Angiotensin-converting enzyme
Details
- Name
- Angiotensin-converting enzyme
- Kind
- protein
- Synonyms
- 3.4.15.1
- ACE
- DCP
- DCP1
- Dipeptidyl carboxypeptidase I
- Kininase II
- Gene Name
- ACE
- UniProtKB Entry
- P12821Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0000441|Angiotensin-converting enzyme MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQV LFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRI IGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSR SYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDL EHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPF PDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCH ASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAI GDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFS GRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQF HEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLL KYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTS QVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRI IKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKY EDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLER LFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPS APSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHAS AWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGD VLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGS ITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHE ALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSY FKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQW LLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
- Number of residues
- 1306
- Molecular Weight
- 149713.675
- Theoretical pI
- 6.36
- GO Classification
- Functionscalmodulin binding / heterocyclic compound binding / metallodipeptidase activity / metalloendopeptidase activity / peptidase activityProcessesamyloid-beta metabolic process / angiogenesis involved in coronary vascular morphogenesis / angiotensin-activated signaling pathway / animal organ regeneration / blood vessel diameter maintenance / bradykinin catabolic process / cellular response to aldosterone / cellular response to glucose stimulus / eating behavior / embryo development ending in birth or egg hatching / female pregnancy / hormone metabolic process / lung alveolus development / male gonad development / negative regulation of calcium ion import / negative regulation of gene expression / negative regulation of glucose import / positive regulation of apoptotic process / positive regulation of neurogenesis / positive regulation of systemic arterial blood pressure / positive regulation of vasoconstriction / post-transcriptional regulation of gene expression / proteolysis / regulation of heart rate by cardiac conduction / regulation of synaptic plasticity / response to dexamethasone / response to hypoxia / response to laminar fluid shear stress / response to lipopolysaccharide / response to nutrient levels / response to thyroid hormone / response to xenobiotic stimulus / substance P catabolic process / vasoconstrictionComponentsbasal plasma membrane / brush border membrane / sperm midpiece
- General Function
- Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubMed:2558109, PubMed:4322742, PubMed:7523412, PubMed:7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:10913258, PubMed:1320019, PubMed:1851160, PubMed:19773553, PubMed:7683654, PubMed:7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:11432860, PubMed:1851160, PubMed:19773553, PubMed:23056909, PubMed:4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:15615692, PubMed:2558109, PubMed:4322742, PubMed:6055465, PubMed:6270633, PubMed:7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed:15615692, PubMed:6208535, PubMed:6270633, PubMed:656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed:2982830, PubMed:6270633, PubMed:656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed:26403559, PubMed:7876104, PubMed:8257427, PubMed:8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed:11604391, PubMed:16154999, PubMed:19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:10336644, PubMed:2983326, PubMed:7683654, PubMed:9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed:10336644, PubMed:19773553, PubMed:7876104)
- Specific Function
- actin binding
- Pfam Domain Function
- Peptidase_M2 (PF01401)
- Signal Regions
- 1-29
- Transmembrane Regions
- 1257-1277
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0018929|Angiotensin-converting enzyme (ACE) ATGGGGGCCGCCTCGGGCCGCCGGGGGCCGGGGCTGCTGCTGCCGCTGCCGCTGCTGTTG CTGCTGCCGCCGCAGCCCGCCCTGGCGTTGGACCCCGGGCTGCAGCCCGGCAACTTTTCT GCTGACGAGGCCGGGGCGCAGCTCTTCGCGCAGAGCTACAACTCCAGCGCCGAACAGGTG CTGTTCCAGAGCGTGGCCGCCAGCTGGGCGCACGACACCAACATCACCGCGGAGAATGCA AGGCGCCAGGAGGAAGCAGCCCTGCTCAGCCAGGAGTTTGCGGAGGCCTGGGGCCAGAAG GCCAAGGAGCTGTATGAACCGATCTGGCAGAACTTCACGGACCCGCAGCTGCGCAGGATC ATCGGAGCTGTGCGCACCCTGGGCTCTGCCAACCTGCCCCTGGCTAAGCGGCAGCAGTAC AACGCCCTGCTAAGCAACATGAGCAGGATCTACTCCACCGCCAAGGTCTGCCTCCCCAAC AAGACTGCCACCTGCTGGTCCCTGGACCCAGATCTCACCAACATCCTGGCTTCCTCGCGA AGCTACGCCATGCTCCTGTTTGCCTGGGAGGGCTGGCACAACGCTGCGGGCATCCCGCTG AAACCGCTGTACGAGGATTTCACTGCCCTCAGCAATGAAGCCTACAAGCAGGACGGCTTC ACAGACACGGGGGCCTACTGGCGCTCCTGGTACAACTCCCCCACCTTCGAGGACGATCTG GAACACCTCTACCAACAGCTAGAGCCCCTCTACCTGAACCTCCATGCCTTCGTCCGCCGC GCACTGCATCGCCGATACGGAGACAGATACATCAACCTCAGGGGACCCATCCCTGCTCAT CTGCTGGGAGACATGTGGGCCCAGAGCTGGGAAAACATCTACGACATGGTGGTGCCTTTC CCAGACAAGCCCAACCTCGATGTCACCAGTACTATGCTGCAGCAGGGCTGGAACGCCACG CACATGTTCCGGGTGGCAGAGGAGTTCTTCACCTCCCTGGAGCTCTCCCCCATGCCTCCC GAGTTCTGGGAAGGGTCGATGCTGGAGAAGCCGGCCGACGGGCGGGAAGTGGTGTGCCAC GCCTCGGCTTGGGACTTCTACAACAGGAAAGACTTCAGGATCAAGCAGTGCACACGGGTC ACGATGGACCAGCTCTCCACAGTGCACCATGAGATGGGCCATATACAGTACTACCTGCAG TACAAGGATCTGCCCGTCTCCCTGCGTCGGGGGGCCAACCCCGGCTTCCATGAGGCCATT GGGGACGTGCTGGCGCTCTCGGTCTCCACTCCTGAACATCTGCACAAAATCGGCCTGCTG GACCGTGTCACCAATGACACGGAAAGTGACATCAATTACTTGCTAAAAATGGCACTGGAA AAAATTGCCTTCCTGCCCTTTGGCTACTTGGTGGACCAGTGGCGCTGGGGGGTCTTTAGT GGGCGTACCCCCCCTTCCCGCTACAACTTCGACTGGTGGTATCTTCGAACCAAGTATCAG GGGATCTGTCCTCCTGTTACCCGAAACGAAACCCACTTTGATGCTGGAGCTAAGTTTCAT GTTCCAAATGTGACACCATACATCAGGTACTTTGTGAGTTTTGTCCTGCAGTTCCAGTTC CATGAAGCCCTGTGCAAGGAGGCAGGCTATGAGGGCCCACTGCACCAGTGTGACATCTAC CGGTCCACCAAGGCAGGGGCCAAGCTCCGGAAGGTGCTGCAGGCTGGCTCCTCCAGGCCC TGGCAGGAGGTGCTGAAGGACATGGTCGGCTTAGATGCCCTGGATGCCCAGCCGCTGCTC AAGTACTTCCAGCCAGTCACCCAGTGGCTGCAGGAGCAGAACCAGCAGAACGGCGAGGTC CTGGGCTGGCCCGAGTACCAGTGGCACCCGCCGTTGCCTGACAACTACCCGGAGGGCATA GACCTGGTGACTGATGAGGCTGAGGCCAGCAAGTTTGTGGAGGAATATGACCGGACATCC CAGGTGGTGTGGAACGAGTATGCCGAGGCCAACTGGAACTACAACACCAACATCACCACA GAGACCAGCAAGATTCTGCTGCAGAAGAACATGCAAATAGCCAACCACACCCTGAAGTAC GGCACCCAGGCCAGGAAGTTTGATGTGAACCAGTTGCAGAACACCACTATCAAGCGGATC ATAAAGAAGGTTCAGGACCTAGAACGGGCAGCACTGCCTGCCCAGGAGCTGGAGGAGTAC AACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCCACTGTGTGCCACCCGAAT GGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATGGCCACGTCCCGGAAATAT GAAGACCTGTTATGGGCATGGGAGGGCTGGCGAGACAAGGCGGGGAGAGCCATCCTCCAG TTTTACCCGAAATACGTGGAACTCATCAACCAGGCTGCCCGGCTCAATGGCTATGTAGAT GCAGGGGACTCGTGGAGGTCTATGTACGAGACACCATCCCTGGAGCAAGACCTGGAGCGG CTCTTCCAGGAGCTGCAGCCACTCTACCTCAACCTGCATGCCTACGTGCGCCGGGCCCTG CACCGTCACTACGGGGCCCAGCACATCAACCTGGAGGGGCCCATTCCTGCTCACCTGCTG GGGAACATGTGGGCGCAGACCTGGTCCAACATCTATGACTTGGTGGTGCCCTTCCCTTCA GCCCCCTCGATGGACACCACAGAGGCTATGCTAAAGCAGGGCTGGACGCCCAGGAGGATG TTTAAGGAGGCTGATGATTTCTTCACCTCCCTGGGGCTGCTGCCCGTGCCTCCTGAGTTC TGGAACAAGTCGATGCTGGAGAAGCCAACCGACGGGCGGGAGGTGGTCTGCCACGCCTCG GCCTGGGACTTCTACAACGGCAAGGACTTCCGGATCAAGCAGTGCACCACCGTGAACTTG GAGGACCTGGTGGTGGCCCACCACGAAATGGGCCACATCCAGTATTTCATGCAGTACAAA GACTTACCTGTGGCCTTGAGGGAGGGTGCCAACCCCGGCTTCCATGAGGCCATTGGGGAC GTGCTAGCCCTCTCAGTGTCTACGCCCAAGCACCTGCACAGTCTCAACCTGCTGAGCAGT GAGGGTGGCAGCGACGAGCATGACATCAACTTTCTGATGAAGATGGCCCTTGACAAGATC GCCTTTATCCCCTTCAGCTACCTCGTCGATCAGTGGCGCTGGAGGGTATTTGATGGAAGC ATCACCAAGGAGAACTATAACCAGGAGTGGTGGAGCCTCAGGCTGAAGTACCAGGGCCTC TGCCCCCCAGTGCCCAGGACTCAAGGTGACTTTGACCCAGGGGCCAAGTTCCACATTCCT TCTAGCGTGCCTTACATCAGGTACTTTGTCAGCTTCATCATCCAGTTCCAGTTCCACGAG GCACTGTGCCAGGCAGCTGGCCACACGGGCCCCCTGCACAAGTGTGACATCTACCAGTCC AAGGAGGCCGGGCAGCGCCTGGCGACCGCCATGAAGCTGGGCTTCAGTAGGCCGTGGCCG GAAGCCATGCAGCTGATCACGGGCCAGCCCAACATGAGCGCCTCGGCCATGTTGAGCTAC TTCAAGCCGCTGCTGGACTGGCTCCGCACGGAGAACGAGCTGCATGGGGAGAAGCTGGGC TGGCCGCAGTACAACTGGACGCCGAACTCCGCTCGCTCAGAAGGGCCCCTCCCAGACAGC GGCCGCGTCAGCTTCCTGGGCCTGGACCTGGATGCGCAGCAGGCCCGCGTGGGCCAGTGG CTGCTGCTCTTCCTGGGCATCGCCCTGCTGGTAGCCACCCTGGGCCTCAGCCAGCGGCTC TTCAGCATCCGCCACCGCAGCCTCCACCGGCACTCCCACGGGCCCCAGTTCGGCTCCGAG GTGGAGCTGAGACACTCCTGA
- Chromosome Location
- 17
- Locus
- 17q23.3
- External Identifiers
Resource Link UniProtKB ID P12821 UniProtKB Entry Name ACE_HUMAN GenBank Protein ID 178286 GenBank Gene ID J04144 GeneCard ID ACE GenAtlas ID ACE HGNC ID HGNC:2707 PDB ID(s) 1O86, 1O8A, 1UZE, 1UZF, 2C6F, 2C6N, 2IUL, 2IUX, 2OC2, 2XY9, 2XYD, 2YDM, 3BKK, 3BKL, 3L3N, 3NXQ, 4APH, 4APJ, 4BXK, 4BZR, 4BZS, 4C2N, 4C2O, 4C2P, 4C2Q, 4C2R, 4CA5, 4CA6, 4UFA, 4UFB, 5AM8, 5AM9, 5AMA, 5AMB, 5AMC, 6EN5, 6EN6, 6F9R, 6F9T, 6F9U, 6F9V, 6H5W, 6H5X, 6QS1, 6TT1, 6TT3, 6TT4, 6ZPQ, 6ZPT, 6ZPU, 7Q24, 7Q25, 7Q26, 7Q27, 7Q28, 7Q29, 7Q3Y, 7Q49, 7Q4C, 7Q4D, 7Q4E, 7Z6Z, 7Z70, 8QFX, 8QHL KEGG ID hsa:1636 IUPHAR/Guide To Pharmacology ID 1613 NCBI Gene ID 1636 - General References
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Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Perindopril approved yes target inhibitor Details Rescinnamine approved yes target inhibitor Details Epicaptopril experimental unknown target Details N-acetyl-alpha-D-glucosamine experimental yes target inhibitor Details Fosinopril approved yes target inhibitor Details Benazepril approved, investigational yes target inhibitor Details Captopril approved yes target inhibitor Details Enalapril approved, vet_approved yes target inhibitor Details Lisinopril approved, investigational yes target inhibitor Details Moexipril approved yes target inhibitor Details Quinapril approved, investigational yes target inhibitor Details Ramipril approved yes target inhibitor Details Trandolapril approved yes target inhibitor Details Omapatrilat investigational yes target modulator Details Spirapril approved yes target inhibitor Details Cilazapril approved yes target inhibitor Details Candoxatril experimental unknown target inhibitor Details Temocapril experimental, investigational unknown target inhibitor Details Enalaprilat approved yes target inhibitor Details Zofenopril approved yes target inhibitor Details Cilazaprilat experimental yes target Details Acetate experimental yes target inhibitor Details beta-D-Ribopyranose experimental yes target inhibitor Details Moexiprilat experimental yes target modulator Details Ilepatril investigational yes target modulator Details Gallopamil investigational yes target inhibitor Details Isoquercetin investigational yes target inhibitor Details Deserpidine approved yes target inhibitor Details Imidapril investigational yes target modulator Details Delapril investigational yes target modulator Details Hydrochlorothiazide approved, vet_approved yes target modulator Details