CRAT (gene)

From Wikipedia, the free encyclopedia

Carnitine acetyltransferase

PDB rendering based on 1ndb.

Available structures: 1ndb, 1ndf, 1ndi, 1nm8, 1s5o, 1t7n, 1t7o, 1t7q, 2h3p, 2h3u, 2h3w

Identifiers

Symbol(s)

CRAT; CAT1

External IDs

OMIM: 600184 MGI: 109501 HomoloGene: 598

Gene ontology
Molecular Function:	• carnitine O-acetyltransferase activity • acyltransferase activity • transferase activity
Cellular Component:	• mitochondrion • peroxisome • endoplasmic reticulum
Biological Process:	• lipid metabolic process • acyl-CoA metabolic process • transport • energy derivation by oxidation of organic compounds

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_144782 (mRNA)
NP_659006 (protein)

NM_007760 (mRNA)
NP_031786 (protein)

Location

Chr 9: 130.9 - 130.91 Mb

Chr 2: 30.22 - 30.24 Mb

Pubmed search

[1]

[2]

Carnitine acetyltransferase, also known as CRAT, is a human gene.^[1]

Carnitine acetyltransferase (CRAT) is a key enzyme in the metabolic pathway in mitochondria, peroxisomes and endoplasmic reticulum. CRAT catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of acylCoA/CoA in the subcellular compartments. Different subcellular localizations of the CRAT mRNAs are thought to result from alternative splicing of the CRAT gene suggested by the divergent sequences in the 5' region of peroxisomal and mitochondrial CRAT cDNAs and the location of an intron where the sequences diverge. The alternatively splicing of this gene results in three distinct isoforms, one of which contains an N-terminial mitochondrial transit peptide, and has been shown to be located in mitochondria.^[1]

[edit] References

^ ^a ^b Entrez Gene: CRAT carnitine acetyltransferase.

[edit] Further reading

van der Leij FR, Huijkman NC, Boomsma C, et al. (2000). "Genomics of the human carnitine acyltransferase genes.". Mol. Genet. Metab. 71 (1-2): 139–53. doi:10.1006/mgme.2000.3055. PMID 11001805.
Kalaria RN, Harik SI (1992). "Carnitine acetyltransferase activity in the human brain and its microvessels is decreased in Alzheimer's disease.". Ann. Neurol. 32 (4): 583–6. doi:10.1002/ana.410320417. PMID 1456745.
Corti O, Finocchiaro G, Rossi E, et al. (1995). "Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1.". Genomics 23 (1): 94–9. doi:10.1006/geno.1994.1463. PMID 7829107.
Corti O, DiDonato S, Finocchiaro G (1994). "Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations.". Biochem. J. 303 ( Pt 1): 37–41. PMID 7945262.
Lian W, Govindasamy L, Gu Y, et al. (2003). "Crystallization and preliminary X-ray crystallographic studies on recombinant human carnitine acetyltransferase.". Acta Crystallogr. D Biol. Crystallogr. 58 (Pt 7): 1193–4. PMID 12077440.
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. PMID 12477932.
Jogl G, Tong L (2003). "Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport.". Cell 112 (1): 113–22. PMID 12526798.
Wu D, Govindasamy L, Lian W, et al. (2003). "Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer.". J. Biol. Chem. 278 (15): 13159–65. doi:10.1074/jbc.M212356200. PMID 12562770.
Govindasamy L, Kukar T, Lian W, et al. (2005). "Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase.". J. Struct. Biol. 146 (3): 416–24. doi:10.1016/j.jsb.2004.01.011. PMID 15099582.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.