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Q99MZ7 (PECR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal trans-2-enoyl-CoA reductase

Short name=TERP
EC=1.3.1.38
Gene names
Name:Pecr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 303302Peroxisomal 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 residue21N-acetylglycine Ref.5
Modified residue51N6-succinyllysine Ref.5
Modified residue171N6-acetyllysine; alternate Ref.6
Modified residue171N6-succinyllysine; alternate Ref.5
Modified residue321N6-succinyllysine Ref.5
Modified residue831N6-acetyllysine Ref.6
Modified residue971N6-acetyllysine Ref.6

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-17 AND LYS-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF232011 mRNA. Translation: AAF69800.1.
AF242204 mRNA. Translation: AAK28336.1.
AK010260 mRNA. Translation: BAB26803.1.
BC013530 mRNA. Translation: AAH13530.1.
RefSeqNP_076012.3. NM_023523.5.
UniGeneMm.281738.

3D structure databases

ProteinModelPortalQ99MZ7.
SMRQ99MZ7. Positions 7-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99MZ7. 2 interactions.
MINTMINT-2514438.

PTM databases

PhosphoSiteQ99MZ7.

2D gel databases

REPRODUCTION-2DPAGEQ99MZ7.

Proteomic databases

PaxDbQ99MZ7.
PRIDEQ99MZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189.
GeneID111175.
KEGGmmu:111175.
UCSCuc007bki.2. mouse.

Organism-specific databases

CTD55825.
MGIMGI:2148199. Pecr.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00740000115347.
HOVERGENHBG105268.
InParanoidQ99MZ7.
KOK07753.
OMAAYEWGHA.
PhylomeDBQ99MZ7.
TreeFamTF315256.

Enzyme and pathway databases

UniPathwayUPA00094.

Gene expression databases

ArrayExpressQ99MZ7.
BgeeQ99MZ7.
CleanExMM_PECR.
GenevestigatorQ99MZ7.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

NextBio365461.
PROQ99MZ7.
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: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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