DECR2_MOUSE
ID DECR2_MOUSE Reviewed; 292 AA.
AC Q9WV68;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing];
DE EC=1.3.1.124 {ECO:0000269|PubMed:10464321};
DE AltName: Full=2,4-dienoyl-CoA reductase 2;
GN Name=Decr2; Synonyms=Pdcr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10464321; DOI=10.1074/jbc.274.36.25814;
RA Geisbrecht B.V., Liang X., Morrell J.C., Schulz H., Gould S.J.;
RT "The mouse gene PDCR encodes a peroxisomal delta(2), delta(4)-dienoyl-CoA
RT reductase.";
RL J. Biol. Chem. 274:25814-25820(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the
CC degradation of unsaturated fatty enoyl-CoA esters having double bonds
CC in both even- and odd-numbered positions in peroxisome. Catalyzes the
CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
CC Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also
CC towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does
CC not constitute a rate limiting step in the peroxisomal degradation of
CC docosahexaenoic acid. {ECO:0000269|PubMed:10464321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000269|PubMed:10464321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000269|PubMed:10464321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4E)-hexadienoyl-CoA + H(+) + NADPH = (3E)-hexenoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:44912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84788, ChEBI:CHEBI:84790;
CC Evidence={ECO:0000269|PubMed:10464321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4E)-decadienoyl-CoA + H(+) + NADPH = (3E)-decenoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:44916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62244, ChEBI:CHEBI:84793;
CC Evidence={ECO:0000269|PubMed:10464321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4Z,7Z,10Z,13Z,16Z,19Z)-docosaheptaenoyl-CoA + H(+) + NADPH
CC = (3E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77559, ChEBI:CHEBI:84791;
CC Evidence={ECO:0000269|PubMed:10464321};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=108 uM for 2,4-hexadienoyl-CoA {ECO:0000269|PubMed:10464321};
CC KM=6 uM for 2,4-decadienoyl-CoA {ECO:0000269|PubMed:10464321};
CC KM=155 uM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA
CC {ECO:0000269|PubMed:10464321};
CC Vmax=8 nmol/min/mg enzyme with 2,4-hexadienoyl-CoA as substrate
CC {ECO:0000269|PubMed:10464321};
CC Vmax=20 nmol/min/mg enzyme with 2,4-decadienoyl-CoA as substrate
CC {ECO:0000269|PubMed:10464321};
CC Vmax=5 nmol/min/mg enzyme with 2,4,7,10,13,16,19-docosaheptaenoyl-CoA
CC as substrate {ECO:0000269|PubMed:10464321};
CC -!- SUBUNIT: Monomer, dimer and oligomer. {ECO:0000250|UniProtKB:Q9NUI1}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10464321}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
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DR EMBL; AF155575; AAD38196.1; -; mRNA.
DR EMBL; BC021865; AAH21865.1; -; mRNA.
DR CCDS; CCDS28543.1; -.
DR RefSeq; NP_036063.1; NM_011933.2.
DR AlphaFoldDB; Q9WV68; -.
DR SMR; Q9WV68; -.
DR BioGRID; 204936; 1.
DR STRING; 10090.ENSMUSP00000045621; -.
DR iPTMnet; Q9WV68; -.
DR PhosphoSitePlus; Q9WV68; -.
DR SwissPalm; Q9WV68; -.
DR jPOST; Q9WV68; -.
DR MaxQB; Q9WV68; -.
DR PaxDb; Q9WV68; -.
DR PRIDE; Q9WV68; -.
DR ProteomicsDB; 277975; -.
DR Antibodypedia; 34897; 152 antibodies from 27 providers.
DR DNASU; 26378; -.
DR Ensembl; ENSMUST00000040907; ENSMUSP00000045621; ENSMUSG00000036775.
DR GeneID; 26378; -.
DR KEGG; mmu:26378; -.
DR UCSC; uc008bdg.1; mouse.
DR CTD; 26063; -.
DR MGI; MGI:1347059; Decr2.
DR VEuPathDB; HostDB:ENSMUSG00000036775; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q9WV68; -.
DR OMA; GSICSAQ; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q9WV68; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.124; 3474.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9WV68; -.
DR BioGRID-ORCS; 26378; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Decr2; mouse.
DR PRO; PR:Q9WV68; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WV68; protein.
DR Bgee; ENSMUSG00000036775; Expressed in dorsal pancreas and 232 other tissues.
DR ExpressionAtlas; Q9WV68; baseline and differential.
DR Genevisible; Q9WV68; MM.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISO:MGI.
DR GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PTHR43296; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Fatty acid metabolism; Lipid metabolism; NADP; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT CHAIN 2..292
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054560"
FT MOTIF 290..292
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 35..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 208..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUI1"
SQ SEQUENCE 292 AA; 31300 MW; E25ED366830CC6AB CRC64;
MAQPPPDVEG DDCLPEYHHL FCPDLLQDKV AFITGGGSGI GFRIAEIFMR HGCHTVIVGR
SLQKVTTAAK KLVAATGKRC LPLSMDVRVP PEVMTAVDQA LQEFGKINIL INCAAGNFLC
PASALSFNAF KTVVDIDTIG TFNVSSVLYK KFFRDHGGVI VNITATLSMR GQVLQLHAGA
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGA ISGTEGLRRL RGSNASSKLK HFSNPIPRLG
TKTEIAHSVL YLASPLASYV SGIVLVVDGG SWMTFPNGIK QLLEFESFSA KL
