CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008190
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 VLCAD 
Gene Name
 ACADVL 
Gene Synonyms/Alias
 VLCAD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
239AVPSPCGKYYTLNGSacetylation[1, 2]
276DPATGAVKEKITAFVacetylation[2, 3]
278ATGAVKEKITAFVVEacetylation[3]
299THGPPEKKMGIKASNubiquitination[4]
331GEVGSGFKVAMHILNacetylation[1, 5]
553VVEAKLIKHKKGIVNubiquitination[6]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. 
Sequence Annotation
 NP_BIND 214 223 FAD.
 NP_BIND 249 251 FAD.
 NP_BIND 435 439 FAD (By similarity).
 NP_BIND 464 466 FAD.
 REGION 41 482 Catalytic.
 REGION 338 341 Substrate binding (By similarity).
 REGION 462 463 Substrate binding.
 REGION 483 516 Membrane-anchoring (Probable).
 ACT_SITE 462 462 Proton acceptor.
 BINDING 223 223 Substrate; via carbonyl oxygen (By
 BINDING 366 366 FAD (By similarity).
 BINDING 463 463 Substrate; via amide nitrogen (By
 MOD_RES 237 237 S-nitrosocysteine (By similarity).
 MOD_RES 239 239 N6-acetyllysine.
 MOD_RES 276 276 N6-acetyllysine (By similarity).
 MOD_RES 331 331 N6-acetyllysine; alternate.
 CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; Complete proteome; Disease mutation; FAD; Fatty acid metabolism; Flavoprotein; Isopeptide bond; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Polymorphism; Reference proteome; S-nitrosylation; Transit peptide; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 655 AA 
Protein Sequence
MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD KSDSHPSDAL 60
TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ FLKELVEPVS RFFEEVNDPA 120
KNDALEMVEE TTWQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLGVGITLGA 180
HQSIGFKGIL LFGTKAQKEK YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY 240
YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM 300
GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIIAKAV 360
DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGATD FQIEAAISKI 420
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK 480
GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL 540
EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK 600
MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS NPLGF 655 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; TAS:ProtInc.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0015980; P:energy derivation by oxidation of organic compounds; TAS:ProtInc.
 GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:BHF-UCL.
 GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:BHF-UCL.
 GO:0046322; P:negative regulation of fatty acid oxidation; ISS:BHF-UCL.
 GO:0090181; P:regulation of cholesterol metabolic process; ISS:BHF-UCL.
 GO:0001659; P:temperature homeostasis; ISS: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