Q9NUI1 (DECR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal 2,4-dienoyl-CoA reductase
Short name=pDCR
EC=1.3.1.34

Alternative name(s):
2,4-dienoyl-CoA reductase 2

Gene names

Name:	DECR2
Synonyms:	PDCR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Ref.1
Subcellular location	Peroxisome By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=59 µM for 2,4-hexadienoyl-CoA Ref.1 KM=6 µM for 2,4-decadienoyl-CoA KM=102 µM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2,4-dienoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NUI1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NUI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: R → RASEDQMGHCSSSGTCLAGVATFMVIVGKQPPNQKSRETKEQGRQIPFVCVR
     114-160: AAGNFLCPAG...KFFRDHGGVI → SSSSCGLPFC...RHLQCVSCAL
     161-292: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NUI1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	Peroxisomal 2,4-dienoyl-CoA reductase		PRO_0000054559
Regions
	Nucleotide binding	33 – 57	25	NADP By similarity
	Motif	290 – 292	3	Microbody targeting signal By similarity
Amino acid modifications
	Modified residue	59	1	Phosphoserine Ref.6
	Modified residue	61	1	Phosphoserine Ref.6
	Modified residue	151	1	N6-acetyllysine Ref.7
	Modified residue	291	1	N6-acetyllysine Ref.7
Natural variations
	Alternative sequence	1 – 48	48	Missing in isoform 3.		VSP_013629
	Alternative sequence	50	1	R → RASEDQMGHCSSSGTCLAGV ATFMVIVGKQPPNQKSRETK EQGRQIPFVCVR in isoform 2.		VSP_013630
	Alternative sequence	114 – 160	47	AAGNF…HGGVI → SSSSCGLPFCRCGRELPVPR WRLVLQRLQDRDGHRYQRHL QCVSCAL in isoform 2.		VSP_013631
	Alternative sequence	161 – 292	132	Missing in isoform 2.		VSP_013632

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 9E7CD2995CE598D6	FASTA	292	30,778
	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
	Isoform 2 [UniParc]. Checksum: 34B6F2CFF91F1827	FASTA	211	23,130
	10 20 30 40 50 60 MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR ASEDQMGHCS 70 80 90 100 110 120 SSGTCLAGVA TFMVIVGKQP PNQKSRETKE QGRQIPFVCV RHGCHTVIAS RSLPRVLTAA 130 140 150 160 170 180 RKLAGATGRR CLPLSMDVRA PPAVMAAVDQ ALKEFGRIDI LINCSSSSCG LPFCRCGREL 190 200 210 PVPRWRLVLQ RLQDRDGHRY QRHLQCVSCA L
	Isoform 3 [UniParc]. Checksum: CF192E5F987E311C	FASTA	244	25,589
	10 20 30 40 50 60 MRHGCHTVIA SRSLPRVLTA ARKLAGATGR RCLPLSMDVR APPAVMAAVD QALKEFGRID 70 80 90 100 110 120 ILINCAAGNF LCPAGALSFN AFKTVMDIDT SGTFNVSRVL YEKFFRDHGG VIVNITATLG 130 140 150 160 170 180 NRGQALQVHA GSAKAAVDAM TRHLAVEWGP QNIRVNSLAP GPISGTEGLR RLGGPQASLS 190 200 210 220 230 240 TKVTASPLQR LGNKTEIAHS VLYLASPLAS YVTGAVLVAD GGAWLTFPNG VKGLPDFASF SAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase." De Nys K., Meyhi E., Mannaerts G.P., Fransen M., Van Veldhoven P.P. Biochim. Biophys. Acta 1533:66-72(2001) [PubMed: 11514237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." 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. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[4]	"The sequence and analysis of duplication-rich human chromosome 16." 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. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORMS 1 AND 3). Tissue: Lung.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-61, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151 AND LYS-291, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ293009 mRNA. Translation: CAC05664.1. AE006463 Genomic DNA. Translation: AAK61231.1. AK128012 mRNA. Translation: BAC87232.1. AL023881 Genomic DNA. Translation: CAB92744.1. BC010740 mRNA. Translation: AAH10740.1. BC011968 mRNA. Translation: AAH11968.1.
IPI	IPI00010190. IPI00444050. IPI00640806.
RefSeq	NP_065715.1. NM_020664.3.
UniGene	Hs.628831.
3D structure databases
ProteinModelPortal	Q9NUI1.
SMR	Q9NUI1. Positions 26-274.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NUI1. 2 interactions.
STRING	Q9NUI1.
PTM databases
PhosphoSite	Q9NUI1.
Polymorphism databases
DMDM	84029527.
Proteomic databases
PRIDE	Q9NUI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219481; ENSP00000219481; ENSG00000242612.
GeneID	26063.
KEGG	hsa:26063.
UCSC	uc002chb.1. human. uc010bqv.1. human.
Organism-specific databases
CTD	26063.
GeneCards	GC16P000451.
H-InvDB	HIX0012648. HIX0079832.
HGNC	HGNC:2754. DECR2.
neXtProt	NX_Q9NUI1.
PharmGKB	PA27235.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00600000084005.
HOGENOM	HBG750976.
HOVERGEN	HBG100327.
InParanoid	Q9NUI1.
OMA	FRDHGGV.
OrthoDB	EOG4JWVF4.
PhylomeDB	Q9NUI1.
Gene expression databases
ArrayExpress	Q9NUI1.
Bgee	Q9NUI1.
CleanEx	HS_DECR2.
Genevestigator	Q9NUI1.
GermOnline	ENSG00000103202. Homo sapiens.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K13237.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	47965.

Entry information

Entry name

DECR2_HUMAN

Accession

Primary (citable) accession number: Q9NUI1
Secondary accession number(s): Q6ZRS7, Q96ET0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.