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Reviewed, UniProtKB/Swiss-Prot Q99MZ7 (PECR_MOUSE)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisomal trans-2-enoyl-CoA reductase
    EC=1.3.1.38
Gene names
Name: Pecr
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processFatty acid biosynthesis
Lipid synthesis
   Cellular componentPeroxisome
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: UniProtKB

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Peroxisomal trans-2-enoyl-CoA reductase
PRO_0000054741

Regions

Nucleotide binding23 – 4725NADP By similarity
Motif301 – 3033Microbody targeting signal By similarity

Sites

Active site1791Proton acceptor By similarity

Amino acid modifications

Modified residue1791Phosphotyrosine By similarity

Experimental info

Sequence conflict891N → Y in BAB26803. Ref.3
Sequence conflict230 – 2323AKR → VSA in AAF69800. Ref.1
Sequence conflict241 – 2444PLVC → LLAR in AAF69800. Ref.1
Sequence conflict2681Y → H in AAF69800. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99MZ7-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 97AD4047A20B30D0

FASTA30332,410
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

AF232011 mRNA. Translation: AAF69800.1.
AF242204 mRNA. Translation: AAK28336.1.
AK010260 mRNA. Translation: BAB26803.1.
BC013530 mRNA. Translation: AAH13530.1.
IPIIPI00331596.
RefSeqNP_076012.3.
UniGeneMm.281738

3D structure databases

HSSPHSSP built from PDB template 1AE1 based on UniProtKB P50162.
SMRQ99MZ7. Positions 7-303.
ModBaseSearch...

PTM databases

PhosphoSiteQ99MZ7.

2-D gel databases

REPRODUCTION-2DPAGEQ99MZ7.

Proteomic databases

PRIDEQ99MZ7.

Genome annotation databases

EnsemblENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189; Mus musculus. [Genome view]
GeneID111175.
KEGGmmu:111175.
UCSCuc007bki.1. mouse.

Organism-specific databases

CTD111175.
MGIMGI:2148199. Pecr.

Phylogenomic databases

HOGENOMQ99MZ7.
HOVERGENQ99MZ7.
OMAARVIPIQ.

Enzyme and pathway databases

BRENDA1.3.1.38. 244.

Gene expression databases

ArrayExpressQ99MZ7.
BgeeQ99MZ7.
CleanExMM_PECR.
GenevestigatorQ99MZ7.
GermOnlineENSMUSG00000026189. Mus musculus.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio365461.
SOURCESearch...

Entry information

Entry namePECR_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents