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Q16698

- DECR_HUMAN

UniProt

Q16698 - DECR_HUMAN

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Protein
2,4-dienoyl-CoA reductase, mitochondrial
Gene
DECR1, DECR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.1 Publication

Kineticsi

  1. KM=7.7 µM for NADPH1 Publication
  2. KM=14.3 µM for trans-2,trans-4-hexadienoyl-CoA

Vmax=30.3 µmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911NADP
Binding sitei91 – 911Substrate By similarity
Binding sitei117 – 1171NADP
Binding sitei119 – 1191Substrate
Binding sitei149 – 1491Substrate
Binding sitei157 – 1571Substrate
Active sitei199 – 1991Proton acceptor Reviewed prediction
Binding sitei214 – 2141NADP
Binding sitei251 – 2511Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 716NADP
Nucleotide bindingi240 – 2434NADP

GO - Molecular functioni

  1. 2,4-dienoyl-CoA reductase (NADPH) activity Source: UniProtKB
  2. NADPH binding Source: UniProtKB
  3. oxidoreductase activity, acting on NAD(P)H Source: Reactome

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid beta-oxidation Source: UniProtKB
  3. protein homotetramerization Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
SABIO-RKQ16698.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DECR1
Synonyms:DECR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:2753. DECR1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProtKB
  5. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481N → A: Reduces enzyme activity by 97%. 1 Publication
Mutagenesisi199 – 1991Y → A: Reduces enzyme activity by 99%. Strongly reduced affinity for substrate and for NADP. 1 Publication
Mutagenesisi210 – 2101S → A: Reduces enzyme activity by over 99%. 1 Publication
Mutagenesisi214 – 2141K → A: Reduces enzyme activity by over 99%. 1 Publication

Organism-specific databases

MIMi222745. gene+phenotype.
PharmGKBiPA141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion By similarity
Add
BLAST
Chaini35 – 3353012,4-dienoyl-CoA reductase, mitochondrial
PRO_0000031965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysine; alternate By similarity
Modified residuei42 – 421N6-succinyllysine; alternate By similarity
Modified residuei49 – 491N6-acetyllysine; alternate By similarity
Modified residuei49 – 491N6-succinyllysine; alternate By similarity
Modified residuei73 – 731N6-succinyllysine By similarity
Modified residuei97 – 971N6-acetyllysine; alternate By similarity
Modified residuei97 – 971N6-succinyllysine; alternate By similarity
Modified residuei230 – 2301N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysine; alternate By similarity
Modified residuei244 – 2441N6-succinyllysine; alternate By similarity
Modified residuei260 – 2601N6-acetyllysine; alternate By similarity
Modified residuei260 – 2601N6-succinyllysine; alternate By similarity
Modified residuei319 – 3191N6-acetyllysine; alternate By similarity
Modified residuei319 – 3191N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16698.
PaxDbiQ16698.
PeptideAtlasiQ16698.
PRIDEiQ16698.

2D gel databases

UCD-2DPAGEQ16698.

PTM databases

PhosphoSiteiQ16698.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ16698.
BgeeiQ16698.
CleanExiHS_DECR1.
GenevestigatoriQ16698.

Organism-specific databases

HPAiHPA023160.
HPA023162.
HPA023238.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi108030. 9 interactions.
IntActiQ16698. 5 interactions.
STRINGi9606.ENSP00000220764.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 438
Turni54 – 596
Beta strandi61 – 655
Turni66 – 683
Helixi70 – 8112
Beta strandi85 – 917
Helixi93 – 10715
Beta strandi111 – 1155
Helixi121 – 13414
Beta strandi139 – 1435
Helixi153 – 1553
Helixi158 – 18528
Beta strandi190 – 1956
Helixi199 – 2024
Helixi208 – 22821
Helixi229 – 2313
Beta strandi233 – 2408
Beta strandi254 – 2563
Helixi257 – 2637
Helixi274 – 28411
Helixi287 – 2893
Beta strandi296 – 3005
Helixi303 – 3086
Helixi312 – 3165
Helixi319 – 3257

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6UX-ray1.75A/B/C/D35-335[»]
1W73X-ray2.10A/B/C/D35-335[»]
1W8DX-ray2.20A/B/C/D35-335[»]
ProteinModelPortaliQ16698.
SMRiQ16698. Positions 35-328.

