ACACA

Acetyl-CoA carboxylase alpha

Identifiers

ACACA; ACAC; ACC; ACC1; ACCA

External IDs

OMIM: 200350 MGI: 108451 HomoloGene: 31015 GeneCards: ACACA Gene

6.4.1.2

Gene Ontology
Molecular function	• nucleotide binding • acetyl-CoA carboxylase activity • acetyl-CoA carboxylase activity • biotin carboxylase activity • protein binding • ATP binding • biotin binding • ligase activity • metal ion binding
Cellular component	• soluble fraction • cytoplasm • mitochondrion • cytosol • cytosol
Biological process	• tissue homeostasis • acetyl-CoA metabolic process • energy reserve metabolic process • fatty acid biosynthetic process • response to organic cyclic compound • triglyceride biosynthetic process • positive regulation of cellular metabolic process • long-chain fatty-acyl-CoA biosynthetic process • response to drug • cellular lipid metabolic process • multicellular organismal protein metabolic process • protein homotetramerization • lipid homeostasis
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
35.44 – 35.77 Mb

Chr 11:
83.94 – 84.22 Mb

PubMed search

[1]

[2]

Acetyl-CoA carboxylase 1 also known as ACC-alpha or ACCa is an enzyme that in humans is encoded by the ACACA gene.^[1]^[2]

Function

Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA.^[1]

References

^ ^a ^b "Entrez Gene: acetyl-Coenzyme A carboxylase alpha". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=31.
^ Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ (April 1995). "Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms". Proc. Natl. Acad. Sci. U.S.A. 92 (9): 4011–5. doi:10.1073/pnas.92.9.4011. PMC 42092. PMID 7732023. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42092.

Sinilnikova OM, McKay JD, Tavtigian SV, et al. (2007). "Haplotype-based analysis of common variation in the acetyl-coA carboxylase alpha gene and breast cancer risk: a case-control study nested within the European Prospective Investigation into Cancer and Nutrition". Cancer Epidemiol. Biomarkers Prev. 16 (3): 409–15. doi:10.1158/1055-9965.EPI-06-0617. PMID 17372234.
Diaz FJ, Meary A, Arranz MJ, et al. (2009). "Acetyl-coenzyme A carboxylase α gene variations may be associated with the direct effects of some antipsychotics on triglyceride levels". Schizophr. Res. 115 (2–3): 136–40. doi:10.1016/j.schres.2009.09.038. PMC 2784140. PMID 19846279. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2784140.
Yatscoff MA, Jaswal JS, Grant MR, et al. (2008). "Myocardial hypertrophy and the maturation of fatty acid oxidation in the newborn human heart". Pediatr. Res. 64 (6): 643–7. doi:10.1203/PDR.0b013e318184d281. PMID 18614968.
Law IK, Liu L, Xu A, et al. (2009). "Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins". Proteomics 9 (9): 2444–56. doi:10.1002/pmic.200800738. PMID 19343720.
Yoon S, Lee MY, Park SW, et al. (2007). "Up-regulation of acetyl-CoA carboxylase alpha and fatty acid synthase by human epidermal growth factor receptor 2 at the translational level in breast cancer cells". J. Biol. Chem. 282 (36): 26122–31. doi:10.1074/jbc.M702854200. PMID 17631500.
de Leon J, Correa JC, RuaÃ±o G, et al. (2008). "Exploring genetic variations that may be associated with the direct effects of some antipsychotics on lipid levels". Schizophr. Res. 98 (1–3): 40–6. doi:10.1016/j.schres.2007.10.003. PMID 18031993.
Lee YK, Hwang JT, Lee MS, et al. (2009). "Kidney bean husk extracts exert antitumor effect by inducing apoptosis involving AMP-activated protein kinase signaling pathway". Ann. N. Y. Acad. Sci. 1171: 484–8. doi:10.1111/j.1749-6632.2009.04697.x. PMID 19723093.
Lee-Young RS, Koufogiannis G, Canny BJ, McConell GK (2008). "Acute exercise does not cause sustained elevations in AMPK signaling or expression". Med Sci Sports Exerc 40 (8): 1490–4. doi:10.1249/MSS.0b013e318173a037. PMID 18614941.
Lu Y, DollÃ© ME, Imholz S, et al. (2008). "Multiple genetic variants along candidate pathways influence plasma high-density lipoprotein cholesterol concentrations". J. Lipid Res. 49 (12): 2582–9. doi:10.1194/jlr.M800232-JLR200. PMID 18660489.
Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
Scaglia N, Chisholm JW, Igal RA (2009). Bonini, Marcelo. ed. "Inhibition of StearoylCoA Desaturase-1 Inactivates Acetyl-CoA Carboxylase and Impairs Proliferation in Cancer Cells: Role of AMPK". PLoS ONE 4 (8): e6812. doi:10.1371/journal.pone.0006812. PMC 2728543. PMID 19710915. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2728543.
Oshikawa M, Sugai Y, Usami R, et al. (2008). "Fine Expression Profiling of Full-length Transcripts using a Size-unbiased cDNA Library Prepared with the Vector-capping Method". DNA Res. 15 (3): 123–36. doi:10.1093/dnares/dsn010. PMC 2650634. PMID 18487259. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2650634.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Conde E, Suarez-Gauthier A, GarcÃa-GarcÃa E, et al. (2007). "Specific pattern of LKB1 and phospho-acetyl-CoA carboxylase protein immunostaining in human normal tissues and lung carcinomas". Hum. Pathol. 38 (9): 1351–60. doi:10.1016/j.humpath.2007.01.022. PMID 17521700.
Ray H, Suau F, Vincent A, Dalla Venezia N (2009). "Cell cycle regulation of the BRCA1/acetyl-CoA-carboxylase complex". Biochem. Biophys. Res. Commun. 378 (3): 615–9. doi:10.1016/j.bbrc.2008.11.090. PMID 19061860.
Ma J, Yan R, Zu X, et al. (2008). "Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells". J. Biol. Chem. 283 (6): 3418–23. doi:10.1074/jbc.M707650200. PMID 18056116.
Locke GA, Cheng D, Witmer MR, et al. (2008). "Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate". Arch. Biochem. Biophys. 475 (1): 72–9. doi:10.1016/j.abb.2008.04.011. PMID 18455495.
RuaÃ±o G, Bernene J, Windemuth A, et al. (2009). "Physiogenomic comparison of edema and BMI in patients receiving rosiglitazone or pioglitazone". Clin. Chim. Acta 400 (1–2): 48–55. doi:10.1016/j.cca.2008.10.009. PMID 18996102.
Shen Y, Tong L (2008). "Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1". Biochemistry 47 (21): 5767–73. doi:10.1021/bi800314m. PMC 2392887. PMID 18452305. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2392887.

ACACA

Function

References

Further reading