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Reviewed, UniProtKB/Swiss-Prot Q64591 (DECR_RAT)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 · 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2,4-dienoyl-CoA reductase (NADPH) activity Ref.1

Traceable author statement. Source: RGD

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.1
Chain35 – 3353012,4-dienoyl-CoA reductase, mitochondrial
PRO_0000031967

Regions

Nucleotide binding62 – 9433NADP By similarity

Sites

Active site1991Proton acceptor By similarity
Binding site1571Substrate By similarity
Binding site2141NADP By similarity

Amino acid modifications

Modified residue1061N6-acetyllysine By similarity
Modified residue1101N6-acetyllysine By similarity

Experimental info

Sequence conflict111G → R in AAH59120. Ref.2
Sequence conflict231R → K in BAA00446. Ref.1
Sequence conflict791L → R in BAA00446. Ref.1
Sequence conflict1621K → R in BAA00446. Ref.1
Sequence conflict1901A → V in BAA00446. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64591-1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: C4386C65E49A4D2F

FASTA33536,133
        10         20         30         40         50         60 
MALLARAFFA GVSRLPCDPG PQRFFSFGTK TLYQSIDAPQ SKFFPPILKP MLPPNAFQGK 

        70         80         90        100        110        120 
VAFITGGGTG LGKAMTTFLS SLGAQCVIAS RNIDVLKATA EEITSKTGNK VYAIRCDVRD 

       130        140        150        160        170        180 
PDMVHNTVLE LIKVAGHPDV VINNAAGNFI SPSERLSPNG WKTITDIVLN GTAYVTIEIG 

       190        200        210        220        230        240 
KQLIKAQKGA AFLAITTIYA ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP 

       250        260        270        280        290        300 
GPIKTKGAFS RLDPTGKFEK DMIERIPCGR LGTVEELANL ATFLCSDYAS WINGAVIRFD 

       310        320        330 
GGEEVFLSGE FNSLKKVTKE EWDVIEGLIR KTKGS 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of rat liver 2,4-dienoyl-CoA reductase."
Hirose A., Kamijo K., Osumi T., Hashimoto T., Mizugaki M.
Biochim. Biophys. Acta 1049:346-349(1990) [PubMed: 2383590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-53.
Tissue: Liver.
[2]"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: Pituitary.

Cross-references

Sequence databases

D00569 mRNA. Translation: BAA00446.1.
BC059120 mRNA. Translation: AAH59120.1.
IPIIPI00213659.
PIRS11021.
RefSeqNP_476545.1.
UniGeneRn.2854

3D structure databases

HSSPHSSP built from PDB template 1LX6 based on UniProtKB P29132.
SMRQ64591. Positions 37-328.
ModBaseSearch...

Proteomic databases

PRIDEQ64591.

Genome annotation databases

EnsemblENSRNOG00000008236. Rattus norvegicus. [Contig view]
GeneID117543.
KEGGrno:117543.

Organism-specific databases

RGD70999. Decr1.

Phylogenomic databases

HOVERGENQ64591.

Enzyme and pathway databases

BRENDA1.3.1.34. 248.

Gene expression databases

ArrayExpressQ64591.
GermOnlineENSRNOG00000008236. Rattus norvegicus.

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

NextBio620365.

Entry information

Entry nameDECR_RAT
AccessionPrimary (citable) accession number: Q64591
Secondary accession number(s): Q6PCV4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 7, 2005
Last modified: June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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