Tag | Content |
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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 |
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29 | CPDLLRDKVAFITGG | ubiquitination | [1] | 151 | VSRVLYEKFFRDHGG | acetylation | [2] | 291 | DFASFSAKL****** | acetylation | [2] |
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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. |
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