CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009121
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; Peroxisomal acyl-CoA thioesterase 2; PTE-2; Peroxisomal acyl-coenzyme A thioester hydrolase 1; PTE-1; Peroxisomal long-chain acyl-CoA thioesterase 1 
Gene Name
 Acot8 
Gene Synonyms/Alias
 Pte1; Pte2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
92FVRAGDPKVPVLYHVacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123
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. 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. May be involved in the metabolic regulation of peroxisome proliferation. 
Sequence Annotation
 MOTIF 318 320 Microbody targeting signal (Potential).
 ACT_SITE 233 233 Charge relay system (By similarity).
 ACT_SITE 255 255 Charge relay system (By similarity).
 ACT_SITE 305 305 Charge relay system (By similarity).
 MOD_RES 2 2 Phosphoserine.  
Keyword
 Complete proteome; Hydrolase; Peroxisome; Peroxisome biogenesis; Phosphoprotein; Reference proteome; Serine esterase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 320 AA 
Protein Sequence
MSAPEGLGDA HGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP TSQRLFGGQI 60
MGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE RIRTGASFSV RAVKAVQHGK 120
AIFICQASFQ QMQPSPLQHQ FSMPSVPPPE DLLDHEALID QYLRDPNLHK KYRVGLNRVA 180
AQEVPIEIKV VNPPTLTQLQ ALEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA 240
LLPHQSKYKV NFMASLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA 300
VTCAQEGVIR LKPQVSESKL 320 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005782; C:peroxisomal matrix; IEA:Compara.
 GO:0005777; C:peroxisome; IDA:HGNC.
 GO:0047617; F:acyl-CoA hydrolase activity; IDA:MGI.
 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; IEA:Compara.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:Compara.
 GO:0006637; P:acyl-CoA metabolic process; IDA:MGI.
 GO:0043649; P:dicarboxylic acid catabolic process; IEA:Compara.
 GO:0016559; P:peroxisome fission; IEA:Compara. 
Interpro
 IPR003703; Acyl_CoA_thio. 
Pfam
  
SMART
  
PROSITE
  
PRINTS