CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022155
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal 2,4-dienoyl-CoA reductase 
Protein Synonyms/Alias
 pDCR; 2,4-dienoyl-CoA reductase 2 
Gene Name
 DECR2 
Gene Synonyms/Alias
 PDCR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29CPDLLRDKVAFITGGubiquitination[1]
151VSRVLYEKFFRDHGGacetylation[2]
291DFASFSAKL******acetylation[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. 
Sequence Annotation
 NP_BIND 35 40 NADP.
 NP_BIND 60 64 NADP.
 NP_BIND 208 214 NADP.
 REGION 126 128 Substrate binding.
 MOTIF 290 292 Microbody targeting signal (By
 BINDING 60 60 Substrate.
 BINDING 86 86 NADP.
 BINDING 88 88 Substrate.
 BINDING 118 118 Substrate.
 BINDING 182 182 NADP.
 BINDING 219 219 Substrate.
 MOD_RES 151 151 N6-acetyllysine.
 MOD_RES 291 291 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Fatty acid metabolism; Lipid metabolism; NADP; Oxidoreductase; Peroxisome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 292 AA 
Protein Sequence
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR HGCHTVIASR 60
SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAVMAAVDQA LKEFGRIDIL INCAAGNFLC 120
PAGALSFNAF KTVMDIDTSG TFNVSRVLYE KFFRDHGGVI VNITATLGNR GQALQVHAGS 180
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG 240
NKTEIAHSVL YLASPLASYV TGAVLVADGG AWLTFPNGVK GLPDFASFSA KL 292 
Gene Ontology
 GO:0005778; C:peroxisomal membrane; IEA:Compara.
 GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
 GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
 GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom. 
Pfam
  
SMART
  
PROSITE
 PS00061; ADH_SHORT 
PRINTS
 PR00081; GDHRDH.
 PR00080; SDRFAMILY.