLWVWKSWRDKVGRAILPFFPKYVDFSNKIAKLNGYSDAGDSWRSSYESDDLEQDLEKLYQELQPLYLNLHAYVRRSLHRHYGSEYINLDGPIPAHLLGNMWAQTWSNIYDLVAPFPSAPSIDATEAMIKQGWTPRRIFKEADNFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTSVNMEELVIAHHEMGHIQYFMQYKDLPVTFREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGSGYEHDINFLMKMALDKIAFIPFSYLIDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRSQGDFDPGSKFHVPANVPYIRYFISFIIQFQFHEALCRAAGHTGPLYKCDIYQSKEAGKLLADAMKLGYSKQWPEAMKIITGQPNMSASAIMNYFKPLTEWLVTENRRHGETLGWPEYTWTPNTARAEGSLPESSRVNFLGMYLEPQQARVGQWVLLFLGVALLVATVGLAHRLYNIHNHHSLRRPHRGPQFGSEVELRHS
Enzyme Length 1313
Uniprot Accession Number P47820
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); Alternative sequence (2); Binding site (7); Chain (2); Glycosylation (14); Metal binding (6); Modified residue (1); Natural variant (1); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Carboxypeptidase;Cell membrane;Cytoplasm;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction INDUCTION: Up-regulated after myocardial infarction. {ECO:0000269|PubMed:15671045}.
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 1306; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903
Post Translational Modification PTM: Phosphorylated by CK2 on Ser-1306; which allows membrane retention. {ECO:0000250}.
Signal Peptide SIGNAL 1..35; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10072897; 10506486; 10580398; 10642323; 10644663; 10844603; 11299220; 11447075; 12131554; 12444051; 14527966; 14586729; 14757777; 15001561; 15770604; 15894569; 15942045; 16148611; 16203874; 16229862; 1659346; 16822509; 16902320; 17097496; 17161436; 17392119; 1750504; 17506716; 17506718; 17626897; 1784836; 17977916; 18223026; 18389998; 18419956; 18555989; 18679036; 19080340; 19114890; 19164508; 19301230; 19307186; 19361967; 19389807; 19424597; 19590507; 19620082; 20122169; 20204775; 20213806; 20229187; 20304959; 20400910; 20436217; 20465954; 20581171; 20630208; 20798958; 21667191; 21680852; 21718676; 2172462; 2175683; 21791939; 21864581; 21901125; 21975128; 22100841; 22123369; 22342460; 22441330; 22587910; 22595130; 22768235; 23663763; 23803175; 23959549; 24035938; 24036592; 24184594; 24342267; 24471927; 24502693; 24583339; 24602481; 24709159; 24775918; 24847689; 24959250; 25143335; 25663023; 27147779; 2827504; 2841539; 28822808; 29335866; 2966592; 3006710; 3021286; 3028670; 3031366; 30458228; 31385307; 3392211; 7585810; 7620708; 7977726; 8303709; 8386093; 8445218; 8505110; 8665777; 8995730; 9048650; 9344638; 9484988; 9495881; 9498404;
Motif
Gene Encoded By
Mass 150,908
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;