[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 35-53. TISSUE=Liver; DOI=10.1016/0167-4781(90)90109-F; PubMed=2383590 [NCBI, ExPASy, EBI, Israel, Japan] Hirose A., Kamijo K., Osumi T., Hashimoto T., Mizugaki M.; "cDNA cloning of rat liver 2,4-dienoyl-CoA reductase."; Biochim. Biophys. Acta 1049:346-349(1990).
[2]	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: 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 ACTIVITY: Trans-2,3-didehydroacyl-CoA + NADP⁺ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.

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

D00569; BAA00446.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059120; AAH59120.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S11021; S11021.

NP_476545.1; -.

3D structure databases

HSSP

P29132; 1LX6. [HSSP ENTRY / PDB]

SMR

Q64591; 37-328.

ModBase

Q64591.

Organism-specific databases

RGD

70999; Decr1.

Gene expression databases

ArrayExpress

Q64591; -.

GermOnline

ENSRNOG00000008236; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0008670;	Molecular function: 2,4-dienoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

PROSITE

PS00061; ADH_SHORT; FALSE_NEG.

Genome annotation databases

Ensembl

ENSRNOG00000008236; Rattus norvegicus. [Contig view]

GeneID

117543; -.

KEGG

rno:117543; -.

Phylogenomic databases

HOVERGEN

Q64591; -.

Other

NextBio

620365; -.

UniRef

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

Keywords

Acetylation; Direct protein sequencing; Mitochondrion; NADP; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 34`	`34`	`Mitochondrion.`
`CHAIN`	`35 335`	`301`	`2,4-dienoyl-CoA reductase, mitochondrial.`	`PRO_0000031967`
`NP_BIND`	`62 94`	`33`	`NADP (By similarity).`
`ACT_SITE`	`199 199`		`Proton acceptor (By similarity).`
`BINDING`	`157 157`		`Substrate (By similarity).`
`BINDING`	`214 214`		`NADP (By similarity).`
`MOD_RES`	`106 106`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`110 110`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`11 11`		`G -> R (in Ref. 2; AAH59120).`
`CONFLICT`	`23 23`		`R -> K (in Ref. 1; BAA00446).`
`CONFLICT`	`79 79`		`L -> R (in Ref. 1; BAA00446).`
`CONFLICT`	`162 162`		`K -> R (in Ref. 1; BAA00446).`
`CONFLICT`	`190 190`		`A -> V (in Ref. 1; BAA00446).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 36133 Da [This is the MW of the unprocessed precursor]

CRC64: C4386C65E49A4D2F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALLARAFFA GVSRLPCDPG PQRFFSFGTK TLYQSIDAPQ SKFFPPILKP MLPPNAFQGK 

        70         80         90        100        110        120 
VAFITGGGTG LGKAMTTFLS SLGAQCVIAS RNIDVLKATA EEITSKTGNK VYAIRCDVRD 

       130        140        150        160        170        180 
PDMVHNTVLE LIKVAGHPDV VINNAAGNFI SPSERLSPNG WKTITDIVLN GTAYVTIEIG 

       190        200        210        220        230        240 
KQLIKAQKGA AFLAITTIYA ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP 

       250        260        270        280        290        300 
GPIKTKGAFS RLDPTGKFEK DMIERIPCGR LGTVEELANL ATFLCSDYAS WINGAVIRFD 

       310        320        330 
GGEEVFLSGE FNSLKKVTKE EWDVIEGLIR KTKGS

Q64591 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