CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020978
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal carnitine O-octanoyltransferase 
Protein Synonyms/Alias
 COT 
Gene Name
 Crot 
Gene Synonyms/Alias
 Cot 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33PALEESLKKYLESVKubiquitination[1]
34ALEESLKKYLESVKPubiquitination[1]
40KKYLESVKPFANEDEacetylation[2]
40KKYLESVKPFANEDEsuccinylation[2]
40KKYLESVKPFANEDEubiquitination[1]
49FANEDEYKKTEEIVQacetylation[3]
50ANEDEYKKTEEIVQKubiquitination[1]
57KTEEIVQKFQEGAGKacetylation[2]
57KTEEIVQKFQEGAGKsuccinylation[2]
57KTEEIVQKFQEGAGKubiquitination[1]
69AGKRLHQKLLERARGubiquitination[1]
143WQLLRREKLPVHKSGacetylation[4]
148REKLPVHKSGNTPLDubiquitination[1]
167RMLFSTCKVPGITRDubiquitination[1]
181DSIMNYFKTESEGHCacetylation[2]
181DSIMNYFKTESEGHCsuccinylation[2]
226RQLTYIHKKCSNEPVacetylation[4]
227QLTYIHKKCSNEPVGubiquitination[1]
384LNDVSQAKAQHLKAAacetylation[2]
384LNDVSQAKAQHLKAAsuccinylation[2]
384LNDVSQAKAQHLKAAubiquitination[1]
406STFTSFGKKLTKEEAacetylation[2, 4, 5]
406STFTSFGKKLTKEEAsuccinylation[2]
406STFTSFGKKLTKEEAubiquitination[1]
482SLLERQQKMLEAFAKacetylation[2]
482SLLERQQKMLEAFAKsuccinylation[2]
482SLLERQQKMLEAFAKubiquitination[1]
489KMLEAFAKHNKMMKDubiquitination[1]
495AKHNKMMKDCSHGKGacetylation[2, 3, 4, 6]
501MKDCSHGKGFDRHLLacetylation[4]
501MKDCSHGKGFDRHLLubiquitination[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] 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] 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]
 [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] 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
Functional Description
 Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate (By similarity). 
Sequence Annotation
 REGION 405 417 Coenzyme A binding (By similarity).
 MOTIF 610 612 Microbody targeting signal (Potential).
 ACT_SITE 327 327 Proton acceptor (By similarity).
 BINDING 439 439 Carnitine (By similarity).
 BINDING 442 442 Coenzyme A (By similarity).
 BINDING 452 452 Carnitine (By similarity).
 BINDING 505 505 Carnitine (By similarity).
 MOD_RES 495 495 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Acyltransferase; Complete proteome; Fatty acid metabolism; Lipid metabolism; Peroxisome; Reference proteome; Transferase; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 612 AA 
Protein Sequence
MENQLTKSVE ERTFQYQDSL PSLPVPALEE SLKKYLESVK PFANEDEYKK TEEIVQKFQE 60
GAGKRLHQKL LERARGKRNW LEEWWLNVAY LDVRIPSQLN VNFVGPCPHF EHYWPAREGT 120
QLERGSMMLW HNLNYWQLLR REKLPVHKSG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF 180
KTESEGHCPT HIAVLCRGRA FVFDVLHEGC LITPPELLRQ LTYIHKKCSN EPVGPSIAAL 240
TSEERTRWAK AREYLISLDP ENLTLLEKIQ TSLFVYSIED SSPHATPEEY SQVFEMLLGG 300
DPSVRWGDKS YNLISFANGI FGCCCDHAPY DAMVMVNIAH YVDERVLETE GRWKGSEKVR 360
DIPLPEELVF TVDEKILNDV SQAKAQHLKA ASDLQIAAST FTSFGKKLTK EEALHPDTFI 420
QLALQLAYYR LHGRPGCCYE TAMTRYFYHG RTETVRSCTV EAVRWCQSMQ DPSASLLERQ 480
QKMLEAFAKH NKMMKDCSHG KGFDRHLLGL LLIAKEEGLP VPELFEDPLF SRSGGGGNFV 540
LSTSLVGYLR VQGVVVPMVH NGYGFFYHIR DDRFVVACSS WRSCPETDAE KLVQMIFHAF 600
HDMIQLMNTA HL 612 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005777; C:peroxisome; IDA:MGI.
 GO:0008458; F:carnitine O-octanoyltransferase activity; IDA:MGI.
 GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
 GO:0015908; P:fatty acid transport; IDA:MGI. 
Interpro
 IPR000542; Carn_acyl_trans. 
Pfam
 PF00755; Carn_acyltransf 
SMART
  
PROSITE
 PS00439; ACYLTRANSF_C_1
 PS00440; ACYLTRANSF_C_2 
PRINTS