UniProt Accession

 ACSM3_MOUSE; Q3UNX5; Q8BRY2; Q91WI1; Q9Z2F3; Q9Z2X0 

Genbank Protein ID

 AY064696; AB022340; AF068246; AK041060; AK143946; AK165516; BC015248 

Genbank Nucleotide ID

 AAL40880.1; BAA37141.1; AAC79656.1; BAC30805.1; BAE25622.1; BAE38232.1; AAH15248.1 

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
67	DQWTNMEKAGKRLSN	acetylation	[1]
67	DQWTNMEKAGKRLSN	succinylation	[1]
100	ELGLLSRKFANILTE	acetylation	[1]
100	ELGLLSRKFANILTE	succinylation	[1]
151	GTTQLTQKDILYRLQ	acetylation	[2, 3]
181	AVDAVAAKCENLHSK	acetylation	[3]
188	KCENLHSKLIVSQHS	acetylation	[3]
207	GNLKEMMKYASDSHT	acetylation	[3]
336	QNDMSSYKFNSLKHC	ubiquitination	[4]
533	SHDQEQLKKEIQEHV	acetylation	[3]
541	KEIQEHVKKTTAPYK	acetylation	[2]
552	APYKYPRKVEFIEEL	ubiquitination	[4]

Reference

 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] 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

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