[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1016/S1388-1981(01)00141-X; PubMed=11514237 [NCBI, ExPASy, EBI, Israel, Japan] De Nys K., Meyhi E., Mannaerts G.P., Fransen M., Van Veldhoven P.P.; "Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase."; Biochim. Biophys. Acta 1533:66-72(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1093/hmg/10.4.339; PubMed=11157797 [NCBI, ExPASy, EBI, Israel, Japan] Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."; Hum. Mol. Genet. 10:339-352(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Testis; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature03187; PubMed=15616553 [NCBI, ExPASy, EBI, Israel, Japan] Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.; "The sequence and analysis of duplication-rich human chromosome 16."; Nature 432:988-994(2004).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). TISSUE=Lung; 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).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-61, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).

Comments

FUNCTION: 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 ACTIVITY: Trans-2,3-didehydroacyl-CoA + NADP⁺ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=59 µM for 2,4-hexadienoyl-CoA;
K_M=6 µM for 2,4-decadienoyl-CoA;
K_M=102 µM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA;
SUBCELLULAR LOCATION: Peroxisome (By similarity).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9NUI1-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9NUI1-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_013630, VSP_013631, VSP_013632.

Name	3
Isoform ID	Q9NUI1-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_013629.

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

AJ293009; CAC05664.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006463; AAK61231.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK128012; BAC87232.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL023881; CAB92744.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010740; AAH10740.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011968; AAH11968.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_065715.1; -.

UniGene

Hs.655999

3D structure databases

HSSP

Q12634; 1G0N. [HSSP ENTRY / PDB]

ModBase

Q9NUI1.

PTM databases

PhosphoSite

Q9NUI1; -.

Organism-specific databases

H-InvDB

HIX0012648; -.
HIX0079832; -.

HGNC:2754; DECR2.

PA27235; -.

Gene expression databases

ArrayExpress

Q9NUI1; -.

CleanEx

HS_DECR2; -.

GermOnline

ENSG00000103202; Homo sapiens.

Ontologies

GO:0005777;	Cellular component: peroxisome (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:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; FALSE_NEG.

ProtoNet

Q9NUI1.

Genome annotation databases

Ensembl

ENSG00000103202; Homo sapiens. [Contig view]

GeneID

26063; -.

KEGG

hsa:26063; -.

Phylogenomic databases

HOGENOM

Q9NUI1; -.

HOVERGEN

Q9NUI1; -.

Other

NextBio

47965; -.

UniRef

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

Keywords

Alternative splicing; NADP; Oxidoreductase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 292`	`292`	`Peroxisomal 2,4-dienoyl-CoA reductase.`	`PRO_0000054559`
`NP_BIND`	`33 57`	`25`	`NADP (By similarity).`
`MOTIF`	`290 292`	`3`	`Microbody targeting signal (By similarity).`
`MOD_RES`	`59 59`		`Phosphoserine.`
`MOD_RES`	`61 61`		`Phosphoserine.`
`VAR_SEQ`	`1 48`		`Missing (in isoform 3).`	`VSP_013629`
`VAR_SEQ`	`50 50`		`R -> RASEDQMGHCSSSGTCLAGVATFMVIVGKQPPNQKSRETK` `EQGRQIPFVCVR (in isoform 2).`	`VSP_013630`
`VAR_SEQ`	`114 160`		`AAGNFLCPAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFF` `RDHGGVI -> SSSSCGLPFCRCGRELPVPRWRLVLQRLQDRDGHRYQRHL` `QCVSCAL (in isoform 2).`	`VSP_013631`
`VAR_SEQ`	`161 292`		`Missing (in isoform 2).`	`VSP_013632`

Sequence information

Length: 292 AA [This is the length of the unprocessed precursor]

Molecular weight: 30778 Da [This is the MW of the unprocessed precursor]

CRC64: 9E7CD2995CE598D6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR HGCHTVIASR 

        70         80         90        100        110        120 
SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAVMAAVDQA LKEFGRIDIL INCAAGNFLC 

       130        140        150        160        170        180 
PAGALSFNAF KTVMDIDTSG TFNVSRVLYE KFFRDHGGVI VNITATLGNR GQALQVHAGS 

       190        200        210        220        230        240 
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG 

       250        260        270        280        290 
NKTEIAHSVL YLASPLASYV TGAVLVADGG AWLTFPNGVK GLPDFASFSA KL

Q9NUI1 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