Reviewed, UniProtKB/Swiss-Prot Q99MZ7 (PECR_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxisomal trans-2-enoyl-CoA reductase
    EC=1.3.1.38

Gene names

Name:

Pecr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Expressed at lowe level in heart and skeletal muscle. Expressed at weak level in other tissues. Ref.1
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Peroxisome
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: UniProtKB peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Peroxisomal trans-2-enoyl-CoA reductase		PRO_0000054741
Regions
	Nucleotide binding	23 – 47	25	NADP By similarity
	Motif	301 – 303	3	Microbody targeting signal By similarity
Sites
	Active site	179	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	179	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	89	1	N → Y in BAB26803. Ref.3
	Sequence conflict	230 – 232	3	AKR → VSA in AAF69800. Ref.1
	Sequence conflict	241 – 244	4	PLVC → LLAR in AAF69800. Ref.1
	Sequence conflict	268	1	Y → H in AAF69800. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99MZ7-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 97AD4047A20B30D0	FASTA	303	32,410
	10 20 30 40 50 60 MGSWKTGQSY LAAGLLKNQV AVVTGGGTGI GKAVSRELLH LGCNVVIASR KLDRLTAAVD 70 80 90 100 110 120 ELRASLPPSS SAEVSAIQCN IRKEEEVSNL VKSTLAKYGK INFLVNNGGG QFMAPVEDIT 130 140 150 160 170 180 AKGWHAVIET NLTGTFYMCK EVYNSWMREH GGSIVNIIVL LNNGFPTAAH TGAAREGVYN 190 200 210 220 230 240 LTKSMALAWA SSGVRINCVA PGTIYSQTAV DNYGEMGQTL FEMAFDSIPA KRLGVPEEIS 250 260 270 280 290 300 PLVCFLLSPA ASYITGQLIN VDGGQALYTH AFSIPDHDNW PVGAGDLSIV KRIKESFKKK AKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs." Das A.K., Uhler M.D., Hajra A.K. J. Biol. Chem. 275:24333-24340(2000) [PubMed: 10811639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology." Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M. Comb. Chem. High Throughput Screen. 4:545-552(2001) [PubMed: 11669066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[4]	"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]. Strain: FVB/N. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF232011 mRNA. Translation: AAF69800.1. AF242204 mRNA. Translation: AAK28336.1. AK010260 mRNA. Translation: BAB26803.1. BC013530 mRNA. Translation: AAH13530.1.
IPI	IPI00331596.
RefSeq	NP_076012.3.
UniGene	Mm.281738
3D structure databases
HSSP	HSSP built from PDB template 1AE1 based on UniProtKB P50162.
SMR	Q99MZ7. Positions 7-303.
ModBase	Search...
PTM databases
PhosphoSite	Q99MZ7.
2-D gel databases
REPRODUCTION-2DPAGE	Q99MZ7.
Proteomic databases
PRIDE	Q99MZ7.
Genome annotation databases
Ensembl	ENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189; Mus musculus. [Genome view]
GeneID	111175.
KEGG	mmu:111175.
UCSC	uc007bki.1. mouse.
Organism-specific databases
CTD	111175.
MGI	MGI:2148199. Pecr.
Phylogenomic databases
HOGENOM	Q99MZ7.
HOVERGEN	Q99MZ7.
OMA	ARVIPIQ.
Enzyme and pathway databases
BRENDA	1.3.1.38. 244.
Gene expression databases
ArrayExpress	Q99MZ7.
Bgee	Q99MZ7.
CleanEx	MM_PECR.
Genevestigator	Q99MZ7.
GermOnline	ENSMUSG00000026189. Mus musculus.
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.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	365461.
SOURCE	Search...

Entry information

Entry name

PECR_MOUSE

Accession

Primary (citable) accession number: Q99MZ7
Secondary accession number(s): Q9CX01, Q9JIF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)