CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 5 
Protein Synonyms/Alias
 Long-chain acyl-CoA synthetase 5; LACS 5 
Gene Name
 Acsl5 
Gene Synonyms/Alias
 Facl5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
62ARRGAFQKNNDLILYubiquitination[1]
109PYKWISYKQVSDRAEubiquitination[1]
200MLVENVEKGLTPGLKubiquitination[1]
221PFDDDLMKRGEKCGVubiquitination[1]
225DLMKRGEKCGVEMLSubiquitination[1]
245NIGKENFKKPVPPKPacetylation[2]
341RLLPDDMKALKPTVFacetylation[2, 3]
344PDDMKALKPTVFPTVacetylation[2, 3]
344PDDMKALKPTVFPTVubiquitination[1]
361LLNRVYDKVQNEAKTacetylation[2, 3, 4, 5]
361LLNRVYDKVQNEAKTubiquitination[1]
367DKVQNEAKTPLKKFLacetylation[3]
367DKVQNEAKTPLKKFLubiquitination[1]
399RRDSLWDKLVFSKIQubiquitination[1]
404WDKLVFSKIQGSLGGubiquitination[1]
412IQGSLGGKVRLMITGubiquitination[1]
502IKGNNVFKGYLKDPEubiquitination[1]
510GYLKDPEKTQEVLDKubiquitination[1]
517KTQEVLDKDGWLHTGubiquitination[1]
536WLPNGTLKIVDRKKNubiquitination[1]
546DRKKNIFKLAQGEYIubiquitination[1]
557GEYIAPEKIENVYSRacetylation[2]
557GEYIAPEKIENVYSRubiquitination[1]
603FAAKIGVKGSFEELCubiquitination[1]
611GSFEELCKNQCVKEAacetylation[3]
611GSFEELCKNQCVKEAubiquitination[1]
616LCKNQCVKEAILEDLubiquitination[1]
625AILEDLQKIGKEGGLacetylation[6]
625AILEDLQKIGKEGGLubiquitination[1]
628EDLQKIGKEGGLKSFacetylation[2]
639LKSFEQVKSIFVHPEubiquitination[1]
668AKRVELAKFFQTQIKubiquitination[1]
675KFFQTQIKSLYESIEubiquitination[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] 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]
 [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] 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] 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]
 [6] 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] 
Functional Description
 Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity). May have a role in the survival of glioma cells (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 683 AA 
Protein Sequence
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF 60
QKNNDLILYY FSDAKTLYEN FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS 120
CLLHKGYKSS QDQFVGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGTEA IIFVINRADI 180
PVVICDTPQK ATMLVENVEK GLTPGLKTII LMDPFDDDLM KRGEKCGVEM LSLHDAENIG 240
KENFKKPVPP KPEDLSVICF TSGTTGDPKG AMLTHENVVS NMAAFLKFLE PIFQPTSDDV 300
TISYLPLAHM FERLVQGILF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD 360
KVQNEAKTPL KKFLLNLAII SKFNEVKNGI IRRDSLWDKL VFSKIQGSLG GKVRLMITGA 420
APISTPVLTF FRAAMGCWVF EAYGQTECTG GCSITSPGDW TAGHVGTPVA CNFVKLEDVA 480
DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIVDR 540
KKNIFKLAQG EYIAPEKIEN VYSRSRPVLQ VFVHGESLRS FLIGVVVPDP DSLPSFAAKI 600
GVKGSFEELC KNQCVKEAIL EDLQKIGKEG GLKSFEQVKS IFVHPEPFTI ENGLLTPTLK 660
AKRVELAKFF QTQIKSLYES IEE 683 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:EC.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS