CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007755
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 MCAD 
Gene Name
 Acadm 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
69PVAPEYDKSGEYPFPacetylation[1, 2, 3, 4]
69PVAPEYDKSGEYPFPsuccinylation[3]
79EYPFPLIKRAWELGLacetylation[1, 2, 3, 4, 5]
79EYPFPLIKRAWELGLsuccinylation[3]
79EYPFPLIKRAWELGLubiquitination[6]
173GSDVAAIKTKAEKKGacetylation[1]
178AIKTKAEKKGDEYVIacetylation[2, 4, 5]
179IKTKAEKKGDEYVINacetylation[2, 3, 5]
179IKTKAEKKGDEYVINsuccinylation[3]
212ARSNPDPKVPASKAFacetylation[2, 3, 4, 5]
212ARSNPDPKVPASKAFsuccinylation[3]
217DPKVPASKAFTGFIVacetylation[2, 3, 4, 5]
217DPKVPASKAFTGFIVsuccinylation[3]
235TPGIHIGKKELNMGQacetylation[2, 3]
235TPGIHIGKKELNMGQsuccinylation[3]
235TPGIHIGKKELNMGQubiquitination[6]
236PGIHIGKKELNMGQRacetylation[2]
259FEDVRVPKENVLIGEacetylation[1, 2, 3, 5]
259FEDVRVPKENVLIGEsuccinylation[3]
271IGEGAGFKIAMGAFDacetylation[2, 3, 4]
271IGEGAGFKIAMGAFDsuccinylation[3]
301RALDEATKYALDRKTacetylation[2, 4, 5]
301RALDEATKYALDRKTubiquitination[6]
395EKLMRDAKIYQIYEGubiquitination[6]
418IAREHIEKYKN****acetylation[2, 4, 5]
Reference
 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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
 This enzyme is specific for acyl chain lengths of 4 to 16. 
Sequence Annotation
 NP_BIND 158 167 FAD (By similarity).
 NP_BIND 191 193 FAD (By similarity).
 NP_BIND 306 308 FAD (By similarity).
 NP_BIND 316 317 FAD (By similarity).
 NP_BIND 374 378 FAD (By similarity).
 NP_BIND 403 405 FAD (By similarity).
 REGION 278 281 Substrate binding (By similarity).
 ACT_SITE 401 401 Proton acceptor (By similarity).
 BINDING 167 167 Substrate; via carbonyl oxygen (By
 BINDING 402 402 Substrate; via amide nitrogen (By
 BINDING 413 413 Substrate (By similarity).
 MOD_RES 301 301 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI 60
IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ 120
TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG 180
DEYVINGQKM WITNGGKANW YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM 240
GQRCSDTRGI AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 300
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAF 360
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK 420
N 421 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
 GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
 GO:0045329; P:carnitine biosynthetic process; IEA:Compara.
 GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
 GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
 GO:0005978; P:glycogen biosynthetic process; IMP:BHF-UCL.
 GO:0001889; P:liver development; IMP:MGI.
 GO:0051793; P:medium-chain fatty acid catabolic process; IEA:Compara.
 GO:0051791; P:medium-chain fatty acid metabolic process; IMP:BHF-UCL.
 GO:0009791; P:post-embryonic development; IMP:MGI.
 GO:0006111; P:regulation of gluconeogenesis; IMP:BHF-UCL.
 GO:0009409; P:response to cold; IMP:MGI.
 GO:0042594; P:response to starvation; IMP:MGI. 
Interpro
 IPR006089; Acyl-CoA_DH_CS.
 IPR006092; Acyl-CoA_DH_N.
 IPR006090; Acyl-CoA_Oxase/DH_1.
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase. 
Pfam
 PF00441; Acyl-CoA_dh_1
 PF02770; Acyl-CoA_dh_M
 PF02771; Acyl-CoA_dh_N 
SMART
  
PROSITE
 PS00072; ACYL_COA_DH_1
 PS00073; ACYL_COA_DH_2 
PRINTS