Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

Pecr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity (By similarity).By similarity

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

Pathway:ifatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 4725NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • receptor binding Source: MGI
  • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.38. 3474.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
Short name:
TERP
Gene namesi
Name:Pecr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2148199. Pecr.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • peroxisomal membrane Source: UniProtKB
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 303302Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei5 – 51N6-succinyllysine1 Publication
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Modified residuei17 – 171N6-succinyllysine; alternate1 Publication
Modified residuei32 – 321N6-succinyllysine1 Publication
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei83 – 831N6-acetyllysine1 Publication
Modified residuei97 – 971N6-acetyllysine1 Publication
Modified residuei179 – 1791PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99MZ7.
PaxDbiQ99MZ7.
PRIDEiQ99MZ7.

2D gel databases

REPRODUCTION-2DPAGEQ99MZ7.

PTM databases

PhosphoSiteiQ99MZ7.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney. Expressed at lowe level in heart and skeletal muscle. Expressed at weak level in other tissues.1 Publication

Gene expression databases

BgeeiQ99MZ7.
CleanExiMM_PECR.
ExpressionAtlasiQ99MZ7. baseline and differential.
GenevisibleiQ99MZ7. MM.

Interactioni

Subunit structurei

Interacts with PEX5, probably required to target it into peroxisomes.By similarity

Protein-protein interaction databases

IntActiQ99MZ7. 2 interactions.
MINTiMINT-2514438.
STRINGi10090.ENSMUSP00000027381.

Structurei

3D structure databases

ProteinModelPortaliQ99MZ7.
SMRiQ99MZ7. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3033Microbody targeting signalBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ99MZ7.
KOiK07753.
OMAiGMHYFAH.
PhylomeDBiQ99MZ7.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99MZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSWKTGQSY LAAGLLKNQV AVVTGGGTGI GKAVSRELLH LGCNVVIASR
60 70 80 90 100
KLDRLTAAVD ELRASLPPSS SAEVSAIQCN IRKEEEVSNL VKSTLAKYGK
110 120 130 140 150
INFLVNNGGG QFMAPVEDIT AKGWHAVIET NLTGTFYMCK EVYNSWMREH
160 170 180 190 200
GGSIVNIIVL LNNGFPTAAH TGAAREGVYN LTKSMALAWA SSGVRINCVA
210 220 230 240 250
PGTIYSQTAV DNYGEMGQTL FEMAFDSIPA KRLGVPEEIS PLVCFLLSPA
260 270 280 290 300
ASYITGQLIN VDGGQALYTH AFSIPDHDNW PVGAGDLSIV KRIKESFKKK

AKL
Length:303
Mass (Da):32,410
Last modified:June 1, 2001 - v1
Checksum:i97AD4047A20B30D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891N → Y in BAB26803 (PubMed:16141072).Curated
Sequence conflicti230 – 2323AKR → VSA in AAF69800 (PubMed:10811639).Curated
Sequence conflicti241 – 2444PLVC → LLAR in AAF69800 (PubMed:10811639).Curated
Sequence conflicti268 – 2681Y → H in AAF69800 (PubMed:10811639).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232011 mRNA. Translation: AAF69800.1.
AF242204 mRNA. Translation: AAK28336.1.
AK010260 mRNA. Translation: BAB26803.1.
BC013530 mRNA. Translation: AAH13530.1.
CCDSiCCDS35607.1.
RefSeqiNP_076012.3. NM_023523.5.
UniGeneiMm.281738.

Genome annotation databases

EnsembliENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189.
GeneIDi111175.
KEGGimmu:111175.
UCSCiuc007bki.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232011 mRNA. Translation: AAF69800.1.
AF242204 mRNA. Translation: AAK28336.1.
AK010260 mRNA. Translation: BAB26803.1.
BC013530 mRNA. Translation: AAH13530.1.
CCDSiCCDS35607.1.
RefSeqiNP_076012.3. NM_023523.5.
UniGeneiMm.281738.

3D structure databases

ProteinModelPortaliQ99MZ7.
SMRiQ99MZ7. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99MZ7. 2 interactions.
MINTiMINT-2514438.
STRINGi10090.ENSMUSP00000027381.

PTM databases

PhosphoSiteiQ99MZ7.

2D gel databases

REPRODUCTION-2DPAGEQ99MZ7.

Proteomic databases

MaxQBiQ99MZ7.
PaxDbiQ99MZ7.
PRIDEiQ99MZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189.
GeneIDi111175.
KEGGimmu:111175.
UCSCiuc007bki.2. mouse.

Organism-specific databases

CTDi55825.
MGIiMGI:2148199. Pecr.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ99MZ7.
KOiK07753.
OMAiGMHYFAH.
PhylomeDBiQ99MZ7.
TreeFamiTF315256.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi1.3.1.38. 3474.

Miscellaneous databases

NextBioi365461.
PROiQ99MZ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MZ7.
CleanExiMM_PECR.
ExpressionAtlasiQ99MZ7. baseline and differential.
GenevisibleiQ99MZ7. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPECR_MOUSE
AccessioniPrimary (citable) accession number: Q99MZ7
Secondary accession number(s): Q9CX01, Q9JIF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.