CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000285
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-coenzyme A thioesterase 8 
Protein Synonyms/Alias
 Acyl-CoA thioesterase 8; Choloyl-coenzyme A thioesterase; HIV-Nef-associated acyl-CoA thioesterase; PTE-2; Peroxisomal acyl-coenzyme A thioester hydrolase 1; PTE-1; Peroxisomal long-chain acyl-CoA thioesterase 1; Thioesterase II; hACTE-III; hACTEIII; hTE 
Gene Name
 ACOT8 
Gene Synonyms/Alias
 ACTEIII; PTE1; PTE2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52RHYWVPAKRLFGGQIacetylation[1]
52RHYWVPAKRLFGGQIubiquitination[2]
188QEVPIEIKPVNPSPLubiquitination[2]
318KPQVSESKL******acetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation. 
Sequence Annotation
 MOTIF 317 319 Microbody targeting signal (Potential).
 ACT_SITE 232 232 Charge relay system (By similarity).
 ACT_SITE 254 254 Charge relay system (By similarity).
 ACT_SITE 304 304 Charge relay system (By similarity).
 MOD_RES 2 2 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Host-virus interaction; Hydrolase; Peroxisome; Peroxisome biogenesis; Phosphoprotein; Reference proteome; Serine esterase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 319 AA 
Protein Sequence
MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV 60
GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP 120
IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA 180
QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL 240
LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV 300
TCAQEGVIRV KPQVSESKL 319 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0033882; F:choloyl-CoA hydrolase activity; IEA:EC.
 GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
 GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
 GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
 GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
 GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
 GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
 GO:0016559; P:peroxisome fission; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR003703; Acyl_CoA_thio. 
Pfam
  
SMART
  
PROSITE
  
PRINTS