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2,4-dienoyl-CoA reductase, mitochondrial (EC 1.3.1.34) (2,4-dienoyl-CoA reductase [NADPH]) (4-enoyl-CoA reductase [NADPH]) (Short chain dehydrogenase/reductase family 18C member 1)

 DECR_HUMAN              Reviewed;         335 AA.
Q16698; B7Z6B8; Q2M304; Q93085;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 167.
RecName: Full=2,4-dienoyl-CoA reductase, mitochondrial;
EC=1.3.1.34 {ECO:0000269|PubMed:15531764};
AltName: Full=2,4-dienoyl-CoA reductase [NADPH];
Short=4-enoyl-CoA reductase [NADPH];
AltName: Full=Short chain dehydrogenase/reductase family 18C member 1;
Flags: Precursor;
Name=DECR1; Synonyms=DECR, SDR18C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=7818482; DOI=10.1042/bj3040787;
Koivuranta K.T., Hakkola E.H., Hiltunen J.K.;
"Isolation and characterization of cDNA for human 120 kDa
mitochondrial 2,4-dienoyl-coenzyme A reductase.";
Biochem. J. 304:787-792(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Ding J.H., Yang B.Z., Roe C.R.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9403065; DOI=10.1006/geno.1997.5004;
Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J.,
Palotie A., Hiltunen J.K.;
"Molecular cloning and characterization of the human mitochondrial
2,4-dienoyl-CoA reductase gene (DECR).";
Genomics 46:112-119(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pericardium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
INVOLVEMENT IN DECRD.
PubMed=24847004; DOI=10.1093/hmg/ddu218;
Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H.,
Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P.,
Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.;
"Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes
dienoyl-CoA reductase deficiency with hyperlysinemia.";
Hum. Mol. Genet. 23:5009-5016(2014).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP
AND SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214.
PubMed=15531764; DOI=10.1074/jbc.M411069200;
Alphey M.S., Yu W., Byres E., Li D., Hunter W.N.;
"Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA
reductase: enzyme-ligand interactions in a distinctive short-chain
reductase active site.";
J. Biol. Chem. 280:3068-3077(2005).
-!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in
the metabolism of unsaturated fatty enoyl-CoA esters having double
bonds in both even- and odd-numbered positions. Catalyzes the
NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-
enoyl-CoA.
-!- CATALYTIC ACTIVITY: Trans-2,3-didehydroacyl-CoA + NADP(+) =
trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.
{ECO:0000269|PubMed:15531764}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.7 uM for NADPH {ECO:0000269|PubMed:15531764};
KM=14.3 uM for trans-2,trans-4-hexadienoyl-CoA
{ECO:0000269|PubMed:15531764};
Vmax=30.3 umol/min/mg enzyme {ECO:0000269|PubMed:15531764};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15531764}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16698-1; Sequence=Displayed;
Name=2;
IsoId=Q16698-2; Sequence=VSP_056388;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Heart = liver = pancreas > kidney >> skeletal
muscle = lung. {ECO:0000269|PubMed:7818482}.
-!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD)
[MIM:616034]: A rare, autosomal recessive, inborn error of
polyunsaturated fatty acids and lysine metabolism, resulting in
mitochondrial dysfunction. Affected individuals have a severe
encephalopathy with neurologic and metabolic abnormalities
beginning in early infancy. Laboratory studies show increased
C10:2 carnitine levels and hyperlysinemia.
{ECO:0000269|PubMed:24847004}. Note=The protein represented in
this entry is involved in disease pathogenesis. A selective
decrease in mitochondrial NADP(H) levels due to NADK2 mutations
causes a deficiency of NADPH-dependent mitochondrial enzymes, such
as DECR1 and AASS. {ECO:0000269|PubMed:24847004}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
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EMBL; L26050; AAA67551.1; -; mRNA.
EMBL; U49352; AAB09423.1; -; mRNA.
EMBL; U78302; AAB88724.1; -; Genomic_DNA.
EMBL; U94980; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94981; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94982; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94983; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94984; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94985; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94986; AAB88724.1; JOINED; Genomic_DNA.
EMBL; U94987; AAB88724.1; JOINED; Genomic_DNA.
EMBL; AK300069; BAH13204.1; -; mRNA.
EMBL; AC004612; AAC14671.1; -; Genomic_DNA.
EMBL; AF049895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC105080; AAI05081.1; -; mRNA.
EMBL; BC105082; AAI05083.1; -; mRNA.
CCDS; CCDS6250.1; -. [Q16698-1]
PIR; S53352; S53352.
RefSeq; NP_001317504.1; NM_001330575.1. [Q16698-2]
RefSeq; NP_001350.1; NM_001359.1. [Q16698-1]
RefSeq; XP_016868636.1; XM_017013147.1. [Q16698-2]
RefSeq; XP_016868637.1; XM_017013148.1. [Q16698-2]
UniGene; Hs.492212; -.
UniGene; Hs.660770; -.
PDB; 1W6U; X-ray; 1.75 A; A/B/C/D=35-335.
PDB; 1W73; X-ray; 2.10 A; A/B/C/D=35-335.
PDB; 1W8D; X-ray; 2.20 A; A/B/C/D=35-335.
PDBsum; 1W6U; -.
PDBsum; 1W73; -.
PDBsum; 1W8D; -.
ProteinModelPortal; Q16698; -.
SMR; Q16698; -.
BioGrid; 108030; 36.
IntAct; Q16698; 24.
STRING; 9606.ENSP00000220764; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
SwissLipids; SLP:000001049; -.
CarbonylDB; Q16698; -.
iPTMnet; Q16698; -.
PhosphoSitePlus; Q16698; -.
SwissPalm; Q16698; -.
BioMuta; DECR1; -.
DMDM; 3913456; -.
UCD-2DPAGE; Q16698; -.
EPD; Q16698; -.
MaxQB; Q16698; -.
PaxDb; Q16698; -.
PeptideAtlas; Q16698; -.
PRIDE; Q16698; -.
ProteomicsDB; 61037; -.
TopDownProteomics; Q16698-1; -. [Q16698-1]
TopDownProteomics; Q16698-2; -. [Q16698-2]
Ensembl; ENST00000220764; ENSP00000220764; ENSG00000104325. [Q16698-1]
Ensembl; ENST00000522161; ENSP00000429779; ENSG00000104325. [Q16698-2]
GeneID; 1666; -.
KEGG; hsa:1666; -.
UCSC; uc003yek.2; human. [Q16698-1]
CTD; 1666; -.
DisGeNET; 1666; -.
EuPathDB; HostDB:ENSG00000104325.6; -.
GeneCards; DECR1; -.
HGNC; HGNC:2753; DECR1.
HPA; HPA023160; -.
HPA; HPA023162; -.
HPA; HPA023238; -.
MIM; 222745; gene.
MIM; 616034; phenotype.
neXtProt; NX_Q16698; -.
OpenTargets; ENSG00000104325; -.
PharmGKB; PA141; -.
eggNOG; KOG0725; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00920000149045; -.
HOVERGEN; HBG005465; -.
InParanoid; Q16698; -.
KO; K13236; -.
OMA; DRIPCGR; -.
OrthoDB; EOG091G0GO6; -.
PhylomeDB; Q16698; -.
TreeFam; TF315256; -.
Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
SABIO-RK; Q16698; -.
ChiTaRS; DECR1; human.
EvolutionaryTrace; Q16698; -.
GenomeRNAi; 1666; -.
PRO; PR:Q16698; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104325; -.
CleanEx; HS_DECR1; -.
ExpressionAtlas; Q16698; baseline and differential.
Genevisible; Q16698; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; TAS:Reactome.
GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Fatty acid metabolism; Lipid metabolism; Mitochondrion; NADP;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 34 Mitochondrion. {ECO:0000250}.
CHAIN 35 335 2,4-dienoyl-CoA reductase, mitochondrial.
/FTId=PRO_0000031965.
NP_BIND 66 71 NADP. {ECO:0000269|PubMed:15531764}.
NP_BIND 240 243 NADP. {ECO:0000269|PubMed:15531764}.
ACT_SITE 199 199 Proton acceptor. {ECO:0000255}.
BINDING 91 91 NADP. {ECO:0000269|PubMed:15531764}.
BINDING 91 91 Substrate. {ECO:0000250}.
BINDING 117 117 NADP. {ECO:0000269|PubMed:15531764}.
BINDING 119 119 Substrate. {ECO:0000269|PubMed:15531764}.
BINDING 149 149 Substrate. {ECO:0000269|PubMed:15531764}.
BINDING 157 157 Substrate. {ECO:0000269|PubMed:15531764}.
BINDING 214 214 NADP. {ECO:0000269|PubMed:15531764}.
BINDING 251 251 Substrate. {ECO:0000250}.
MOD_RES 42 42 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 42 42 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 49 49 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 49 49 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 69 69 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 73 73 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 97 97 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 97 97 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 230 230 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 244 244 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 244 244 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 260 260 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 260 260 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 319 319 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
MOD_RES 319 319 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CQ62}.
VAR_SEQ 1 23 MKLPARVFFTLGSRLPCGLAPRR -> MSGLGKKHLLLMGE
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056388.
VARIANT 333 333 K -> N (in dbSNP:rs15094).
/FTId=VAR_012034.
MUTAGEN 148 148 N->A: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:15531764}.
MUTAGEN 199 199 Y->A: Reduces enzyme activity by 99%.
Strongly reduced affinity for substrate
and for NADP.
{ECO:0000269|PubMed:15531764}.
MUTAGEN 210 210 S->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:15531764}.
MUTAGEN 214 214 K->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:15531764}.
CONFLICT 287 287 D -> G (in Ref. 2; AAB09423).
{ECO:0000305}.
CONFLICT 292 292 I -> V (in Ref. 2; AAB09423).
{ECO:0000305}.
CONFLICT 303 303 E -> G (in Ref. 2; AAB09423).
{ECO:0000305}.
CONFLICT 311 311 F -> G (in Ref. 2; AAB09423).
{ECO:0000305}.
HELIX 36 43 {ECO:0000244|PDB:1W6U}.
TURN 54 59 {ECO:0000244|PDB:1W6U}.
STRAND 61 65 {ECO:0000244|PDB:1W6U}.
TURN 66 68 {ECO:0000244|PDB:1W6U}.
HELIX 70 81 {ECO:0000244|PDB:1W6U}.
STRAND 85 91 {ECO:0000244|PDB:1W6U}.
HELIX 93 107 {ECO:0000244|PDB:1W6U}.
STRAND 111 115 {ECO:0000244|PDB:1W6U}.
HELIX 121 134 {ECO:0000244|PDB:1W6U}.
STRAND 139 143 {ECO:0000244|PDB:1W6U}.
HELIX 153 155 {ECO:0000244|PDB:1W6U}.
HELIX 158 185 {ECO:0000244|PDB:1W6U}.
STRAND 190 195 {ECO:0000244|PDB:1W6U}.
HELIX 199 202 {ECO:0000244|PDB:1W6U}.
HELIX 208 228 {ECO:0000244|PDB:1W6U}.
HELIX 229 231 {ECO:0000244|PDB:1W6U}.
STRAND 233 240 {ECO:0000244|PDB:1W6U}.
STRAND 254 256 {ECO:0000244|PDB:1W73}.
HELIX 257 263 {ECO:0000244|PDB:1W6U}.
HELIX 274 284 {ECO:0000244|PDB:1W6U}.
HELIX 287 289 {ECO:0000244|PDB:1W6U}.
STRAND 296 300 {ECO:0000244|PDB:1W6U}.
HELIX 303 308 {ECO:0000244|PDB:1W6U}.
HELIX 312 316 {ECO:0000244|PDB:1W6U}.
HELIX 319 325 {ECO:0000244|PDB:1W6U}.
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


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EIAAB10842 2,4-dienoyl-CoA reductase 2,Decr2,Mouse,Mus musculus,Pdcr,Peroxisomal 2,4-dienoyl-CoA reductase
EIAAB05620 15-hydroxyprostaglandin dehydrogenase [NADP+],Carbonyl reductase [NADPH] 1,Cbr,Cbr1,Mouse,Mus musculus,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reductase
EIAAB05619 15-hydroxyprostaglandin dehydrogenase [NADP+],Bos taurus,Bovine,Carbonyl reductase [NADPH] 1,CBR1,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reductase
EIAAB10843 2,4-dienoyl-CoA reductase 2,DCR-AKL,Decr2,Peroxisomal 2,4-dienoyl-CoA reductase,pVI-AKL,Rat,Rattus norvegicus
EIAAB30518 2,4-dienoyl-CoA reductase-related protein,DCR-RP,Homo sapiens,HPDHase,Human,PECR,Peroxisomal trans-2-enoyl-CoA reductase,PRO1004,pVI-ARL,TERP
EIAAB05621 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,CBR,CBR1,NADPH-dependent carbonyl reductase 1,Oryctolagus cuniculus,Prostaglandin 9-keto
EIAAB05616 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,CBR,CBR1,CRN,NADPH-dependent carbonyl reductase 1,Pig,Prostaglandin 9-ketoreductase,Pros
EIAAB05618 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,Cbr,Cbr1,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandi
EIAAB05623 Adipocyte protein P27,AP27,Carbonyl reductase [NADPH] 2,Cbr2,LCR,Lung carbonyl reductase,Mouse,Mus musculus,NADPH-dependent carbonyl reductase 2
EIAAB10844 2,4-dienoyl-CoA reductase 2,DECR2,Homo sapiens,Human,pDCR,PDCR,Peroxisomal 2,4-dienoyl-CoA reductase
EIAAB30520 Pecr,Peroxisomal 2,4-dienoyl-CoA reductase,Peroxisomal trans-2-enoyl-CoA reductase,PX-2,4-DCR1,Rat,Rattus norvegicus,RLF98,TERP
EIAAB05617 15-hydroxyprostaglandin dehydrogenase [NADP+],Carbonyl reductase [NADPH] 1,CBR,CBR1,CRN,Homo sapiens,Human,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reduc
EIAAB05622 Carbonyl reductase [NADPH] 2,CBR2,LCR,Lung carbonyl reductase,NADPH-dependent carbonyl reductase 2,Pig,Sus scrofa
EIAAB34168 EPHD-2,Epidermal retinol dehydrogenase 2,Mouse,Mus musculus,Rdhe2,RDH-E2,Retinal short-chain dehydrogenase reductase 2,retSDR2,Scdr9,Sdr16c5,Short-chain dehydrogenase reductase 9,Short-chain dehydroge
EIAAB05624 Carbonyl reductase [NADPH] 3,CBR3,Homo sapiens,Human,NADPH-dependent carbonyl reductase 3
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
E2220h AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human
abx111227 Polyclonal Rabbit Biliverdin Reductase B (Flavin Reductase (Nadph)) Antibody 50 μl
201-20-0647 BLVRB{biliverdin reductase B (flavin reductase (NADPH))}rabbit.pAb 0.1ml
U2220h CLIA kit AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
U2220h CLIA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T
E2220h ELISA AKR1B1,Aldehyde reductase,Aldo-keto reductase family 1 member B1,Aldose reductase,ALDR1,AR,Homo sapiens,Human 96T


 

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