UniProt Accession

 DECR2_MOUSE; Q9WV68 

Genbank Protein ID

 AF155575; BC021865 

Genbank Nucleotide ID

 AAD38196.1; AAH21865.1 

Protein Name

 Peroxisomal 2,4-dienoyl-CoA reductase 

Protein Synonyms/Alias

 2,4-dienoyl-CoA reductase 2 

Gene Name

 Decr2 

Gene Synonyms/Alias

 Pdcr 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
64	IVGRSLQKVTTAAKK	acetylation	[1, 2, 3, 4]
78	KLVAATGKRCLPLSM	acetylation	[2]
228	RGSNASSKLKHFSNP	acetylation	[2, 3, 4]
230	SNASSKLKHFSNPIP	acetylation	[3]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 

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 (By similarity).
 NP_BIND 60 64 NADP (By similarity).
 NP_BIND 208 214 NADP (By similarity).
 REGION 126 128 Substrate binding (By similarity).
 MOTIF 290 292 Microbody targeting signal (By
 BINDING 60 60 Substrate (By similarity).
 BINDING 86 86 NADP (By similarity).
 BINDING 88 88 Substrate (By similarity).
 BINDING 118 118 Substrate (By similarity).
 BINDING 182 182 NADP (By similarity).
 BINDING 219 219 Substrate (By similarity).
 MOD_RES 151 151 N6-acetyllysine (By similarity).
 MOD_RES 291 291 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; 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

Gene Ontology

 GO:0005778; C:peroxisomal membrane; IEA:Compara.
 GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
 GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:Compara.
 GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:UniProtKB. 

Interpro

 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom. 

Pfam

  

SMART

  

PROSITE

 PS00061; ADH_SHORT 

PRINTS

 PR00081; GDHRDH.