Carnitine O-acetyltransferase

Details

Name
Carnitine O-acetyltransferase
Synonyms
  • 2.3.1.7
  • Carnitine acetylase
  • Carnitine acetyltransferase
  • CAT
  • CAT1
  • CrAT
Gene Name
CRAT
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037028|Carnitine O-acetyltransferase
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSE
EEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSP
GVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSC
RVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSS
LQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVY
RSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIE
YTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKD
FPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVK
AMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMD
TSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNA
ARLAHYLEKALLDMRALLQSHPRAKL
Number of residues
626
Molecular Weight
70857.055
Theoretical pI
8.63
GO Classification
Functions
carnitine O-acetyltransferase activity / receptor binding
Processes
carnitine metabolic process, CoA-linked / cellular lipid metabolic process / fatty acid beta-oxidation using acyl-CoA oxidase / small molecule metabolic process / transport
Components
endoplasmic reticulum / mitochondrial inner membrane / mitochondrion / peroxisomal matrix / peroxisome
General Function
Receptor binding
Specific Function
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum
Gene sequence
>lcl|BSEQ0018962|Carnitine O-acetyltransferase (CRAT)
ATGTTAGCCTTCGCTGCCAGGACCGTGGTGAAGCCTCTGGGCTTCCTGAAGCCCTTCTCC
TTGATGAAGGCTTCCAGCCGCTTCAAGGCACACCAGGATGCACTGCCACGGCTGCCCGTG
CCCCCTCTCCAGCAGTCCCTGGACCACTACCTGAAGGCGCTGCAGCCCATCGTGAGTGAG
GAGGAGTGGGCCCACACCAAGCAGCTGGTGGATGAGTTTCAGGCCTCAGGAGGTGTAGGG
GAGCGCCTGCAGAAGGGGCTGGAGCGTCGGGCCAGGAAGACGGAGAACTGGCTGTCTGAG
TGGTGGCTCAAGACCGCCTACCTCCAGTACCGCCAGCCTGTGGTCATCTACTCGAGCCCA
GGCGTGATGCTACCCAAGCAGGACTTCGTGGACCTGCAGGGTCAGCTCCGATTTGCTGCC
AAACTCATTGAGGGTGTGTTGGATTTCAAGGTCATGATTGACAACGAGACCCTGCCCGTG
GAGTACCTGGGGGGGAAGCCACTGTGCATGAACCAGTACTATCAGATCTTGTCCTCCTGC
CGAGTGCCGGGCCCCAAGCAGGACACAGTCAGCAACTTCAGCAAGACCAAGAAGCCTCCC
ACGCACATCACCGTGGTACACAACTACCAGTTTTTTGAGCTGGATGTGTACCACAGTGAC
GGGACACCCCTCACTGCGGATCAGATCTTTGTGCAGCTGGAGAAGATCTGGAACTCATCC
CTACAGACCAACAAGGAGCCTGTGGGCATCCTCACCTCCAACCACCGCAACTCCTGGGCC
AAGGCATACAACACCCTCATCAAAGACAAGGTGAACCGGGATTCCGTGCGCTCCATCCAG
AAGAGCATCTTCACCGTGTGCCTAGATGCAACCATGCCCAGGGTCTCAGAAGACGTGTAC
CGCAGCCACGTGGCAGGCCAGATGCTGCATGGGGGCGGCAGCAGGCTCAACAGCGGCAAC
CGCTGGTTCGACAAGACGCTGCAGTTCATCGTGGCAGAAGATGGCTCCTGTGGGCTTGTG
TACGAGCATGCTGCAGCGGAGGGGCCCCCTATTGTCACCCTTCTGGACTATGTCATCGAG
TACACGAAGAAACCCGAGCTTGTGCGGTCTCCCATGGTGCCCCTGCCCATGCCCAAGAAG
CTGCGGTTCAACATCACCCCCGAGATCAAGAGCGACATCGAGAAGGCCAAGCAGAACCTC
AGCATCATGATCCAGGACCTGGATATCACCGTGATGGTGTTCCACCATTTTGGAAAAGAC
TTCCCCAAGTCGGAGAAGCTAAGCCCAGATGCCTTCATCCAGATGGCTTTGCAGCTGGCC
TACTACAGGATCTACGGACAGGCATGTGCCACCTATGAAAGTGCCTCCCTGCGCATGTTT
CACCTGGGCCGCACCGACACCATCCGCTCGGCTTCCATGGACTCACTCACCTTTGTCAAG
GCCATGGATGACTCCAGCGTCACGGAGCACCAGAAGGTGGAGCTGCTGCGGAAGGCCGTG
CAGGCCCACCGAGGCTACACCGACCGGGCCATCCGCGGGGAGGCCTTTGATCGACACCTG
CTGGGCCTGAAGCTGCAGGCCATCGAGGACCTGGTGAGCATGCCCGACATCTTCATGGAC
ACCTCCTACGCCATCGCCATGCACTTCCACCTCTCCACCAGCCAGGTCCCTGCCAAGACA
GACTGTGTCATGTTCTTCGGGCCCGTGGTCCCCGACGGCTACGGTGTCTGCTATAACCCC
ATGGAGGCCCACATCAACTTCTCCCTGTCGGCCTACAACAGCTGCGCGGAGACCAACGCC
GCCCGCCTGGCGCATTACCTGGAGAAGGCGCTCCTGGACATGCGTGCCCTGCTGCAGAGC
CACCCCCGGGCCAAGCTCTGA
Chromosome Location
9
Locus
9q34.1
External Identifiers
ResourceLink
UniProtKB IDP43155
UniProtKB Entry NameCACP_HUMAN
GenBank Protein ID927415
GenBank Gene IDX78706
GenAtlas IDCRAT
HGNC IDHGNC:2342
General References
  1. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053]
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  3. Corti O, DiDonato S, Finocchiaro G: 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. 1994 Oct 1;303 ( Pt 1):37-41. [PubMed:7945262]
  4. Corti O, Finocchiaro G, Rossi E, Zuffardi O, DiDonato S: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. Genomics. 1994 Sep 1;23(1):94-9. [PubMed:7829107]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861]
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  7. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00583Levocarnitineapproved, investigationalunknownDetails
DB02648(3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-AmmoniumexperimentalunknownDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails