DECR_MOUSE
ID DECR_MOUSE Reviewed; 335 AA.
AC Q9CQ62; Q9DCI7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
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;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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-106, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-42; LYS-49; LYS-73; LYS-97; LYS-106; LYS-244; LYS-260 AND
RP LYS-319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-49; LYS-97; LYS-106;
RP LYS-244; LYS-260; LYS-315 AND LYS-319, 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. 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:0000250|UniProtKB:Q16698}.
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; AK002756; BAB22333.1; -; mRNA.
DR EMBL; AK004725; BAB23508.1; -; mRNA.
DR EMBL; AK015692; BAB29933.1; -; mRNA.
DR EMBL; BC046972; AAH46972.1; -; mRNA.
DR CCDS; CCDS17985.1; -.
DR RefSeq; NP_080448.1; NM_026172.3.
DR AlphaFoldDB; Q9CQ62; -.
DR SMR; Q9CQ62; -.
DR BioGRID; 212204; 29.
DR IntAct; Q9CQ62; 5.
DR STRING; 10090.ENSMUSP00000029877; -.
DR iPTMnet; Q9CQ62; -.
DR PhosphoSitePlus; Q9CQ62; -.
DR EPD; Q9CQ62; -.
DR jPOST; Q9CQ62; -.
DR MaxQB; Q9CQ62; -.
DR PaxDb; Q9CQ62; -.
DR PRIDE; Q9CQ62; -.
DR ProteomicsDB; 279398; -.
DR Antibodypedia; 12737; 274 antibodies from 28 providers.
DR DNASU; 67460; -.
DR Ensembl; ENSMUST00000029877; ENSMUSP00000029877; ENSMUSG00000028223.
DR GeneID; 67460; -.
DR KEGG; mmu:67460; -.
DR UCSC; uc008sbm.1; mouse.
DR CTD; 1666; -.
DR MGI; MGI:1914710; Decr1.
DR VEuPathDB; HostDB:ENSMUSG00000028223; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q9CQ62; -.
DR OMA; FPTKGAW; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q9CQ62; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.124; 3474.
DR Reactome; R-MMU-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR BioGRID-ORCS; 67460; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Decr1; mouse.
DR PRO; PR:Q9CQ62; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CQ62; protein.
DR Bgee; ENSMUSG00000028223; Expressed in heart right ventricle and 248 other tissues.
DR ExpressionAtlas; Q9CQ62; baseline and differential.
DR Genevisible; Q9CQ62; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP: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; Fatty acid metabolism; Lipid metabolism; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..335
FT /note="2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-
FT producing], mitochondrial"
FT /id="PRO_0000031966"
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 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:0007744|PubMed:23576753"
FT MOD_RES 42
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 49
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16698"
FT MOD_RES 73
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 106
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 106
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 244
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 260
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 319
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 319
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 203
FT /note="G -> V (in Ref. 1; BAB22333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36214 MW; C064AC03F818E25A CRC64;
MALLGRAFFA GVSRLPCDPG PQRFFSFGTK TLYQSKDAPQ SKFFQPVLKP MLPPDAFQGK
VAFITGGGTG LGKAMTTFLS TLGAQCVIAS RNIDVLKATA EEISSKTGNK VHAIRCDVRD
PDMVHNTVLE LIKVAGHPDV VINNAAGNFI SPSERLTPNG WKTITDIVLN GTAYVTLEIG
KQLIKAQKGA AFLAITTIYA ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP
GPIKTKGAFS RLDPTGRFEK EMIDRIPCGR LGTMEELANL ATFLCSDYAS WINGAVIRFD
GGEEVFLSGE FNSLKKVTKE EWDIIEGLIR KTKGS
