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Protein

Peroxisomal 2,4-dienoyl-CoA reductase

Gene

DECR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.

Catalytic activityi

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

Kineticsi

  1. KM=59 µM for 2,4-hexadienoyl-CoA2 Publications
  2. KM=6 µM for 2,4-decadienoyl-CoA2 Publications
  3. KM=102 µM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA2 Publications
  1. Vmax=1.75 µmol/min/mg enzyme toward 2,4-Hexadienoyl CoA2 Publications
  2. Vmax=1.37 µmol/min/mg enzyme toward 2,4-Decadienoyl CoA2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60Substrate1
Binding sitei86NADP1 Publication1
Binding sitei88Substrate1
Binding sitei118Substrate1
Binding sitei182NADP1 Publication1
Binding sitei219Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 40NADP1 Publication6
Nucleotide bindingi60 – 64NADP1 Publication5
Nucleotide bindingi208 – 214NADP1 Publication7

GO - Molecular functioni

  • 2,4-dienoyl-CoA reductase (NADPH) activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciZFISH:HS02474-MONOMER.
BRENDAi1.3.1.34. 2681.
ReactomeiR-HSA-535734. Fatty acid, triacylglycerol, and ketone body metabolism.

Chemistry databases

SwissLipidsiSLP:000001050.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal 2,4-dienoyl-CoA reductase (EC:1.3.1.34)
Short name:
pDCR
Alternative name(s):
2,4-dienoyl-CoA reductase 2
Short chain dehydrogenase/reductase family 17C member 1
Gene namesi
Name:DECR2
Synonyms:PDCR, SDR17C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2754. DECR2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86D → A: Reduces enzyme activity by 98%. 1 Publication1
Mutagenesisi137D → A: Reduces enzyme activity by 97%. 1 Publication1
Mutagenesisi186D → A: Reduces enzyme activity by about 95%. 1 Publication1
Mutagenesisi268D → A: Reduces enzyme activity by 97%. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000242612.
ENSG00000274296.
PharmGKBiPA27235.

Polymorphism and mutation databases

BioMutaiDECR2.
DMDMi84029527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000545592 – 292Peroxisomal 2,4-dienoyl-CoA reductaseAdd BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei151N6-acetyllysineCombined sources1
Modified residuei287PhosphoserineCombined sources1
Modified residuei291N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NUI1.
MaxQBiQ9NUI1.
PaxDbiQ9NUI1.
PeptideAtlasiQ9NUI1.
PRIDEiQ9NUI1.

PTM databases

iPTMnetiQ9NUI1.
PhosphoSitePlusiQ9NUI1.

Expressioni

Gene expression databases

BgeeiENSG00000242612.
CleanExiHS_DECR2.
ExpressionAtlasiQ9NUI1. baseline and differential.
GenevisibleiQ9NUI1. HS.

Organism-specific databases

HPAiHPA047631.

Interactioni

Subunit structurei

Monomer, dimer and oligomer.1 Publication

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117525. 14 interactors.
IntActiQ9NUI1. 10 interactors.
MINTiMINT-2819394.
STRINGi9606.ENSP00000219481.

Structurei

Secondary structure

1292
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Turni23 – 28Combined sources6
Beta strandi30 – 34Combined sources5
Turni35 – 37Combined sources3
Helixi39 – 49Combined sources11
Turni50 – 52Combined sources3
Beta strandi54 – 60Combined sources7
Helixi62 – 76Combined sources15
Beta strandi80 – 84Combined sources5
Helixi90 – 104Combined sources15
Beta strandi109 – 112Combined sources4
Helixi122 – 124Combined sources3
Helixi127 – 137Combined sources11
Helixi139 – 151Combined sources13
Helixi153 – 156Combined sources4
Beta strandi158 – 163Combined sources6
Helixi167 – 170Combined sources4
Helixi176 – 196Combined sources21
Helixi197 – 199Combined sources3
Beta strandi201 – 208Combined sources8
Beta strandi211 – 214Combined sources4
Helixi215 – 220Combined sources6
Helixi224 – 232Combined sources9
Helixi242 – 253Combined sources12
Helixi255 – 257Combined sources3
Beta strandi264 – 268Combined sources5
Helixi271 – 274Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FC6X-ray2.10A/B/C/D2-278[»]
4FC7X-ray1.84A/B/C/D2-278[»]
ProteinModelPortaliQ9NUI1.
SMRiQ9NUI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 128Substrate binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi290 – 292Microbody targeting signalBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG100327.
InParanoidiQ9NUI1.
KOiK13237.
OMAiDDTEGMR.
OrthoDBiEOG091G0GO6.
PhylomeDBiQ9NUI1.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUI1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR
60 70 80 90 100
HGCHTVIASR SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAVMAAVDQA
110 120 130 140 150
LKEFGRIDIL INCAAGNFLC PAGALSFNAF KTVMDIDTSG TFNVSRVLYE
160 170 180 190 200
KFFRDHGGVI VNITATLGNR GQALQVHAGS AKAAVDAMTR HLAVEWGPQN
210 220 230 240 250
IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG NKTEIAHSVL
260 270 280 290
YLASPLASYV TGAVLVADGG AWLTFPNGVK GLPDFASFSA KL
Length:292
Mass (Da):30,778
Last modified:October 1, 2000 - v1
Checksum:i9E7CD2995CE598D6
GO
Isoform 2 (identifier: Q9NUI1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: R → RASEDQMGHCSSSGTCLAGVATFMVIVGKQPPNQKSRETKEQGRQIPFVCVR
     114-160: AAGNFLCPAG...KFFRDHGGVI → SSSSCGLPFC...RHLQCVSCAL
     161-292: Missing.

