MCAT (gene)

MCAT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2C2N
Identifiers
Aliases	MCAT, FASN2C, MCT, MT, NET62, fabD, malonyl-CoA-acyl carrier protein transacylase, MCT1
External IDs	OMIM: 614479; MGI: 2388651; HomoloGene: 15511; GeneCards: MCAT; OMA:MCAT - orthologs
Gene location (Human) Chr. Chromosome 22 (human) Band 22q13.2 Start 43,132,209 bp End 43,143,398 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 E1 Start 83,430,998 bp End 83,447,988 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon right uterine tube right adrenal gland right adrenal cortex epithelium of bronchus left adrenal gland prefrontal cortex gonad left adrenal cortex bronchial epithelial cell Top expressed in spermatocyte interventricular septum right kidney spermatid seminiferous tubule proximal tubule right ventricle muscle of thigh left lobe of liver ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity catalytic activity [acyl-carrier-protein S-malonyltransferase activity] RNA binding fatty acid synthase activity S-malonyltransferase activity Cellular component mitochondrion mitochondrial matrix Biological process metabolism fatty acid biosynthetic process fatty acid metabolic process lipid metabolism fatty acid beta-oxidation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27349 223722 Ensembl ENSG00000100294 ENSMUSG00000048755 UniProt Q8IVS2 Q8R3F5 RefSeq (mRNA) NM_014507 NM_173467 NM_001030014 RefSeq (protein) NP_055322 NP_775738 NP_001025185 Location (UCSC) Chr 22: 43.13 – 43.14 Mb Chr 15: 83.43 – 83.45 Mb PubMed search
Wikidata
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Malonyl CoA-acyl carrier protein transacylase, mitochondrial is an enzyme that in humans is encoded by the MCAT gene.

Function

The protein encoded by this gene is found exclusively in the mitochondrion, where it catalyzes the transfer of a malonyl group from malonyl-CoA to the mitochondrial acyl carrier protein. The encoded protein may be part of a fatty acid synthase complex that is more like the type II prokaryotic and plastid complexes rather than the type I human cytosolic complex. Two transcript variants encoding different isoforms have been found for this gene.

Clinical significance

The enzyme encoded by the MCAT gene, along with other enzymes that regulate Malonyl-CoA concentration, have been shown to regulate levels such that malonyl-CoA concentration decreases in human muscle tissue when under exercise training. This enzyme specifically has increased activity under these conditions, as it is known to catabolize malonyl-CoA.

Interactions

The human Malonyl CoA-acel carrier protein transacylase in human mitochondria associates with respiratory complex one, such that it interacts functionally with a mitochondrial malonyltransferase. Both species are encoded by nuclear genes, and their translocation into mitochondria is dependent on the presence of an N-terminal targeting sequence.

Further reading

• Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC (Mar 2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
• Kuhl JE, Ruderman NB, Musi N, Goodyear LJ, Patti ME, Crunkhorn S, Dronamraju D, Thorell A, Nygren J, Ljungkvist O, Degerblad M, Stahle A, Brismar TB, Andersen KL, Saha AK, Efendic S, Bavenholm PN (Jun 2006). "Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle". American Journal of Physiology. Endocrinology and Metabolism. 290 (6): E1296–303. doi:10.1152/ajpendo.00341.2005. PMID 16434556.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I (Jan 2003). "Reevaluating human gene annotation: a second-generation analysis of chromosome 22". Genome Research. 13 (1): 27–36. doi:10.1101/gr.695703. PMC 430954. PMID 12529303.
• Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.