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Identification
HMDB Protein ID HMDBP01047
Secondary Accession Numbers
  • 6336
Name Acyl-coenzyme A thioesterase 2, mitochondrial
Synonyms
  1. Acyl-CoA thioesterase 2
  2. Acyl-coenzyme A thioester hydrolase 2a
  3. CTE-Ia
  4. Long-chain acyl-CoA thioesterase 2
  5. ZAP128
Gene Name ACOT2
Protein Type Enzyme
Biological Properties
General Function Involved in thiolester hydrolase activity
Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs.
Pathways
  • Biosynthesis of unsaturated fatty acids
  • Fatty acid elongation
Reactions
hexadecanoyl-CoA + Water → Coenzyme A + Palmitic acid details
Stearoyl-CoA + Water → Coenzyme A + Stearic acid details
Eicosanoyl-CoA + Water → Coenzyme A + Arachidic acid details
Oleoyl-CoA + Water → Coenzyme A + Oleic acid details
Linoleoyl-CoA + Water → Coenzyme A + Linoleic acid details
Alpha-Linolenoyl-CoA + Water → Coenzyme A + alpha-Linolenic acid details
(5Z,8Z,11Z,14Z,17Z)-Icosapentaenoyl-CoA + Water → Coenzyme A + Eicosapentaenoic acid details
Cervonyl coenzyme A + Water → Coenzyme A + Docosahexaenoic acid details
Gamma-linolenoyl-CoA + Water → Coenzyme A + gamma-Linolenic acid details
Dihomo-gamma-linolenyl coenzyme A + Water → Coenzyme A + Dihomo-gamma-linolenic acid details
Arachidonyl-CoA + Water → Coenzyme A + Arachidonic acid details
Propionyl-CoA + Water → Long-chain fatty acid + Coenzyme A details
GO Classification
Biological Process
very long-chain fatty acid metabolic process
acyl-CoA metabolic process
long-chain fatty acid metabolic process
Cellular Component
mitochondrion
Function
coa hydrolase activity
hydrolase activity, acting on ester bonds
acyl-coa thioesterase activity
palmitoyl-coa hydrolase activity
catalytic activity
hydrolase activity
thiolester hydrolase activity
Molecular Function
acyl-CoA hydrolase activity
carboxylesterase activity
palmitoyl-CoA hydrolase activity
Process
acyl-coa metabolic process
metabolic process
primary metabolic process
cellular metabolic process
lipid metabolic process
cofactor metabolic process
coenzyme metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 14
Locus 14q24.3
SNPs ACOT2
Gene Sequence
>1452 bp
ATGTCTAACAAGCTTCTTTCTCCCCACCCCCATTCAGTTGTTCTCAGGTCTGAATTCAAA
ATGGCCTCATCTCCTGCTGTCCTTCGAGCGTCCCGGCTGTACCAATGGAGCCTGAAGAGT
TCGGCGCAGTTCCTGGGGTCTCCACAGCTGAGGCAGGTTGGTCAGATCATTAGGGTTCCT
GCTCGGATGGCGGCGACGCTGATCCTGGAGCCTGCGGGCCGCTGCTGCTGGGACGAACCG
GTGCGAATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTG
CGCGACGAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACTCTTGGC
GAGCTGGACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATG
GGGCTGCTCTGGGCCTTGGAGCCCGAGAAACCTTTGGTGCGGCTGGTGAAGCGCGACGTG
CGAACGCCCTTGGCCGTGGTGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGG
CTGCTGTGCCAGACGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCG
GTGCGCGTGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCT
GGGATTGTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTG
GCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTATTATAACTATGAAGACCTCCCCAAG
ACCATGGAGACGCTCCATCTGGAGTACTTTGAAGAAGCCATGAACTACTTGCTCAGTCAT
CCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGC
CTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTG
GCCAATGTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAAC
AGAAATCGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGC
CCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTC
CTGTTCCTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCC
TGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACA
GGGCACTATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTG
GGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCT
TGGAAACAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCGCGAGGGGACAATCCCA
TCAAAAGTGTAA
Protein Properties
Number of Residues 483
Molecular Weight 53218.02
Theoretical pI 8.471
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Acyl-coenzyme A thioesterase 2, mitochondrial
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIP
SKV
GenBank ID Protein 7023514
UniProtKB/Swiss-Prot ID P49753
UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN
PDB IDs
GenBank Gene ID AK001939
GeneCard ID ACOT2
GenAtlas ID ACOT2
HGNC ID HGNC:18431
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. 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 ]
  4. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, Tsuda T, Mar L, Foncin JF, Bruni AC, Montesi MP, Sorbi S, Rainero I, Pinessi L, Nee L, Chumakov I, Pollen D, Brookes A, Sanseau P, Polinsky RJ, Wasco W, Da Silva HA, Haines JL, Perkicak-Vance MA, Tanzi RE, Roses AD, Fraser PE, Rommens JM, St George-Hyslop PH: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed:7596406 ]
  5. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed:16940157 ]
  6. Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed:10944470 ]