Angiotensin-converting enzyme 2

Angiotensin I converting enzyme 2

PDB rendering based on 1r42.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1R42, 1R4L, 1XJP, 2AJF, 3D0G, 3D0H, 3D0I, 3KBH, 3SCI, 3SCJ, 3SCK, 3SCL

Identifiers

Symbols

ACE2 ; ACEH

External IDs

OMIM: 300335 MGI: 1917258 HomoloGene: 41448 IUPHAR: 1614 ChEMBL: 3736 GeneCards: ACE2 Gene

EC number

3.4.17.23

Gene ontology
Molecular function	• virus receptor activity • glycoprotein binding • endopeptidase activity • carboxypeptidase activity • protein binding • metallopeptidase activity • peptidyl-dipeptidase activity • zinc ion binding • peptide hormone binding
Cellular component	• extracellular region • extracellular space • plasma membrane • cell surface • integral component of membrane • membrane raft • extracellular vesicular exosome
Biological process	• regulation of cytokine production • angiotensin maturation • angiotensin catabolic process in blood • angiotensin-mediated drinking behavior • regulation of systemic arterial blood pressure by renin-angiotensin • proteolysis • response to virus • regulation of vasoconstriction • receptor biosynthetic process • regulation of cell proliferation • regulation of vasodilation • cellular protein metabolic process • viral entry into host cell • receptor-mediated virion attachment to host cell • regulation of inflammatory response • positive regulation of reactive oxygen species metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
15.58 – 15.62 Mb

Chr X:
164.14 – 164.19 Mb

PubMed search

AngiotensinI-converting enzyme 2 (ACE 2) is an exopeptidase that catalyses the conversion of angiotensin I to the nonapeptide angiotensin[1-9],^[1] or the conversion of angiotensin II to angiotensin 1-7.^[2] ACE 2 has direct effects on cardiac function^a, and is expressed predominantly in vascular endothelial cells of the heart and the kidneys.^[3]

ACE 2 is the receptor for SARS virus.^[4]

References

↑ Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S (2000). "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9". Circ. Res. 87 (5): E1–9. PMID 10969042.
↑ Keidar S, Kaplan M, Gamliel-Lazarovich A (2007). [_ http://cardiovascres.oxfordjournals.org/cgi/content/full/73/3/463 "ACE2 of the heart: From angiotensin I to angiotensin (1-7)"]. Cardiovasc Res. 73 (3): 463–9. doi:10.1016/j.cardiores.2006.09.006. PMID 17049503.
↑ Boehm M, Nabel EG (2002). "Angiotensin-converting enzyme 2--a new cardiac regulator". N. Engl. J. Med. 347 (22): 1795–7. doi:10.1056/NEJMcibr022472. PMID 12456857.
↑ Kuba, K., Imai, Y., Rao, S., Gao, H., Guo, F., Guan, B., ... & Penninger, J. M. (2005). A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury. Nature medicine, 11(8), 875-879. doi:10.1038/nm1267

Turner AJ, Tipnis SR, Guy JL et al. (2002). "ACEH/ACE2 is a novel mammalian metallocarboxypeptidase and a homologue of angiotensin-converting enzyme insensitive to ACE inhibitors". Can. J. Physiol. Pharmacol. 80 (4): 346–53. doi:10.1139/y02-021. PMID 12025971.
Turner AJ, Hiscox JA, Hooper NM (2004). "ACE2: from vasopeptidase to SARS virus receptor". Trends Pharmacol. Sci. 25 (6): 291–4. doi:10.1016/j.tips.2004.04.001. PMID 15165741.
Katovich MJ, Grobe JL, Huentelman M, Raizada MK (2005). "Angiotensin-converting enzyme 2 as a novel target for gene therapy for hypertension". Exp. Physiol. 90 (3): 299–305. doi:10.1113/expphysiol.2004.028522. PMID 15640278.
Ferrario CM, Trask AJ, Jessup JA (2006). "Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function". Am. J. Physiol. Heart Circ. Physiol. 289 (6): H2281–90. doi:10.1152/ajpheart.00618.2005. PMID 16055515.
Jia HP, Look DC, Hickey M et al. (2006). "Infection of human airway epithelia by SARS coronavirus is associated with ACE2 expression and localization". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology 581: 479–84. doi:10.1007/978-0-387-33012-9_85. ISBN 978-0-387-26202-4. PMID 17037581. |chapter= ignored (help)
Lazartigues E, Feng Y, Lavoie JL (2007). "The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases". Curr. Pharm. Des. 13 (12): 1231–45. doi:10.2174/138161207780618911. PMID 17504232.
Raizada MK, Ferreira AJ (2007). "ACE2: a new target for cardiovascular disease therapeutics". J. Cardiovasc. Pharmacol. 50 (2): 112–9. doi:10.1097/FJC.0b013e3180986219. PMID 17703127.
Dean RG, Burrell LM (2007). "ACE2 and diabetic complications". Curr. Pharm. Des. 13 (26): 2730–5. doi:10.2174/138161207781662876. PMID 17897017.
Tipnis SR, Hooper NM, Hyde R et al. (2000). "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase". J. Biol. Chem. 275 (43): 33238–43. doi:10.1074/jbc.M002615200. PMID 10924499.
Donoghue M, Hsieh F, Baronas E et al. (2000). "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9". Circ. Res. 87 (5): E1–9. PMID 10969042.
Vickers C, Hales P, Kaushik V et al. (2002). "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase". J. Biol. Chem. 277 (17): 14838–43. doi:10.1074/jbc.M200581200. PMID 11815627.
Crackower MA, Sarao R, Oudit GY et al. (2002). "Angiotensin-converting enzyme 2 is an essential regulator of heart function". Nature 417 (6891): 822–8. doi:10.1038/nature00786. PMID 12075344.
Harmer D, Gilbert M, Borman R, Clark KL (2003). "Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme". FEBS Lett. 532 (1–2): 107–10. doi:10.1016/S0014-5793(02)03640-2. PMID 12459472.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Donoghue M, Wakimoto H, Maguire CT et al. (2004). "Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins". J. Mol. Cell. Cardiol. 35 (9): 1043–53. doi:10.1016/S0022-2828(03)00177-9. PMID 12967627.
Clark HF, Gurney AL, Abaya E et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Li W, Moore MJ, Vasilieva N et al. (2003). "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus". Nature 426 (6965): 450–4. doi:10.1038/nature02145. PMID 14647384.
Wong SK, Li W, Moore MJ et al. (2004). "A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2". J. Biol. Chem. 279 (5): 3197–201. doi:10.1074/jbc.C300520200. PMID 14670965.
Towler P, Staker B, Prasad SG et al. (2004). "ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis". J. Biol. Chem. 279 (17): 17996–8007. doi:10.1074/jbc.M311191200. PMID 14754895.

PDB gallery

1r42: Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

1r4l: Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

2ajf: Structure of SARS coronavirus spike receptor-binding domain complexed with its receptor

Angiotensin-converting enzyme 2

See also

References

Further reading