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UniProtKB/Swiss-Prot entry P35700


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

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Entry information
Entry name PRDX1_MOUSE
Primary accession number P35700
Secondary accession numbers Q3UBV4 Q9CWI2
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 98)
Name and origin of the protein
Protein name Peroxiredoxin-1
Synonyms EC 1.11.1.15
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Osteoblast-specific factor 3
OSF-3
Macrophage 23 kDa stress protein
Gene name
Name: Prdx1
Synonyms: Msp23, Paga, Tdpx2
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].
TISSUE=Peritoneal macrophage;
PubMed=8360158 [NCBI, ExPASy, EBI, Israel, Japan]
Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., Sugita Y., Bannai S.;
"Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein.";
J. Biol. Chem. 268:18633-18636(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6;
TISSUE=Osteoblast;
PubMed=8089076 [NCBI, ExPASy, EBI, Israel, Japan]
Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E.;
"Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells.";
J. Biochem. 115:641-643(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvJ;
DOI=10.1016/S0378-1119(99)00413-8; PubMed=10548725 [NCBI, ExPASy, EBI, Israel, Japan]
Lee T.-H., Yu S.-L., Kim S.-U., Lee K.-K., Rhee S.G., Yu D.-Y.;
"Characterization of mouse peroxiredoxin I genomic DNA and its expression.";
Gene 239:243-250(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
TISSUE=Liver;
Hino K., Sato H., Bannai S.;
"Characterization of mouse type I peroxiredoxin gene and pseudogenes.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Hippocampus, Kidney, Liver, Mammary gland, and Stomach;
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].
STRAIN=C57BL/6;
TISSUE=Brain;
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 17-27; 111-120; 141-151 AND 159-168, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 94-109; 141-151; 159-168 AND 173-190, AND MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
Comments
  • FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). May form heterodimers with AOP2.
  • SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity).
  • TISSUE SPECIFICITY: Found in various tissues; high concentration in liver.
  • INDUCTION: By oxidative and sulfhydryl-reactive agents.
  • PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity (By similarity).
  • MISCELLANEOUS: The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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: Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized (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
D16142; BAA03713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D21252; BAA04796.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF157331; AAD45323.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF157329; AAD45323.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF157330; AAD45323.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB023564; BAA86992.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002287; BAB21990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008711; BAB25847.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010688; BAB27120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK083243; BAC38827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK145138; BAE26255.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150797; BAE29860.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK151459; BAE30417.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK167624; BAE39676.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169154; BAE40933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC083348; AAH83348.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC086648; AAH86648.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48513; A48513.
RefSeq NP_035164.1; -.
UniGene Mm.30929
3D structure databases
HSSP Q63716; 1QQ2. [HSSP ENTRY / PDB]
SMR P35700; 3-175.
ModBase P35700.
Protein family/group databases
PeroxiBase 4555; Mm2CysPrx01-1.
PTM databases
PhosphoSite P35700; -.
2D gel databases
SWISS-2DPAGE P35700; -.
REPRODUCTION-2DPAGE P35700; -.
Organism-specific databases
MGI MGI:99523; Prdx1.
Gene expression databases
ArrayExpress P35700; -.
CleanEx MM_PRDX1; -.
GermOnline ENSMUSG00000028691; Mus musculus.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0008283; Biological process: cell proliferation (inferred from mutant phenotype from MGI).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0034101; Biological process: erythrocyte homeostasis (inferred from mutant phenotype from MGI).
GO:0042267; Biological process: natural killer cell mediated cytotoxicity (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0042345; Biological process: regulation of NF-kappaB import into nucleus (inferred from mutant phenotype from MGI).
GO:0032872; Biological process: regulation of stress-activated MAPK cascade (inferred from mutant phenotype from MGI).
GO:0019430; Biological process: removal of superoxide radicals (inferred from mutant phenotype from MGI).
GO:0000302; Biological process: response to reactive oxygen species (inferred from mutant phenotype from MGI).
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).
ProtoNet P35700.
Genome annotation databases
Ensembl ENSMUSG00000028691; Mus musculus. [Contig view]
GeneID 18477; -.
KEGG mmu:18477; -.
NMPDR fig|10090.3.peg.10171; -.
Phylogenomic databases
HOGENOM P35700; -.
HOVERGEN P35700; -.
Other
NextBio 294178; -.
SOURCE Prdx1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   199  199     Peroxiredoxin-1. PRO_0000135077
DOMAIN   6   165  160     Thioredoxin. 
ACT_SITE   52    52        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   10    10        Phosphotyrosine. 
MOD_RES   90    90        Phosphothreonine (By similarity). 
MOD_RES   183   183        Phosphothreonine (By similarity). 
MOD_RES   194   194        Phosphotyrosine (By similarity). 
DISULFID   52    52        Interchain (with C-173); in linked form (By similarity). 
DISULFID   173   173        Interchain (with C-52); in linked form (By similarity). 
CONFLICT   196   196        S -> F (in Ref. 5; BAB27120). 
Sequence information
Length: 199 AA [This is the length of the unprocessed precursor] Molecular weight: 22176 Da [This is the MW of the unprocessed precursor] CRC64: BEF5C995A86124D1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF VCPTEIIAFS 

        70         80         90        100        110        120 
DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLISDPKR TIAQDYGVLK 

       130        140        150        160        170        180 
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG 

       190 
SDTIKPDVNK SKEYFSKQK 

P35700 in FASTA format

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