CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008363
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain specific acyl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 LCAD 
Gene Name
 Acadl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
42RLETPSAKKLTDVGIacetylation[1, 2, 3]
42RLETPSAKKLTDVGIsuccinylation[2]
66IFRESVRKFFQEEVIacetylation[1, 2]
66IFRESVRKFFQEEVIsuccinylation[2]
81PHHTEWEKAGEVSREacetylation[1, 2, 3, 4, 5, 6, 7]
81PHHTEWEKAGEVSREsuccinylation[2]
81PHHTEWEKAGEVSREubiquitination[8]
92VSREVWEKAGKQGLLacetylation[1, 2, 3, 4, 5, 9]
92VSREVWEKAGKQGLLsuccinylation[2]
95EVWEKAGKQGLLGINacetylation[1, 2, 3]
95EVWEKAGKQGLLGINsuccinylation[2]
151YIANYGTKEQIEKFIacetylation[1, 4]
156GTKEQIEKFIPQMTAacetylation[2, 3, 5]
156GTKEQIEKFIPQMTAsuccinylation[2]
165IPQMTAGKCIGAIAMacetylation[2]
165IPQMTAGKCIGAIAMsuccinylation[2]
240FLVENGMKGFIKGRKacetylation[2]
240FLVENGMKGFIKGRKsuccinylation[2]
254KLHKMGMKAQDTAELacetylation[1, 2, 3, 4, 5]
254KLHKMGMKAQDTAELsuccinylation[2]
279ALLGEENKGFYYLMQacetylation[1, 2, 4]
279ALLGEENKGFYYLMQsuccinylation[2]
315EETRNYVKQRKAFGKacetylation[1]
318RNYVKQRKAFGKTVAacetylation[1]
322KQRKAFGKTVAHIQTacetylation[1, 2, 3, 4, 5, 10]
322KQRKAFGKTVAHIQTsuccinylation[2]
358CLQLHETKRLDSGSAacetylation[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [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 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]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [8] 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]
 [9] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [10] 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] 
Functional Description
  
Sequence Annotation
  
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
 430 AA 
Protein Sequence
MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR RIFSSEHDIF 60
RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT 120
WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD 180
LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK 240
GFIKGRKLHK MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI 300
SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS CLQLHETKRL 360
DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE 420
LIARQIVSDS 430 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0031966; C:mitochondrial membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:Compara.
 GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
 GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:BHF-UCL.
 GO:0042413; P:carnitine catabolic process; IMP:BHF-UCL.
 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:0042758; P:long-chain fatty acid catabolic process; IEA:Compara.
 GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
 GO:0046322; P:negative regulation of fatty acid oxidation; IMP:BHF-UCL.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL.
 GO:0001659; P:temperature homeostasis; IMP:BHF-UCL. 
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