Miscellaneous databases

EvolutionaryTraceiQ16698.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1028.
HOVERGENiHBG005465.
InParanoidiQ16698.
KOiK13236.
OMAiSMAGEFN.
PhylomeDBiQ16698.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16698-1 [UniParc]FASTAAdd to Basket

« Hide

MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA    50
MLPPNSFQGK VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA 100
EQISSQTGNK VHAIQCDVRD PDMVQNTVSE LIKVAGHPNI VINNAAGNFI 150
SPTERLSPNA WKTITDIVLN GTAFVTLEIG KQLIKAQKGA AFLSITTIYA 200
ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP GPIKTKGAFS 250
RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD 300
GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS 335
Length:335
Mass (Da):36,068
Last modified:November 1, 1996 - v1
Checksum:iF04E72AACB718430
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti333 – 3331K → N.
Corresponds to variant rs15094 [ dbSNP | Ensembl ].
VAR_012034

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871D → G in AAB09423. 1 Publication
Sequence conflicti292 – 2921I → V in AAB09423. 1 Publication
Sequence conflicti303 – 3031E → G in AAB09423. 1 Publication
Sequence conflicti311 – 3111F → G in AAB09423. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26050 mRNA. Translation: AAA67551.1.
U49352 mRNA. Translation: AAB09423.1.
U78302
, 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.
CCDSiCCDS6250.1.
PIRiS53352.
RefSeqiNP_001350.1. NM_001359.1.
UniGeneiHs.492212.

Genome annotation databases

EnsembliENST00000220764; ENSP00000220764; ENSG00000104325.
GeneIDi1666.
KEGGihsa:1666.
UCSCiuc003yek.1. human.

Polymorphism databases

DMDMi3913456.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26050 mRNA. Translation: AAA67551.1 .
U49352 mRNA. Translation: AAB09423.1 .
U78302
, 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 .
CCDSi CCDS6250.1.
PIRi S53352.
RefSeqi NP_001350.1. NM_001359.1.
UniGenei Hs.492212.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q16698.
SMRi Q16698. Positions 35-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108030. 9 interactions.
IntActi Q16698. 5 interactions.
STRINGi 9606.ENSP00000220764.

PTM databases

PhosphoSitei Q16698.

Polymorphism databases

DMDMi 3913456.

2D gel databases

UCD-2DPAGE Q16698.

Proteomic databases

MaxQBi Q16698.
PaxDbi Q16698.
PeptideAtlasi Q16698.
PRIDEi Q16698.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220764 ; ENSP00000220764 ; ENSG00000104325 .
GeneIDi 1666.
KEGGi hsa:1666.
UCSCi uc003yek.1. human.

Organism-specific databases

CTDi 1666.
GeneCardsi GC08P091082.
HGNCi HGNC:2753. DECR1.
HPAi HPA023160.
HPA023162.
HPA023238.
MIMi 222745. gene+phenotype.
neXtProti NX_Q16698.
PharmGKBi PA141.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1028.
HOVERGENi HBG005465.
InParanoidi Q16698.
KOi K13236.
OMAi SMAGEFN.
PhylomeDBi Q16698.
TreeFami TF315256.

Enzyme and pathway databases

Reactomei REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
SABIO-RK Q16698.

Miscellaneous databases

ChiTaRSi DECR1. human.
EvolutionaryTracei Q16698.
GenomeRNAii 1666.
NextBioi 6856.
PROi Q16698.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16698.
Bgeei Q16698.
CleanExi HS_DECR1.
Genevestigatori Q16698.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiDECR_HUMAN
AccessioniPrimary (citable) accession number: Q16698
Secondary accession number(s): Q2M304, Q93085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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