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Reviewed, UniProtKB/Swiss-Prot Q9WVK3 (PECR_RAT)

Last modified October 13, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Peroxisomal trans-2-enoyl-CoA reductase
    EC=1.3.1.38
Alternative name(s):
    RLF98
    Peroxisomal 2,4-dienoyl-CoA reductase
    PX-2,4-DCR1
Gene names
Name: Pecr
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

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

Subcellular location

Peroxisome By similarity.

Tissue specificity

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

Induction

Up-regulated by fasting. Ref.1

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentPeroxisome
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome

Inferred from direct assay. Source: HGNC

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

trans-2-enoyl-CoA reductase (NADPH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Peroxisomal trans-2-enoyl-CoA reductase
PRO_0000054743

Regions

Nucleotide binding23 – 4725NADP By similarity
Motif301 – 3033Microbody targeting signal By similarity

Sites

Active site1791Proton acceptor By similarity

Amino acid modifications

Modified residue1791Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVK3-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F137C5517D655D7B

FASTA30332,433
        10         20         30         40         50         60 
MGSWKSGQSY LAAGLLQNQV AVVTGGATGI GKAISRELLH LGCNVVIASR KLDRLTAAVD 

        70         80         90        100        110        120 
ELRASQPPSS STQVTAIQCN IRKEEEVNNL VKSTLAKYGK INFLVNNAGG QFMAPAEDIT 

       130        140        150        160        170        180 
AKGWQAVIET NLTGTFYMCK AVYNSWMKDH GGSIVNIIVL LNNGFPTAAH SGAARAGVYN 

       190        200        210        220        230        240 
LTKTMALTWA SSGVRINCVA PGTIYSQTAV DNYGELGQTM FEMAFENIPA KRVGLPEEIS 

       250        260        270        280        290        300 
PLVCFLLSPA ASFITGQLIN VDGGQALYTR NFTIPDHDNW PVGAGDSSFI KKVKESLKKQ 


ARL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a new fasting-inducible short-chain dehydrogenase/reductase from rat liver."
Zhang J., Underwood L.E.
Biochim. Biophys. Acta 1435:184-190(1999) [PubMed: 10561551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Mitochondria and peroxisomes contain distinct isoforms of 2,4-dienoyl CoA reductase that interact with an Hsp70 member: isolation and characterisation of a cDNA encoding rat peroxisomal 2,4-dienoyl CoA reductase."
Naylor D.J., Koivurantac K.T., Stines A.P., Hiltunen J.K., Hoogenraad N.J., Hoj P.B.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF099742 mRNA. Translation: AAD38447.1.
AF021854 mRNA. Translation: AAF14047.1.
BC060546 mRNA. Translation: AAH60546.1.
IPIIPI00326195.
RefSeqNP_579833.1.
UniGeneRn.163081

3D structure databases

HSSPHSSP built from PDB template 1AE1 based on UniProtKB P50162.
SMRQ9WVK3. Positions 7-303.
ModBaseSearch...

Proteomic databases

PRIDEQ9WVK3.

Genome annotation databases

EnsemblENSRNOT00000021512; ENSRNOP00000021512; ENSRNOG00000015809; Rattus norvegicus. [Genome view]
GeneID113956.
KEGGrno:113956.

Organism-specific databases

CTD113956.
RGD70925. Pecr.

Phylogenomic databases

HOVERGENQ9WVK3.

Enzyme and pathway databases

BRENDA1.3.1.38. 248.

Gene expression databases

ArrayExpressQ9WVK3.
GenevestigatorQ9WVK3.
GermOnlineENSRNOG00000015809. 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

NextBio618083.

Entry information

Entry namePECR_RAT
AccessionPrimary (citable) accession number: Q9WVK3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1999
Last modified: October 13, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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