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Q16698 (DECR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference 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. Ref.8

Subunit structure

Homotetramer. Ref.8

Subcellular location

Mitochondrion.

Tissue specificity

Heart = liver = pancreas > kidney >> skeletal muscle = lung. Ref.1

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=7.7 µM for NADPH Ref.8

KM=14.3 µM for trans-2,trans-4-hexadienoyl-CoA

Vmax=30.3 µmol/min/mg enzyme

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 binding66 – 716NADP
Nucleotide binding240 – 2434NADP

Sites

Active site1991Proton acceptor Potential
Binding site911NADP
Binding site911Substrate By similarity
Binding site1171NADP
Binding site1191Substrate
Binding site1491Substrate
Binding site1571Substrate
Binding site2141NADP
Binding site2511Substrate By similarity

Amino acid modifications

Modified residue421N6-acetyllysine; alternate By similarity
Modified residue421N6-succinyllysine; alternate By similarity
Modified residue491N6-acetyllysine; alternate By similarity
Modified residue491N6-succinyllysine; alternate By similarity
Modified residue731N6-succinyllysine By similarity
Modified residue971N6-acetyllysine; alternate By similarity
Modified residue971N6-succinyllysine; alternate By similarity
Modified residue2301N6-acetyllysine Ref.6
Modified residue2441N6-acetyllysine; alternate By similarity
Modified residue2441N6-succinyllysine; alternate By similarity
Modified residue2601N6-acetyllysine; alternate By similarity
Modified residue2601N6-succinyllysine; alternate By similarity
Modified residue3191N6-acetyllysine; alternate By similarity
Modified residue3191N6-succinyllysine; alternate By similarity

Natural variations

Natural variant3331K → N.
Corresponds to variant rs15094 [ dbSNP | Ensembl ].
VAR_012034

Experimental info

Mutagenesis1481N → A: Reduces enzyme activity by 97%. Ref.8
Mutagenesis1991Y → A: Reduces enzyme activity by 99%. Strongly reduced affinity for substrate and for NADP. Ref.8
Mutagenesis2101S → A: Reduces enzyme activity by over 99%. Ref.8
Mutagenesis2141K → A: Reduces enzyme activity by over 99%. Ref.8
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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS53352.
RefSeqNP_001350.1. NM_001359.1.
UniGeneHs.492212.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6UX-ray1.75A/B/C/D35-335[»]
1W73X-ray2.10A/B/C/D35-335[»]
1W8DX-ray2.20A/B/C/D35-335[»]
ProteinModelPortalQ16698.
SMRQ16698. Positions 35-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108030. 8 interactions.
IntActQ16698. 5 interactions.
STRING9606.ENSP00000220764.

PTM databases

PhosphoSiteQ16698.

Polymorphism databases

DMDM3913456.

2D gel databases

UCD-2DPAGEQ16698.

Proteomic databases

PaxDbQ16698.
PeptideAtlasQ16698.
PRIDEQ16698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220764; ENSP00000220764; ENSG00000104325.
GeneID1666.
KEGGhsa:1666.
UCSCuc003yek.1. human.

Organism-specific databases

CTD1666.
GeneCardsGC08P091082.
HGNCHGNC:2753. DECR1.
HPAHPA023160.
HPA023162.
HPA023238.
MIM222745. gene+phenotype.
neXtProtNX_Q16698.
PharmGKBPA141.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG005465.
InParanoidQ16698.
KOK13236.
OMANCTLAFG.
PhylomeDBQ16698.
TreeFamTF315256.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ16698.

Gene expression databases

ArrayExpressQ16698.
BgeeQ16698.
CleanExHS_DECR1.
GenevestigatorQ16698.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

ChiTaRSDECR1. human.
EvolutionaryTraceQ16698.
GenomeRNAi1666.
NextBio6856.
PROQ16698.
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: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

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