DECR_HUMAN
ID DECR_HUMAN Reviewed; 335 AA.
AC Q16698; B7Z6B8; Q2M304; Q93085;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial;
DE EC=1.3.1.124 {ECO:0000269|PubMed:15531764};
DE AltName: Full=2,4-dienoyl-CoA reductase [NADPH];
DE Short=4-enoyl-CoA reductase [NADPH];
DE AltName: Full=Short chain dehydrogenase/reductase family 18C member 1;
DE Flags: Precursor;
GN Name=DECR1; Synonyms=DECR, SDR18C1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=7818482; DOI=10.1042/bj3040787;
RA Koivuranta K.T., Hakkola E.H., Hiltunen J.K.;
RT "Isolation and characterization of cDNA for human 120 kDa mitochondrial
RT 2,4-dienoyl-coenzyme A reductase.";
RL Biochem. J. 304:787-792(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Ding J.H., Yang B.Z., Roe C.R.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9403065; DOI=10.1006/geno.1997.5004;
RA Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J.,
RA Palotie A., Hiltunen J.K.;
RT "Molecular cloning and characterization of the human mitochondrial 2,4-
RT dienoyl-CoA reductase gene (DECR).";
RL Genomics 46:112-119(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pericardium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INVOLVEMENT IN DECRD.
RX PubMed=24847004; DOI=10.1093/hmg/ddu218;
RA Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H.,
RA Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P.,
RA Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.;
RT "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes
RT dienoyl-CoA reductase deficiency with hyperlysinemia.";
RL Hum. Mol. Genet. 23:5009-5016(2014).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND
RP SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214, AND FUNCTION.
RX PubMed=15531764; DOI=10.1074/jbc.m411069200;
RA Alphey M.S., Yu W., Byres E., Li D., Hunter W.N.;
RT "Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase:
RT enzyme-ligand interactions in a distinctive short-chain reductase active
RT site.";
RL J. Biol. Chem. 280:3068-3077(2005).
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:0000269|PubMed:15531764}.
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:15531764};
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:15531764};
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:15531764};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 uM for NADPH {ECO:0000269|PubMed:15531764};
CC KM=14.3 uM for trans-2,trans-4-hexadienoyl-CoA
CC {ECO:0000269|PubMed:15531764};
CC Vmax=30.3 umol/min/mg enzyme {ECO:0000269|PubMed:15531764};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15531764}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7818482}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16698-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16698-2; Sequence=VSP_056388;
CC -!- TISSUE SPECIFICITY: Heart = liver = pancreas > kidney >> skeletal
CC muscle = lung. {ECO:0000269|PubMed:7818482}.
CC -!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A
CC rare, autosomal recessive, inborn error of polyunsaturated fatty acids
CC and lysine metabolism, resulting in mitochondrial dysfunction. Affected
CC individuals have a severe encephalopathy with neurologic and metabolic
CC abnormalities beginning in early infancy. Laboratory studies show
CC increased C10:2 carnitine levels and hyperlysinemia.
CC {ECO:0000269|PubMed:24847004}. Note=The protein represented in this
CC entry is involved in disease pathogenesis. A selective decrease in
CC mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency
CC of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.
CC {ECO:0000269|PubMed:24847004}.
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; L26050; AAA67551.1; -; mRNA.
DR EMBL; U49352; AAB09423.1; -; mRNA.
DR EMBL; U78302; AAB88724.1; -; Genomic_DNA.
DR EMBL; U94980; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94981; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94982; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94983; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94984; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94985; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94986; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; U94987; AAB88724.1; JOINED; Genomic_DNA.
DR EMBL; AK300069; BAH13204.1; -; mRNA.
DR EMBL; AC004612; AAC14671.1; -; Genomic_DNA.
DR EMBL; AF049895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105080; AAI05081.1; -; mRNA.
DR EMBL; BC105082; AAI05083.1; -; mRNA.
DR CCDS; CCDS6250.1; -. [Q16698-1]
DR CCDS; CCDS87618.1; -. [Q16698-2]
DR PIR; S53352; S53352.
DR RefSeq; NP_001317504.1; NM_001330575.1. [Q16698-2]
DR RefSeq; NP_001350.1; NM_001359.1. [Q16698-1]
DR RefSeq; XP_016868636.1; XM_017013147.1.
DR RefSeq; XP_016868637.1; XM_017013148.1. [Q16698-2]
DR PDB; 1W6U; X-ray; 1.75 A; A/B/C/D=35-335.
DR PDB; 1W73; X-ray; 2.10 A; A/B/C/D=35-335.
DR PDB; 1W8D; X-ray; 2.20 A; A/B/C/D=35-335.
DR PDBsum; 1W6U; -.
DR PDBsum; 1W73; -.
DR PDBsum; 1W8D; -.
DR AlphaFoldDB; Q16698; -.
DR SMR; Q16698; -.
DR BioGRID; 108030; 73.
DR IntAct; Q16698; 43.
