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Showing Protein Angiotensin-converting enzyme (HMDBP01710)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 18 metabolites
Identification
HMDB Protein ID HMDBP01710
Secondary Accession Numbers
  • 7050
Name Angiotensin-converting enzyme
Synonyms
  1. ACE
  2. Angiotensin-converting enzyme, soluble form
  3. CD143 antigen
  4. Dipeptidyl carboxypeptidase I
  5. Kininase II
Gene Name ACE
Protein Type Unknown
Biological Properties
General Function Involved in metallopeptidase activity
Specific 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
Pathways
  • Angiotensin Metabolism
  • Benazepril Action Pathway
  • Benazepril Metabolism Pathway
  • Candesartan Action Pathway
  • Captopril Action Pathway
  • Cilazapril Action Pathway
  • Cilazapril Metabolism Pathway
  • Enalapril Action Pathway
  • Enalapril Metabolism Pathway
  • Eprosartan Action Pathway
  • Forasartan Action Pathway
  • Fosinopril Action Pathway
  • Fosinopril Metabolism Pathway
  • Irbesartan Action Pathway
  • Lisinopril Action Pathway
  • Losartan Action Pathway
  • Moexipril Action Pathway
  • Moexipril Metabolism Pathway
  • Olmesartan Action Pathway
  • Perindopril Action Pathway
  • Quinapril Action Pathway
  • Quinapril Metabolism Pathway
  • Ramipril Action Pathway
  • Ramipril Metabolism Pathway
  • Rescinnamine Action Pathway
  • Spirapril Action Pathway
  • Spirapril Metabolism Pathway
  • Telmisartan Action Pathway
  • Temocapril Action Pathway
  • Temocapril Metabolism Pathway
  • Trandolapril Action Pathway
  • Trandolapril Metabolism Pathway
  • Valsartan Action Pathway
Reactions Not Available
GO Classification
Component
membrane
cell part
Function
exopeptidase activity
catalytic activity
hydrolase activity
peptidyl-dipeptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Cell membrane
  2. Single-pass type I membrane protein
Gene Properties
Chromosome Location Chromosome:1
Locus 17q23.3
SNPs ACE
Gene Sequence 
>3921 bp
ATGGGGGCCGCCTCGGGCCGCCGGGGGCCGGGGCTGCTGCTGCCGCTGCCGCTGCTGTTG
CTGCTGCCGCCGCAGCCCGCCCTGGCGTTGGACCCCGGGCTGCAGCCCGGCAACTTTTCT
GCTGACGAGGCCGGGGCGCAGCTCTTCGCGCAGAGCTACAACTCCAGCGCCGAACAGGTG
CTGTTCCAGAGCGTGGCCGCCAGCTGGGCGCACGACACCAACATCACCGCGGAGAATGCA
AGGCGCCAGGAGGAAGCAGCCCTGCTCAGCCAGGAGTTTGCGGAGGCCTGGGGCCAGAAG
GCCAAGGAGCTGTATGAACCGATCTGGCAGAACTTCACGGACCCGCAGCTGCGCAGGATC
ATCGGAGCTGTGCGAACCCTGGGCTCTGCCAACCTGCCCCTGGCTAAGCGGCAGCAGTAC
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
ATAAAGAAGGTTCAGGACCTAGAACGGGCAGCGCTGCCTGCCCAGGAGCTGGAGGAGTAC
AACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCCACTGTGTGCCACCCGAAT
GGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATGGCCACATCCCGGAAATAT
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
Protein Properties
Number of Residues 1306
Molecular Weight 149713.7
Theoretical pI 6.36
Pfam Domain Function
Signals
  • 1-29
Transmembrane Regions
  • 1257-1277
Protein Sequence 
>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
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P12821
UniProtKB/Swiss-Prot Entry Name ACE_HUMAN
PDB IDs
GenBank Gene ID J04144
GeneCard ID ACE
GenAtlas ID ACE
HGNC ID HGNC:2707
References
General References
  1. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218 ]
  2. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  3. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
  4. Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed:15534175 ]
  5. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed:10391210 ]
  6. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G, Corvol P: Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A. 1988 Dec;85(24):9386-90. [PubMed:2849100 ]
  7. Lattion AL, Soubrier F, Allegrini J, Hubert C, Corvol P, Alhenc-Gelas F: The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 1989 Jul 31;252(1-2):99-104. [PubMed:2547653 ]
  8. Ehlers MR, Fox EA, Strydom DJ, Riordan JF: Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7741-5. [PubMed:2554286 ]
  9. Rieder MJ, Taylor SL, Clark AG, Nickerson DA: Sequence variation in the human angiotensin converting enzyme. Nat Genet. 1999 May;22(1):59-62. [PubMed:10319862 ]
  10. Takeuchi K, Shimizu T, Ohishi N, Seyama Y, Takaku F, Yotsumoto H: Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence. J Biochem. 1989 Sep;106(3):442-5. [PubMed:2558109 ]