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):23,130
Checksum:i34B6F2CFF91F1827
GO
Isoform 3 (identifier: Q9NUI1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.
Show »
Length:244
Mass (Da):25,589
Checksum:iCF192E5F987E311C
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0136291 – 48Missing in isoform 3. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_01363050R → RASEDQMGHCSSSGTCLAGV ATFMVIVGKQPPNQKSRETK EQGRQIPFVCVR in isoform 2. 1 Publication1
Alternative sequenceiVSP_013631114 – 160AAGNF…HGGVI → SSSSCGLPFCRCGRELPVPR WRLVLQRLQDRDGHRYQRHL QCVSCAL in isoform 2. 1 PublicationAdd BLAST47
Alternative sequenceiVSP_013632161 – 292Missing in isoform 2. 1 PublicationAdd BLAST132

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293009 mRNA. Translation: CAC05664.1.
AE006463 Genomic DNA. Translation: AAK61231.1.
AK128012 mRNA. Translation: BAC87232.1.
AL023881 Genomic DNA. Translation: CAB92744.1.
BC010740 mRNA. Translation: AAH10740.1.
BC011968 mRNA. Translation: AAH11968.1.
CCDSiCCDS10409.1. [Q9NUI1-1]
RefSeqiNP_065715.1. NM_020664.3. [Q9NUI1-1]
UniGeneiHs.628831.

Genome annotation databases

EnsembliENST00000219481; ENSP00000219481; ENSG00000242612. [Q9NUI1-1]
ENST00000439661; ENSP00000399697; ENSG00000242612. [Q9NUI1-2]
ENST00000613476; ENSP00000481547; ENSG00000274296. [Q9NUI1-1]
ENST00000631856; ENSP00000488824; ENSG00000274296. [Q9NUI1-2]
GeneIDi26063.
KEGGihsa:26063.
UCSCiuc002chb.4. human. [Q9NUI1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293009 mRNA. Translation: CAC05664.1.
AE006463 Genomic DNA. Translation: AAK61231.1.
AK128012 mRNA. Translation: BAC87232.1.
AL023881 Genomic DNA. Translation: CAB92744.1.
BC010740 mRNA. Translation: AAH10740.1.
BC011968 mRNA. Translation: AAH11968.1.
CCDSiCCDS10409.1. [Q9NUI1-1]
RefSeqiNP_065715.1. NM_020664.3. [Q9NUI1-1]
UniGeneiHs.628831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FC6X-ray2.10A/B/C/D2-278[»]
4FC7X-ray1.84A/B/C/D2-278[»]
ProteinModelPortaliQ9NUI1.
SMRiQ9NUI1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117525. 14 interactors.
IntActiQ9NUI1. 10 interactors.
MINTiMINT-2819394.
STRINGi9606.ENSP00000219481.

Chemistry databases

SwissLipidsiSLP:000001050.

PTM databases

iPTMnetiQ9NUI1.
PhosphoSitePlusiQ9NUI1.

Polymorphism and mutation databases

BioMutaiDECR2.
DMDMi84029527.

Proteomic databases

EPDiQ9NUI1.
MaxQBiQ9NUI1.
PaxDbiQ9NUI1.
PeptideAtlasiQ9NUI1.
PRIDEiQ9NUI1.

Protocols and materials databases

DNASUi26063.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219481; ENSP00000219481; ENSG00000242612. [Q9NUI1-1]
ENST00000439661; ENSP00000399697; ENSG00000242612. [Q9NUI1-2]
ENST00000613476; ENSP00000481547; ENSG00000274296. [Q9NUI1-1]
ENST00000631856; ENSP00000488824; ENSG00000274296. [Q9NUI1-2]
GeneIDi26063.
KEGGihsa:26063.
UCSCiuc002chb.4. human. [Q9NUI1-1]

Organism-specific databases

CTDi26063.
GeneCardsiDECR2.
H-InvDBHIX0012648.
HIX0079832.
HIX0173312.
HGNCiHGNC:2754. DECR2.
HPAiHPA047631.
MIMi615839. gene.
neXtProtiNX_Q9NUI1.
OpenTargetsiENSG00000242612.
ENSG00000274296.
PharmGKBiPA27235.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG100327.
InParanoidiQ9NUI1.
KOiK13237.
OMAiDDTEGMR.
OrthoDBiEOG091G0GO6.
PhylomeDBiQ9NUI1.
TreeFamiTF315256.

Enzyme and pathway databases

BioCyciZFISH:HS02474-MONOMER.
BRENDAi1.3.1.34. 2681.
ReactomeiR-HSA-535734. Fatty acid, triacylglycerol, and ketone body metabolism.

Miscellaneous databases

ChiTaRSiDECR2. human.
GeneWikiiDECR2.
GenomeRNAii26063.
PROiQ9NUI1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000242612.
CleanExiHS_DECR2.
ExpressionAtlasiQ9NUI1. baseline and differential.
GenevisibleiQ9NUI1. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDECR2_HUMAN
AccessioniPrimary (citable) accession number: Q9NUI1
Secondary accession number(s): Q6ZRS7, Q96ET0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 131 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.