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Reviewed, UniProtKB/Swiss-Prot Q16698 (DECR_HUMAN)

Last modified July 7, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processfatty 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 componentmitochondrion Ref.1

Non-traceable author statement. Source: UniProtKB

   Molecular function2,4-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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 3353012,4-dienoyl-CoA reductase, mitochondrial
PRO_0000031965

Regions

Nucleotide binding62 – 9433NADP

Sites

Active site1991Proton acceptor Probable
Binding site1571Substrate
Binding site2141NAD

Amino acid modifications

Modified residue1101N6-acetyllysine By similarity

Natural variations

Natural variant3331K → N: dbSNP rs15094.
VAR_012034

Experimental info

Sequence conflict2871D → G in AAB09423. Ref.2
Sequence conflict2921I → V in AAB09423. Ref.2
Sequence conflict3031E → G in AAB09423. Ref.2
Sequence conflict3111F → G in AAB09423. Ref.2

Secondary structure

............................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16698-1 [UniParc].

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

FASTA33536,068
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
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.

Web resources

Cross-references

Sequence databases

L26050 mRNA. Translation: AAA67551.1.
U49352 mRNA. Translation: AAB09423.1.
U78302 expand/collapse EMBL AC list , U94980, U94981, U94982, U94983, U94984, U94985, U94986, 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.
IPIIPI00003482.
PIRS53352.
RefSeqNP_001350.1.
UniGeneHs.492212

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1W6UX-ray1.75A/B/C/D35-335[»]
1W73X-ray2.10A/B/C/D35-335[»]
1W8DX-ray2.20A/B/C/D35-335[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ16698.

Proteomic databases

PeptideAtlasQ16698.
PRIDEQ16698.

Genome annotation databases

EnsemblENSG00000104325. Homo sapiens. [Contig view]
GeneID1666.
KEGGhsa:1666.
UCSCuc003yek.1. human.

Organism-specific databases

GeneCardsGC08P091082.
H-InvDBHIX0034361.
HGNCHGNC:2753. DECR1.
MIM222745. gene+phenotype.
PharmGKBPA141.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ16698.
HOVERGENQ16698.
OMAQ16698. LIKAQKG.

Enzyme and pathway databases

BRENDA1.3.1.34. 247.
ReactomeREACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressQ16698.
BgeeQ16698.
CleanExHS_DECR1.
GermOnlineENSG00000104325. Homo sapiens.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio6856.
SOURCESearch...

Entry information

Entry nameDECR_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents