DECR2_RAT
ID DECR2_RAT Reviewed; 292 AA.
AC Q9Z2M4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing];
DE EC=1.3.1.124 {ECO:0000269|PubMed:10333503, ECO:0000269|PubMed:11514237};
DE AltName: Full=2,4-dienoyl-CoA reductase 2;
DE AltName: Full=DCR-AKL;
DE AltName: Full=pVI-AKL;
GN Name=Decr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=10333503; DOI=10.1042/bj3400561;
RA Fransen M., Van Veldhoven P.P., Subramani S.;
RT "Identification of peroxisomal proteins by using M13 phage protein VI phage
RT display: molecular evidence that mammalian peroxisomes contain a 2,4-
RT dienoyl-CoA reductase.";
RL Biochem. J. 340:561-568(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11514237; DOI=10.1016/s1388-1981(01)00141-x;
RA De Nys K., Meyhi E., Mannaerts G.P., Fransen M., Van Veldhoven P.P.;
RT "Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase.";
RL Biochim. Biophys. Acta 1533:66-72(2001).
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:10333503,
CC ECO:0000269|PubMed:11514237}.
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:10333503, ECO:0000269|PubMed:11514237};
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:10333503, ECO:0000269|PubMed:11514237};
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:11514237};
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:11514237};
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:11514237};
CC -!- SUBUNIT: Monomer, dimer and oligomer. {ECO:0000250|UniProtKB:Q9NUI1}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10333503}.
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; AF044574; AAD02333.1; -; mRNA.
DR EMBL; BC070959; AAH70959.1; -; mRNA.
DR RefSeq; NP_741993.1; NM_171996.3.
DR RefSeq; XP_006246086.1; XM_006246024.3.
DR AlphaFoldDB; Q9Z2M4; -.
DR SMR; Q9Z2M4; -.
DR IntAct; Q9Z2M4; 5.
DR STRING; 10116.ENSRNOP00000027518; -.
DR SwissLipids; SLP:000001051; -.
DR iPTMnet; Q9Z2M4; -.
DR PhosphoSitePlus; Q9Z2M4; -.
DR PaxDb; Q9Z2M4; -.
DR PRIDE; Q9Z2M4; -.
DR Ensembl; ENSRNOT00000027518; ENSRNOP00000027518; ENSRNOG00000032152.
DR GeneID; 64461; -.
DR KEGG; rno:64461; -.
DR UCSC; RGD:71002; rat.
DR CTD; 26063; -.
DR RGD; 71002; Decr2.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q9Z2M4; -.
DR OMA; GSICSAQ; -.
DR OrthoDB; 1105725at2759; -.
DR BRENDA; 1.3.1.124; 5301.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR PRO; PR:Q9Z2M4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000050424; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; Q9Z2M4; baseline and differential.
DR Genevisible; Q9Z2M4; RN.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA: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:RGD.
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; ISO:RGD.
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 PRINTS; PR00080; SDRFAMILY.
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 CHAIN 1..292
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054562"
FT MOTIF 290..292
FT /note="Microbody targeting signal"
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 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; 31292 MW; B969DC35647DD844 CRC64;
MTQQPPDVEE DDCLSEYHHL FCPDLLQDKV AFITGGGSGI GFRIAEIFMR HGCHTVIVSR
SLPRVSEAAK KLVAATGKRC LPLSMDVRVP PAVMAAVDQA LKEFGKIDIL INCAAGNFLC
PASALSFNAF KTVVDIDTLG TFNVSRVLYE KFFRDHGGVI VNITATLSMR GQVLQLHAGA
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGA ISGTEGLRRL GGPKASSKFK YLSSPIPRLG
TKTEIAHSVL YLASPLASYV SGIVLVVDGG SWMTLPNDIG RLLEFESSSA KL
