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UniProtKB/Swiss-Prot entry P99029


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX5_MOUSE
Primary accession number P99029
Secondary accession numbers Q9QX45 Q9QZ75
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on February 21, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 81)
Name and origin of the protein
Protein name Peroxiredoxin-5, mitochondrial [Precursor]
Synonyms EC 1.11.1.15
Prx-V
Peroxisomal antioxidant enzyme
PLP
Thioredoxin reductase
Thioredoxin peroxidase PMP20
Antioxidant enzyme B166
AOEB166
Liver tissue 2D-page spot 2D-0014IV
Gene name
Name: Prdx5
Synonyms: Prdx6
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
DOI=10.1006/bbrc.2000.2231; PubMed=10679306 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.;
"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis.";
Biochem. Biophys. Res. Commun. 268:921-927(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
DOI=10.1074/jbc.274.42.29897; PubMed=10514471 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.;
"Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro.";
J. Biol. Chem. 274:29897-29904(1999).
[3]
NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION.
STRAIN=C3H/HeJ;
TISSUE=Lung;
DOI=10.1074/jbc.274.43.30451; PubMed=10521424 [NCBI, ExPASy, EBI, Israel, Japan]
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.;
"Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.";
J. Biol. Chem. 274:30451-30458(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/bbrc.2000.2430; PubMed=10753630 [NCBI, ExPASy, EBI, Israel, Japan]
Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.;
"Molecular cloning and characterization of the mouse Peroxiredoxin V gene.";
Biochem. Biophys. Res. Commun. 270:356-362(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 50-61.
TISSUE=Liver;
Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
Submitted (AUG-1998) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 72-79 AND 145-155, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 83-112 AND 156-172, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF197951; AAF04855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF124994; AAF27532.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110733; AAG13450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF208730; AAF21016.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF208729; AAF21016.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002383; BAB22058.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003332; BAB22720.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008174; AAH08174.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC7239; JC7239.
RefSeq NP_036151.1; -.
UniGene Mm.279782
3D structure databases
HSSP P30044; 1HD2. [HSSP ENTRY / PDB]
SMR P99029; 50-210.
ModBase P99029.
Protein family/group databases
PeroxiBase 4453; MmPrxV.
PTM databases
PhosphoSite P99029; -.
2D gel databases
SWISS-2DPAGE P99029; -.
REPRODUCTION-2DPAGE P99029; -.
Organism-specific databases
MGI MGI:1859821; Prdx5.
Gene expression databases
ArrayExpress P99029; -.
CleanEx MM_PRDX5; -.
MM_PRDX6; -.
GermOnline ENSMUSG00000024953; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF08534; Redoxin; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P99029.
Genome annotation databases
Ensembl ENSMUSG00000024953; Mus musculus. [Contig view]
GeneID 54683; -.
KEGG mmu:54683; -.
Phylogenomic databases
HOGENOM P99029; -.
HOVERGEN P99029; -.
Other
SOURCE Prdx5; Mus musculus.
ProtoNet P99029.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; Antioxidant; Cytoplasm; Direct protein sequencing; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    48  48     Mitochondrion (Potential). 
CHAIN   49   210  162     Peroxiredoxin-5, mitochondrial. PRO_0000023795
DOMAIN   52   210  159     Thioredoxin. 
MOTIF   208   210  3     Microbody targeting signal (By similarity). 
ACT_SITE   96    96        Cysteine sulfenic acid (-SOH) intermediate (Potential). 
DISULFID   96   200        Redox-active (By similarity). 
VAR_SEQ   1    48        Missing (in isoform Cytoplasmic+peroxisomal). VSP_018830
CONFLICT   55    55        G -> D (in Ref. 7; AA sequence). 
CONFLICT   83   102        GVLFGVPGAFTPGCSKTHLP -> VFCLESLGHLHLAVLRPTA (in Ref. 4; AAF21016). 
Sequence information
Length: 210 AA [This is the length of the unprocessed precursor] Molecular weight: 21897 Da [This is the MW of the unprocessed precursor] CRC64: E944104CC468BDD8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS 

        70         80         90        100        110        120 
VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA 

       130        140        150        160        170        180 
CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV 

       190        200        210 
IDNGIVKALN VEPDGTGLTC SLAPNILSQL 

P99029 in FASTA format

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