DR MINT; Q16698; -.
DR STRING; 9606.ENSP00000220764; -.
DR DrugBank; DB08605; 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR SwissLipids; SLP:000001049; -.
DR CarbonylDB; Q16698; -.
DR iPTMnet; Q16698; -.
DR MetOSite; Q16698; -.
DR PhosphoSitePlus; Q16698; -.
DR SwissPalm; Q16698; -.
DR BioMuta; DECR1; -.
DR DMDM; 3913456; -.
DR UCD-2DPAGE; Q16698; -.
DR EPD; Q16698; -.
DR jPOST; Q16698; -.
DR MassIVE; Q16698; -.
DR MaxQB; Q16698; -.
DR PaxDb; Q16698; -.
DR PeptideAtlas; Q16698; -.
DR PRIDE; Q16698; -.
DR ProteomicsDB; 61037; -. [Q16698-1]
DR ProteomicsDB; 6768; -.
DR TopDownProteomics; Q16698-1; -. [Q16698-1]
DR TopDownProteomics; Q16698-2; -. [Q16698-2]
DR Antibodypedia; 12737; 274 antibodies from 28 providers.
DR DNASU; 1666; -.
DR Ensembl; ENST00000220764.7; ENSP00000220764.2; ENSG00000104325.7. [Q16698-1]
DR Ensembl; ENST00000522161.5; ENSP00000429779.1; ENSG00000104325.7. [Q16698-2]
DR GeneID; 1666; -.
DR KEGG; hsa:1666; -.
DR MANE-Select; ENST00000220764.7; ENSP00000220764.2; NM_001359.2; NP_001350.1.
DR UCSC; uc003yek.2; human. [Q16698-1]
DR CTD; 1666; -.
DR DisGeNET; 1666; -.
DR GeneCards; DECR1; -.
DR HGNC; HGNC:2753; DECR1.
DR HPA; ENSG00000104325; Tissue enhanced (heart muscle, liver).
DR MIM; 222745; gene.
DR MIM; 616034; phenotype.
DR neXtProt; NX_Q16698; -.
DR OpenTargets; ENSG00000104325; -.
DR PharmGKB; PA141; -.
DR VEuPathDB; HostDB:ENSG00000104325; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q16698; -.
DR OMA; FPTKGAW; -.
DR PhylomeDB; Q16698; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.124; 2681.
DR PathwayCommons; Q16698; -.
DR Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR SABIO-RK; Q16698; -.
DR SignaLink; Q16698; -.
DR BioGRID-ORCS; 1666; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; DECR1; human.
DR EvolutionaryTrace; Q16698; -.
DR GenomeRNAi; 1666; -.
DR Pharos; Q16698; Tbio.
DR PRO; PR:Q16698; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q16698; protein.
DR Bgee; ENSG00000104325; Expressed in left ventricle myocardium and 198 other tissues.
DR ExpressionAtlas; Q16698; baseline and differential.
DR Genevisible; Q16698; HS.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA: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 3D-structure; Acetylation; Alternative splicing; 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:7818482"
FT CHAIN 35..335
FT /note="2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-
FT producing], mitochondrial"
FT /id="PRO_0000031965"
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:0000269|PubMed:15531764"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15531764"
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:0000269|PubMed:15531764"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15531764"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15531764"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15531764"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15531764"
FT BINDING 240..243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15531764"
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:0007744|PubMed:24275569"
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 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
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 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 VAR_SEQ 1..23
FT /note="MKLPARVFFTLGSRLPCGLAPRR -> MSGLGKKHLLLMGE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056388"
FT VARIANT 333
FT /note="K -> N (in dbSNP:rs15094)"
FT /id="VAR_012034"
FT MUTAGEN 148
FT /note="N->A: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:15531764"
FT MUTAGEN 199
FT /note="Y->A: Reduces enzyme activity by 99%. Strongly
FT reduced affinity for substrate and for NADP."
FT /evidence="ECO:0000269|PubMed:15531764"
FT MUTAGEN 210
FT /note="S->A: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:15531764"
FT MUTAGEN 214
FT /note="K->A: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:15531764"
FT CONFLICT 287
FT /note="D -> G (in Ref. 2; AAB09423)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="I -> V (in Ref. 2; AAB09423)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> G (in Ref. 2; AAB09423)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="F -> G (in Ref. 2; AAB09423)"
FT /evidence="ECO:0000305"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:1W6U"
FT TURN 54..59
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1W6U"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 158..185
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1W73"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1W6U"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:1W6U"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:1W6U"
SQ SEQUENCE 335 AA; 36068 MW; F04E72AACB718430 CRC64;
MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA MLPPNSFQGK
VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA EQISSQTGNK VHAIQCDVRD
PDMVQNTVSE LIKVAGHPNI VINNAAGNFI SPTERLSPNA WKTITDIVLN GTAFVTLEIG
KQLIKAQKGA AFLSITTIYA ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP
GPIKTKGAFS RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD
GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS
