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Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

Pecr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity (By similarity).By similarity

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei179Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi23 – 47NADPBy similarityAdd BLAST25

GO - Molecular functioni

  • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
Short name:
TERP
Alternative name(s):
PX-2,4-DCR1
Peroxisomal 2,4-dienoyl-CoA reductase
RLF98
Gene namesi
Name:Pecr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70925. Pecr.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000547432 – 303Peroxisomal trans-2-enoyl-CoA reductaseAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineBy similarity1
Modified residuei5N6-succinyllysineBy similarity1
Modified residuei32N6-succinyllysineBy similarity1
Modified residuei49PhosphoserineBy similarity1
Modified residuei83N6-acetyllysineBy similarity1
Modified residuei97N6-acetyllysineBy similarity1
Modified residuei179PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ9WVK3.

PTM databases

iPTMnetiQ9WVK3.
PhosphoSitePlusiQ9WVK3.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney. Weakly expressed in other tissues.1 Publication

Inductioni

Up-regulated by fasting.1 Publication

Interactioni

Subunit structurei

Interacts with PEX5, probably required to target it into peroxisomes.By similarity

Protein-protein interaction databases

IntActiQ9WVK3. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliQ9WVK3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi301 – 303Microbody targeting signalBy similarity3

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG105268.
InParanoidiQ9WVK3.
KOiK07753.
PhylomeDBiQ9WVK3.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9WVK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSWKSGQSY LAAGLLQNQV AVVTGGATGI GKAISRELLH LGCNVVIASR
60 70 80 90 100
KLDRLTAAVD ELRASQPPSS STQVTAIQCN IRKEEEVNNL VKSTLAKYGK
110 120 130 140 150
INFLVNNAGG QFMAPAEDIT AKGWQAVIET NLTGTFYMCK AVYNSWMKDH
160 170 180 190 200
GGSIVNIIVL LNNGFPTAAH SGAARAGVYN LTKTMALTWA SSGVRINCVA
210 220 230 240 250
PGTIYSQTAV DNYGELGQTM FEMAFENIPA KRVGLPEEIS PLVCFLLSPA
260 270 280 290 300
ASFITGQLIN VDGGQALYTR NFTIPDHDNW PVGAGDSSFI KKVKESLKKQ

ARL
Length:303
Mass (Da):32,433
Last modified:November 1, 1999 - v1
Checksum:iF137C5517D655D7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099742 mRNA. Translation: AAD38447.1.
AF021854 mRNA. Translation: AAF14047.1.
BC060546 mRNA. Translation: AAH60546.1.
RefSeqiNP_579833.1. NM_133299.2.
UniGeneiRn.163081.

Genome annotation databases

GeneIDi113956.
KEGGirno:113956.
UCSCiRGD:70925. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099742 mRNA. Translation: AAD38447.1.
AF021854 mRNA. Translation: AAF14047.1.
BC060546 mRNA. Translation: AAH60546.1.
RefSeqiNP_579833.1. NM_133299.2.
UniGeneiRn.163081.

3D structure databases

ProteinModelPortaliQ9WVK3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVK3. 1 interactor.

PTM databases

iPTMnetiQ9WVK3.
PhosphoSitePlusiQ9WVK3.

Proteomic databases

PRIDEiQ9WVK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113956.
KEGGirno:113956.
UCSCiRGD:70925. rat.

Organism-specific databases

CTDi55825.
RGDi70925. Pecr.

Phylogenomic databases

HOVERGENiHBG105268.
InParanoidiQ9WVK3.
KOiK07753.
PhylomeDBiQ9WVK3.
TreeFamiTF315256.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

PROiQ9WVK3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPECR_RAT
AccessioniPrimary (citable) accession number: Q9WVK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.