CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000587
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Very long-chain acyl-CoA synthetase 
Protein Synonyms/Alias
 VLACS; VLCS; Fatty acid transport protein 2; FATP-2; Fatty-acid-coenzyme A ligase, very long-chain 1; Long-chain-fatty-acid--CoA ligase; Solute carrier family 27 member 2; THCA-CoA ligase; Very long-chain-fatty-acid-CoA ligase 
Gene Name
 Slc27a2 
Gene Synonyms/Alias
 Acsvl1; Facvl1; Fatp2; Vlacs; Vlcs 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
141LNYNIRAKSLLHCFQubiquitination[1]
173EEVLPTLKKDAVSVFubiquitination[1]
174EVLPTLKKDAVSVFYubiquitination[1]
197GVDTILDKVDGVSAEubiquitination[1]
233SGTTGLPKAATINHHubiquitination[1]
291ATLALRSKFSASQFWacetylation[2, 3]
325YLCNTPQKPNDRDHKacetylation[2]
325YLCNTPQKPNDRDHKubiquitination[1]
332KPNDRDHKVKKALGNubiquitination[1]
335DRDHKVKKALGNGLRubiquitination[1]
351DVWREFIKRFGDIHVubiquitination[1]
398VARYELIKYDVEKDEacetylation[3, 4]
398VARYELIKYDVEKDEubiquitination[1]
403LIKYDVEKDEPVRDAacetylation[3, 4]
416DANGYCIKVPKGEVGubiquitination[1]
419GYCIKVPKGEVGLLVubiquitination[1]
442FIGYAGGKTQTEKKKubiquitination[1]
456KLRDVFKKGDIYFNSubiquitination[1]
530RIGMASLKIKENYEFubiquitination[1]
532GMASLKIKENYEFNGubiquitination[1]
540ENYEFNGKKLFQHIAacetylation[3, 4]
541NYEFNGKKLFQHIAEubiquitination[1]
572IEITGTFKHRKVTLMubiquitination[1]
575TGTFKHRKVTLMEEGubiquitination[1]
589GFNPTVIKDTLYFMDubiquitination[1]
600YFMDDAEKTFVPMTEacetylation[5]
616IYNAIIDKTLKL***ubiquitination[1]
Reference
 [1] 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]
 [2] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [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] 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] 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] 
Functional Description
 Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism (By similarity). May be involved in translocation of long-chain fatty acids (LFCA) across membranes. 
Sequence Annotation
 NP_BIND 222 233 AMP (Potential).
 MOD_RES 291 291 N6-acetyllysine.
 MOD_RES 325 325 N6-acetyllysine.
 MOD_RES 577 577 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 620 AA 
Protein Sequence
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RYFLRLANMA RRVRSYRQRR PVRTILRAFL 60
EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDQLG LRQGDCVALF MGNEPAYVWI 120
WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPD LQEAVEEVLP TLKKDAVSVF 180
YVSRTSNTNG VDTILDKVDG VSAEPTPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH 240
RLWYGTGLAM SSGITAQDVI YTTMPLYHSA ALMIGLHGCI VVGATLALRS KFSASQFWDD 300
CRKYNVTVIQ YIGELLRYLC NTPQKPNDRD HKVKKALGNG LRGDVWREFI KRFGDIHVYE 360
FYASTEGNIG FVNYPRKIGA VGRANYLQRK VARYELIKYD VEKDEPVRDA NGYCIKVPKG 420
EVGLLVCKIT QLTPFIGYAG GKTQTEKKKL RDVFKKGDIY FNSGDLLMID RENFVYFHDR 480
VGDTFRWKGE NVATTEVADI VGLVDFVEEV NVYGVPVPGH EGRIGMASLK IKENYEFNGK 540
KLFQHIAEYL PSYARPRFLR IQDTIEITGT FKHRKVTLME EGFNPTVIKD TLYFMDDAEK 600
TFVPMTENIY NAIIDKTLKL 620 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:Compara.
 GO:0005779; C:integral to peroxisomal membrane; ISS:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0015245; F:fatty acid transporter activity; IDA:MGI.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
 GO:0050197; F:phytanate-CoA ligase activity; IEA:Compara.
 GO:0070251; F:pristanate-CoA ligase activity; IEA:Compara.
 GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
 GO:0006699; P:bile acid biosynthetic process; IEA:Compara.
 GO:0001561; P:fatty acid alpha-oxidation; IEA:Compara.
 GO:0006635; P:fatty acid beta-oxidation; IEA:Compara.
 GO:0044539; P:long-chain fatty acid import; IEA:Compara.
 GO:0097089; P:methyl-branched fatty acid metabolic process; IEA:Compara.
 GO:0042760; P:very long-chain fatty acid catabolic process; IMP:MGI. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS