2,4-dienoyl-CoA reductase, mitochondrial precursor

Names and origin

Protein names

Recommended name:
    2,4-dienoyl-CoA reductase, mitochondrial
    EC=1.3.1.34
Alternative name(s):
    2,4-dienoyl-CoA reductase [NADPH]
      Short name=4-enoyl-CoA reductase [NADPH]

Gene names

Name:	DECR1
Synonyms:	DECR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Subunit structure	Homotetramer. Ref.7
Subcellular location	Mitochondrion.
Tissue specificity	Heart = liver = pancreas > kidney >> skeletal muscle = lung.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.

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Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.1 Ref.7 Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homotetramerization Ref.7 Inferred from direct assay. Source: UniProtKB
Cellular component	mitochondrion Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	2,4-dienoyl-CoA reductase (NADPH) activity Ref.1 Ref.7 Inferred from direct assay. Source: UniProtKB NADPH binding Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 34

34

Mitochondrion By similarity

Chain

35 – 335

301

2,4-dienoyl-CoA reductase, mitochondrial

PRO_0000031965

Regions

Nucleotide binding

62 – 94

33

NADP

Sites

Active site

199

1

Proton acceptor Probable

Binding site

157

1

Substrate

Binding site

214

1

NAD

Amino acid modifications

Modified residue

110

1

N6-acetyllysine By similarity

Natural variations

Natural variant

333

1

K → N: dbSNP rs15094.

VAR_012034

Experimental info

Sequence conflict

287

1

D → G in AAB09423. Ref.2

Sequence conflict

292

1

I → V in AAB09423. Ref.2

Sequence conflict

303

1

E → G in AAB09423. Ref.2

Sequence conflict

311

1

F → G in AAB09423. Ref.2

Secondary structure

1

.

335

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q16698-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F04E72AACB718430
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FASTA

335

36,068

        10         20         30         40         50         60 
MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA MLPPNSFQGK 

        70         80         90        100        110        120 
VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA EQISSQTGNK VHAIQCDVRD 

       130        140        150        160        170        180 
PDMVQNTVSE LIKVAGHPNI VINNAAGNFI SPTERLSPNA WKTITDIVLN GTAFVTLEIG 

       190        200        210        220        230        240 
KQLIKAQKGA AFLSITTIYA ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP 

       250        260        270        280        290        300 
GPIKTKGAFS RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD 

       310        320        330 
GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase." Koivuranta K.T., Hakkola E.H., Hiltunen J.K. Biochem. J. 304:787-792(1994) [PubMed: 7818482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	Ding J.H., Yang B.Z., Roe C.R. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Molecular cloning and characterization of the human mitochondrial 2,4-dienoyl-CoA reductase gene (DECR)." Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J., Palotie A., Hiltunen J.K. Genomics 46:112-119(1997) [PubMed: 9403065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"DNA sequence and analysis of human chromosome 8." 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. Lander E.S. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site." Alphey M.S., Yu W., Byres E., Li D., Hunter W.N. J. Biol. Chem. 280:3068-3077(2005) [PubMed: 15531764] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND SUBSTRATE, SUBUNIT.
+	Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

L26050 mRNA. Translation: AAA67551.1.
U49352 mRNA. Translation: AAB09423.1.
U78302

U94987 Genomic DNA. Translation: AAB88724.1.
AC004612 Genomic DNA. Translation: AAC14671.1.
AF049895 Genomic DNA. No translation available.
BC105080 mRNA. Translation: AAI05081.1.
BC105082 mRNA. Translation: AAI05083.1.

IPI

IPI00003482.

PIR

S53352.

RefSeq

NP_001350.1.

UniGene

Hs.492212

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W6U	X-ray	1.75	A/B/C/D	35-335	[»]
1W73	X-ray	2.10	A/B/C/D	35-335	[»]
1W8D	X-ray	2.20	A/B/C/D	35-335	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q16698.

Proteomic databases

PeptideAtlas

Q16698.

PRIDE

Q16698.

Genome annotation databases

Ensembl

ENSG00000104325. Homo sapiens. [Contig view]

GeneID

1666.

KEGG

hsa:1666.

UCSC

uc003yek.1. human.

Organism-specific databases

GeneCards

GC08P091082.

H-InvDB

HIX0034361.

HGNC

HGNC:2753. DECR1.

MIM

222745. gene+phenotype.

PharmGKB

PA141.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q16698.

HOVERGEN

Q16698.

OMA

Q16698. LIKAQKG.

Enzyme and pathway databases

BRENDA

1.3.1.34. 247.

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

Q16698.

Bgee

Q16698.

CleanEx

HS_DECR1.

GermOnline

ENSG00000104325. Homo sapiens.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

PROSITE

PS00061. ADH_SHORT. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

6856.

SOURCE

Search...

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Entry information

Entry name

DECR_HUMAN

Accession

Primary (citable) accession number: Q16698
Secondary accession number(s): Q2M304, Q93085

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	July 7, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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