  11. Sugimura K, Tian XL, Hoffmann S, Ganten D, Bader M: Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization. Biochem Biophys Res Commun. 1998 Jun 18;247(2):466-72. [PubMed:9642152 ]
  12. Ehlers MR, Riordan JF: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991 Jul 23;30(29):7118-26. [PubMed:1649623 ]
  13. Sturrock ED, Yu XC, Wu Z, Biemann K, Riordan JF: Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications. Biochemistry. 1996 Jul 23;35(29):9560-6. [PubMed:8755737 ]
  14. Yu XC, Sturrock ED, Wu Z, Biemann K, Ehlers MR, Riordan JF: Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form. J Biol Chem. 1997 Feb 7;272(6):3511-9. [PubMed:9013598 ]
  15. Woodman ZL, Oppong SY, Cook S, Hooper NM, Schwager SL, Brandt WF, Ehlers MR, Sturrock ED: Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites. Biochem J. 2000 May 1;347 Pt 3:711-8. [PubMed:10769174 ]
  16. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9. [PubMed:10969042 ]
  17. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000 Oct 27;275(43):33238-43. [PubMed:10924499 ]
  18. Eyries M, Michaud A, Deinum J, Agrapart M, Chomilier J, Kramers C, Soubrier F: Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region. J Biol Chem. 2001 Feb 23;276(8):5525-32. Epub 2000 Nov 13. [PubMed:11076943 ]
  19. Kohlstedt K, Shoghi F, Muller-Esterl W, Busse R, Fleming I: CK2 phosphorylates the angiotensin-converting enzyme and regulates its retention in the endothelial cell plasma membrane. Circ Res. 2002 Oct 18;91(8):749-56. [PubMed:12386153 ]
  20. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 2002 Dec 4;532(1-2):107-10. [PubMed:12459472 ]
  21. Gordon K, Redelinghuys P, Schwager SL, Ehlers MR, Papageorgiou AC, Natesh R, Acharya KR, Sturrock ED: Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme. Biochem J. 2003 Apr 15;371(Pt 2):437-42. [PubMed:12542396 ]
  22. Goulter AB, Goddard MJ, Allen JC, Clark KL: ACE2 gene expression is up-regulated in the human failing heart. BMC Med. 2004 May 19;2:19. [PubMed:15151696 ]
  23. Burrell LM, Risvanis J, Kubota E, Dean RG, MacDonald PS, Lu S, Tikellis C, Grant SL, Lew RA, Smith AI, Cooper ME, Johnston CI: Myocardial infarction increases ACE2 expression in rat and humans. Eur Heart J. 2005 Feb;26(4):369-75; discussion 322-4. Epub 2005 Jan 25. [PubMed:15671045 ]
  24. Natesh R, Schwager SL, Sturrock ED, Acharya KR: Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature. 2003 Jan 30;421(6922):551-4. Epub 2003 Jan 19. [PubMed:12540854 ]
  25. Natesh R, Schwager SL, Evans HR, Sturrock ED, Acharya KR: Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry. 2004 Jul 13;43(27):8718-24. [PubMed:15236580 ]
  26. Corradi HR, Schwager SL, Nchinda AT, Sturrock ED, Acharya KR: Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. J Mol Biol. 2006 Mar 31;357(3):964-74. Epub 2006 Jan 31. [PubMed:16476442 ]
  27. Vleming LJ, van der Pijl JW, Lemkes HH, Westendorp RG, Maassen JA, Daha MR, van Es LA, van Kooten C: The DD genotype of the ACE gene polymorphism is associated with progression of diabetic nephropathy to end stage renal failure in IDDM. Clin Nephrol. 1999 Mar;51(3):133-40. [PubMed:10099885 ]
  28. Kramers C, Danilov SM, Deinum J, Balyasnikova IV, Scharenborg N, Looman M, Boomsma F, de Keijzer MH, van Duijn C, Martin S, Soubrier F, Adema GJ: Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease. Circulation. 2001 Sep 11;104(11):1236-40. [PubMed:11551873 ]
  29. Linnebank M, Kesper K, Jeub M, Urbach H, Wullner U, Klockgether T, Schmidt S: Hereditary elevation of angiotensin converting enzyme suggesting neurosarcoidosis. Neurology. 2003 Dec 23;61(12):1819-20. [PubMed:14694062 ]
  30. Slowik A, Turaj W, Dziedzic T, Haefele A, Pera J, Malecki MT, Glodzik-Sobanska L, Szermer P, Figlewicz DA, Szczudlik A: DD genotype of ACE gene is a risk factor for intracerebral hemorrhage. Neurology. 2004 Jul 27;63(2):359-61. [PubMed:15277638 ]
  31. Gribouval O, Gonzales M, Neuhaus T, Aziza J, Bieth E, Laurent N, Bouton JM, Feuillet F, Makni S, Ben Amar H, Laube G, Delezoide AL, Bouvier R, Dijoud F, Ollagnon-Roman E, Roume J, Joubert M, Antignac C, Gubler MC: Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet. 2005 Sep;37(9):964-8. Epub 2005 Aug 14. [PubMed:16116425 ]