CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018146
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxylesterase 1D 
Protein Synonyms/Alias
 Carboxylesterase 3; Fatty acid ethyl ester synthase; FAEE synthase; Triacylglycerol hydrolase; TGH 
Gene Name
 Ces1d 
Gene Synonyms/Alias
 Ces1; Ces3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
288MVHCLRQKTEDELLEacetylation[1, 2]
299ELLETSLKLNLFKLDacetylation[2]
304SLKLNLFKLDLLGNPubiquitination[3]
338PEEILAEKSFSTVPYubiquitination[3]
382TANSLLWKSYPTLKIacetylation[4]
382TANSLLWKSYPTLKIsuccinylation[4]
400MIPVVAEKYLGGTDDacetylation[2, 5]
400MIPVVAEKYLGGTDDubiquitination[3]
521HWPEYDQKEGYLKIGacetylation[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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
 Major lipase in white adipose tissue. Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. 
Sequence Annotation
 MOTIF 562 565 Prevents secretion from ER (Potential).
 ACT_SITE 221 221 Acyl-ester intermediate (By similarity).
 ACT_SITE 353 353 Charge relay system (By similarity).
 ACT_SITE 466 466 Charge relay system (By similarity).
 CARBOHYD 79 79 N-linked (GlcNAc...) (By similarity).
 CARBOHYD 489 489 N-linked (GlcNAc...) (Potential).
 DISULFID 87 116 By similarity.
 DISULFID 273 284 By similarity.  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Reference proteome; Serine esterase; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 565 AA 
Protein Sequence
MGLYPLIWLS LAACTAWGYP SSPPVVNTVK GKVLGKYVNL EGFTQPVAVF LGVPFAKPPL 60
GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD AVGGQVLSEL FTNRKENIPL QFSEDCLYLN 120
IYTPADLTKN SRLPVMVWIH GGGLVVGGAS TYDGLALSAH ENVVVVTIQY RLGIWGFFST 180
GDEHSRGNWG HLDQVAALRW VQDNIANFGG NPGSVTIFGE SAGGFSVSVL VLSPLAKNLF 240
HRAISESGVS LTAALITTDV KPIAGLVATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL 300
NLFKLDLLGN PKESYPFLPT VIDGVVLPKA PEEILAEKSF STVPYIVGIN KQEFGWIIPT 360
LMGYPLAEGK LDQKTANSLL WKSYPTLKIS ENMIPVVAEK YLGGTDDLTK KKDLFQDLMA 420
DVVFGVPSVI VSRSHRDAGA STYMYEFEYR PSFVSAMRPK AVIGDHGDEI FSVFGSPFLK 480
DGASEEETNL SKMVMKFWAN FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK 540
EVSFWAELRA KESAQRPSHR EHVEL 565 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
 GO:0005811; C:lipid particle; IDA:UniProtKB.
 GO:0004091; F:carboxylesterase activity; IDA:UniProtKB.
 GO:0030339; F:fatty-acyl-ethyl-ester synthase activity; IEA:EC.
 GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:EC.
 GO:0080032; F:methyl jasmonate esterase activity; IEA:EC.
 GO:0080031; F:methyl salicylate esterase activity; IEA:EC.
 GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC.
 GO:0004771; F:sterol esterase activity; IDA:UniProtKB.
 GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
 GO:0006637; P:acyl-CoA metabolic process; TAS:ProtInc.
 GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
 GO:0009636; P:response to toxic substance; TAS:ProtInc.
 GO:0019626; P:short-chain fatty acid catabolic process; IDA:MGI.
 GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:MGI. 
Interpro
 IPR002018; CarbesteraseB.
 IPR019826; Carboxylesterase_B_AS.
 IPR019819; Carboxylesterase_B_CS. 
Pfam
 PF00135; COesterase 
SMART
  
PROSITE
 PS00122; CARBOXYLESTERASE_B_1
 PS00941; CARBOXYLESTERASE_B_2 
PRINTS