CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004444
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxylesterase 1D 
Protein Synonyms/Alias
 Carboxyesterase ES-10; Carboxylesterase 3; ES-HVEL; Fatty acid ethyl ester synthase; FAEE synthase; Liver carboxylesterase 10; pI 6.1 esterase 
Gene Name
 Ces1d 
Gene Synonyms/Alias
 Ces3 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
304SLKLNLFKLDLLGNPacetylation[1]
338PEEILAEKSFNTVPYacetylation[1]
540AAQRLKDKEVAFWSEacetylation[1]
Reference
 [1] 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
 Major lipase in white adipose tissue (By similarity). 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
MRLYPLVWLF LAACTAWGYP SSPPVVNTVK GKVLGKYVNL EGFAQPVAVF LGIPFAKPPL 60
GSLRFAPPQP AEPWNFVKNT TSYPPMCSQD AVGGQVLSEL FTNRKENIPL QFSEDCLYLN 120
VYTPADLTKN SRLPVMVWIH GGGLVVGGAS TYDGQVLSAH ENVVVVTIQY RLGIWGFFST 180
GDEHSQGNWG HLDQVAALHW VQDNIANFGG NPGSVTIFGE SAGGFSVSAL VLSPLAKNLF 240
HRAISESGVV LTSALITTDS KPIANLIATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL 300
NLFKLDLLGN PKESYPFLPT VIDGVVLPKT PEEILAEKSF NTVPYIVGIN KQEFGWIIPT 360
LMGYPLSEGK LDQKTAKSLL WKSYPTLKIS EKMIPVVAEK YFGGTDDPAK RKDLFQDLVA 420
DVMFGVPSVM VSRSHRDAGA PTFMYEFEYR PSFVSAMRPK TVIGDHGDEL FSVFGSPFLK 480
DGASEEETNL SKMVMKYWAN FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK 540
EVAFWSELRA KEAAEEPSHW KHVEL 565 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
 GO:0005811; C:lipid particle; ISS:UniProtKB.
 GO:0004091; F:carboxylesterase activity; IMP:RGD.
 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; ISS:UniProtKB.
 GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
 GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB. 
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