CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013136
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-coenzyme A synthetase ACSM3, mitochondrial 
Protein Synonyms/Alias
 Acyl-CoA synthetase medium-chain family member 3; Butyrate--CoA ligase 3; Butyryl-coenzyme A synthetase 3; Middle-chain acyl-CoA synthetase 3; Protein SA homolog 
Gene Name
 Acsm3 
Gene Synonyms/Alias
 Sa; Sah 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
67DQWTNMEKAGKRLSNacetylation[1]
151GTTQLTQKDILYRLQacetylation[1]
181AVDAVAAKCENLHSKacetylation[1]
336QNDMSSYKFNSLKHCacetylation[1]
336QNDMSSYKFNSLKHCubiquitination[2]
533SHDQEQLKKEIQEHVacetylation[1]
541KEIQEHVKKTTAPYKacetylation[1]
548KKTTAPYKYPRKVEFacetylation[1]
552APYKYPRKVEFIEELubiquitination[2]
566LPKTVSGKVKRNELRacetylation[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]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). 
Sequence Annotation
 NP_BIND 229 237 ATP (By similarity).
 NP_BIND 368 373 ATP (By similarity).
 BINDING 455 455 ATP (By similarity).
 BINDING 470 470 ATP (By similarity).
 BINDING 566 566 ATP (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 580 AA 
Protein Sequence
MVMLLRARCF QRLAIPDPMR VLYKDYRTAT PQNFSNYESM KQDFKIEIPE YFNFAKDVLD 60
QWTNMEKAGK RLSNPAFWWI DGNGEELRWS FEELGLLSRK FANILTEACS LQRGDRVMVI 120
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KAKCIITDDT LAPAVDAVAA 180
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH DEMMAIYFTS GTTGPPKMIG 240
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF 300
ESTSILQTLS KFPITVFCSA PTAYRMLVQN DMSSYKFNSL KHCVSAGEPI NPEVMEQWRK 360
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFD VKILDENGAT LPPGQEGDIA 420
LQVLPERPFG LFTHYVDNPS KTASTLRGSF YITGDRGYMD EDGYFWFVAR SDDIILSSGY 480
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKSHDQE QLKKEIQEHV 540
KKTTAPYKYP RKVEFIEELP KTVSGKVKRN ELRKKEWEQG LLHEQMTVDR LLGKSARHER 600
HVPSVCMNCS GVAAVLRYAE AA 622 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0047760; F:butyrate-CoA ligase activity; IEA:EC.
 GO:0015645; F:fatty acid ligase activity; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006633; P:fatty acid biosynthetic process; IDA:MGI. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 
Pfam
 PF00501; AMP-binding
 PF13193; DUF4009 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS