CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011495
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Short-chain specific acyl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 SCAD; Butyryl-CoA dehydrogenase 
Gene Name
 Acads 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
51TCRDFAEKELVPIAAacetylation[1, 2, 3, 4, 5, 6]
51TCRDFAEKELVPIAAsuccinylation[5]
72LFPTAQVKKMGELGLacetylation[3, 4]
136KFGSAQQKQQWITPFacetylation[3]
262GEPGMGFKIAMQTLDacetylation[1, 3, 4, 5, 6]
262GEPGMGFKIAMQTLDsuccinylation[5]
292ASLDCAVKYAENRNAacetylation[1, 4, 7]
306AFGAPLTKLQNIQFKacetylation[1, 3, 4, 5, 6, 7, 8]
306AFGAPLTKLQNIQFKsuccinylation[5]
306AFGAPLTKLQNIQFKubiquitination[9]
335TWRAAMLKDNKKPFTacetylation[3]
338AAMLKDNKKPFTKESacetylation[3]
339AMLKDNKKPFTKESAacetylation[3]
343DNKKPFTKESAMAKLacetylation[3]
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] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] 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
  
Sequence Annotation
 NP_BIND 152 161 FAD (By similarity).
 NP_BIND 185 187 FAD (By similarity).
 NP_BIND 365 369 FAD (By similarity).
 NP_BIND 365 369 FAD; shared with dimeric partner (By
 NP_BIND 394 396 FAD (By similarity).
 REGION 269 272 Substrate binding (By similarity).
 ACT_SITE 392 392 Proton acceptor (By similarity).
 BINDING 161 161 Substrate; via carbonyl oxygen (By
 BINDING 297 297 FAD (By similarity).
 BINDING 297 297 FAD; shared with dimeric partner (By
 BINDING 308 308 FAD (By similarity).
 BINDING 393 393 Substrate; via amide nitrogen (By  
Keyword
 Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL 60
DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRACA STGVIMSVNN 120
SLYLGPILKF GSAQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN 180
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN 240
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF 300
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS 360
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS 412 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0031966; C:mitochondrial membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
 GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:EC.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0046359; P:butyrate catabolic process; IEA:Compara.
 GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0042594; P:response to starvation; IEA:Compara. 
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