human-ACOT2

 
Homo sapiens (Human) peroxisomal long-chain Acyl-CoA thioesterase 2 (zap128) (protein for mgc:3983) mitochondrial (EC 3.1.2.2) CTE-1a

Comment
Trembl Q86TX2 genbank BX161396 humant-cte1 some aa different the two genes are adjacent. Acyl-CoA thioesterase 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 The mouse ACOT gene cluster comprises six genes with localizations in cytosol (ACOT1), mitochondria (ACOT2), and peroxisomes (ACOT3-6). The corresponding human gene cluster contains only three genes (ACOT1, ACOT2, and ACOT4) coding for full-length thioesterase proteins only ACOT4 is peroxisomal


Relationship
Block X
Homo sapiens position in NCBI Life Tree :
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain.
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E

Molecular evidence
Database
No mutation
1 structure:
3HLK: Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
No kinetic


Inhibitor: Rocaglate-Derived-beta-Lactone-5 ,
>3 Genbank links 7 more: DQ082755, AK223635, AY005822
1 UniProt : P49753
1 Structure : 3HLK
1 UniProtTrembl : P49753
1 Interpro : P49753
1 Prodom : P49753
1 Pfam : P49753
1 PIRSF : P49753
1 SUPERFAM : P49753
1 QuickSwissBlast : P49753
1 EntrezGene : 10965
1 SNP : 10965
1 UniGene : 446685
1 HUGO HGNC : 18431
1 OMIM : 609972
1 Ensembl : ENSG00000119673
 
Sequence
Graphical view for this peptide sequence: human-ACOT2
Colored MSA for Acyl-CoA_Thioesterase (raw)
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQL
RQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASL
RDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEK
PLVRLVKRDVRTPLAVVLEVLDGHDPDPGRLLCQTRHERYFLPPGVRREP
VRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMAL
AYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDG
YADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEA
CKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEP
RAHAMAQVDAWKQLQTFFHKHLGGREGTIPSKV
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQL
RQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASL
RDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEK
PLVRLVKRDVRTPLAVVLEVLDGHDPDPGRLLCQTRHERYFLPPGVRREP
VRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMAL
AYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDG
YADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEA
CKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEP
RAHAMAQVDAWKQLQTFFHKHLGGREGTIPSKV

no DNA




References
4 more
    Title: Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived beta-lactone
    Lajkiewicz NJ, Cognetta AB, 3rd, Niphakis MJ, Cravatt BF, Porco JA, Jr.
    Ref: Journal of the American Chemical Society, 136:2659, 2014 : PubMed

            

    Title: 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
    Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE
    Ref: FASEB Journal, 20:1855, 2006 : PubMed

            

    Title: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase.
    Jones JM, Gould SJ
    Ref: Biochemical & Biophysical Research Communications, 275:233, 2000 : PubMed

            


Other Papers


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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