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UniProtKB/Swiss-Prot entry O08807


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

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Entry information
Entry name PRDX4_MOUSE
Primary accession number O08807
Secondary accession number Q3U8E4
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name Peroxiredoxin-4
Synonyms EC 1.11.1.15
Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372
Antioxidant enzyme AOE372
Gene name
Name: Prdx4
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].
STRAIN=C57BL/6J;
DOI=10.1089/15230860050192288; PubMed=11229364 [NCBI, ExPASy, EBI, Israel, Japan]
Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F., Jeang K.-T., Jin D.-Y.;
"Characterization of human and mouse peroxiredoxin IV: evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species.";
Antioxid. Redox Signal. 2:507-518(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2;
TISSUE=Bone marrow, and Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NMRI;
TISSUE=Mammary gland, and 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).
[4]
PROTEIN SEQUENCE OF 190-203.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 216-226, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
Comments
  • FUNCTION: Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity).
  • MISCELLANEOUS: The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).
  • MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-127 (to Cys-SO(3)H) upon oxidative stress (By similarity).
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
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
U96746; AAB57846.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005031; BAB23758.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146402; BAE27143.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK152255; BAE31074.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003349; AAH03349.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019578; AAH19578.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_058044.1; -.
UniGene Mm.247542
3D structure databases
HSSP Q63716; 1QQ2. [HSSP ENTRY / PDB]
ModBase O08807.
Protein family/group databases
PeroxiBase 4532; Mm2CysPrx04.
2D gel databases
PMMA-2DPAGE O08807; -.
REPRODUCTION-2DPAGE O08807; -.
Organism-specific databases
MGI MGI:1859815; Prdx4.
Gene expression databases
ArrayExpress O08807; -.
CleanEx MM_PRDX4; -.
GermOnline ENSMUSG00000025289; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O08807; -.
Genome annotation databases
Ensembl ENSMUSG00000025289; Mus musculus. [Contig view]
GeneID 53381; -.
KEGG mmu:53381; -.
NMPDR fig|10090.3.peg.22366; -.
Phylogenomic databases
HOGENOM O08807; -.
HOVERGEN O08807; -.
Other
NextBio 310209; -.
SOURCE Prdx4; Mus musculus.
ProtoNet O08807.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   274  274     Peroxiredoxin-4. PRO_0000135099
DOMAIN   82   240  159     Thioredoxin. 
ACT_SITE   127   127        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
DISULFID   127   127        Interchain (with C-248); in linked form (By similarity). 
DISULFID   248   248        Interchain (with C-127); in linked form (By similarity). 
Sequence information
Length: 274 AA [This is the length of the unprocessed precursor] Molecular weight: 31053 Da [This is the MW of the unprocessed precursor] CRC64: 73DB5374EC46241C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG 

        70         80         90        100        110        120 
QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP 

       130        140        150        160        170        180 
LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL 

       190        200        210        220        230        240 
SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY 

       250        260        270 
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN 

O08807 in FASTA format

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