[1]	NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1016/S0167-4838(99)00218-6; PubMed=10561551 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Underwood L.E.; "Molecular cloning and characterization of a new fasting-inducible short-chain dehydrogenase/reductase from rat liver."; Biochim. Biophys. Acta 1435:184-190(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; Naylor D.J., Koivurantac K.T., Stines A.P., Hiltunen J.K., Hoogenraad N.J., Hoj P.B.; "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."; Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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: 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.
INDUCTION: Up-regulated by fasting.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF099742; AAD38447.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF021854; AAF14047.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC060546; AAH60546.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_579833.1; -.

UniGene

Rn.163081

3D structure databases

HSSP

P50162; 1AE1. [HSSP ENTRY / PDB]

SMR

Q9WVK3; 7-303.

ModBase

Q9WVK3.

Protein-protein interaction databases

IntAct

Q9WVK3; -.

Organism-specific databases

RGD

70925; Pecr.

Gene expression databases

ArrayExpress

Q9WVK3; -.

GermOnline

ENSRNOG00000015809; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0005777;	Cellular component: peroxisome (inferred from direct assay from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; FALSE_NEG.

BLOCKS

Q9WVK3.

Genome annotation databases

Ensembl

ENSRNOG00000015809; Rattus norvegicus. [Contig view]

GeneID

113956; -.

KEGG

rno:113956; -.

Phylogenomic databases

HOVERGEN

Q9WVK3; -.

Other

ProtoNet

Q9WVK3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Fatty acid biosynthesis; Lipid synthesis; NADP; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 303`	`303`	`Peroxisomal trans-2-enoyl-CoA reductase.`	`PRO_0000054743`
`NP_BIND`	`23 47`	`25`	`NADP (By similarity).`
`MOTIF`	`301 303`	`3`	`Microbody targeting signal (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`

Sequence information

Length: 303 AA [This is the length of the unprocessed precursor]

Molecular weight: 32433 Da [This is the MW of the unprocessed precursor]

CRC64: F137C5517D655D7B [This is a checksum on the sequence]

        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

Q9WVK3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools