DECR_RAT
ID DECR_RAT Reviewed; 335 AA.
AC Q64591; Q6PCV4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial;
DE EC=1.3.1.124 {ECO:0000250|UniProtKB:Q16698};
DE AltName: Full=2,4-dienoyl-CoA reductase [NADPH];
DE Short=4-enoyl-CoA reductase [NADPH];
DE Flags: Precursor;
GN Name=Decr1; Synonyms=Decr;
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], PROTEIN SEQUENCE OF 35-53, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=2383590; DOI=10.1016/0167-4781(90)90109-f;
RA Hirose A., Kamijo K., Osumi T., Hashimoto T., Mizugaki M.;
RT "cDNA cloning of rat liver 2,4-dienoyl-CoA reductase.";
RL Biochim. Biophys. Acta 1049:346-349(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the
CC metabolism of unsaturated fatty enoyl-CoA esters having double bonds in
CC both even- and odd-numbered positions in mitochondria. Catalyzes the
CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
CC {ECO:0000250|UniProtKB:Q16698}.
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:0000250|UniProtKB:Q16698};
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:0000250|UniProtKB:Q16698};
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:0000250|UniProtKB:Q16698};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q16698}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:2383590}.
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; D00569; BAA00446.1; -; mRNA.
DR EMBL; BC059120; AAH59120.1; -; mRNA.
DR PIR; S11021; S11021.
DR RefSeq; NP_476545.2; NM_057197.2.
DR AlphaFoldDB; Q64591; -.
DR SMR; Q64591; -.
DR BioGRID; 250758; 2.
DR IntAct; Q64591; 2.
DR STRING; 10116.ENSRNOP00000011330; -.
DR iPTMnet; Q64591; -.
DR PhosphoSitePlus; Q64591; -.
DR jPOST; Q64591; -.
DR PaxDb; Q64591; -.
DR PRIDE; Q64591; -.
DR GeneID; 117543; -.
DR KEGG; rno:117543; -.
DR UCSC; RGD:70999; rat.
DR CTD; 1666; -.
DR RGD; 70999; Decr1.
DR eggNOG; KOG0725; Eukaryota.
DR InParanoid; Q64591; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q64591; -.
DR BRENDA; 1.3.1.124; 5301.
DR Reactome; R-RNO-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR PRO; PR:Q64591; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0070402; F:NADPH binding; ISO:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Fatty acid metabolism;
KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:2383590"
FT CHAIN 35..335
FT /note="2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-
FT producing], mitochondrial"
FT /id="PRO_0000031967"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 66..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 240..243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 42
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 49
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT MOD_RES 73
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 106
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 106
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 244
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 244
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 260
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 319
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT MOD_RES 319
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ62"
FT CONFLICT 11
FT /note="G -> R (in Ref. 2; AAH59120)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="R -> K (in Ref. 1; BAA00446)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="L -> R (in Ref. 1; BAA00446)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="K -> R (in Ref. 1; BAA00446)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> V (in Ref. 1; BAA00446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36133 MW; C4386C65E49A4D2F CRC64;
MALLARAFFA GVSRLPCDPG PQRFFSFGTK TLYQSIDAPQ SKFFPPILKP MLPPNAFQGK
VAFITGGGTG LGKAMTTFLS SLGAQCVIAS RNIDVLKATA EEITSKTGNK VYAIRCDVRD
PDMVHNTVLE LIKVAGHPDV VINNAAGNFI SPSERLSPNG WKTITDIVLN GTAYVTIEIG
KQLIKAQKGA AFLAITTIYA ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP
GPIKTKGAFS RLDPTGKFEK DMIERIPCGR LGTVEELANL ATFLCSDYAS WINGAVIRFD
GGEEVFLSGE FNSLKKVTKE EWDVIEGLIR KTKGS
