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P35700 (PRDX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin-1

EC=1.11.1.15
Alternative name(s):
Macrophage 23 kDa stress protein
Osteoblast-specific factor 3
Short name=OSF-3
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene names
Name:Prdx1
Synonyms:Msp23, Paga, Tdpx2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 H2O2. Regulates GDPD5 function by reducing an intramolecular disulfide bond By similarity. Cooperates with GDPD5 to drive postmitotic motor neuron differentiation. Ref.8

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.

Subcellular location

Cytoplasm. Melanosome By similarity.

Tissue specificity

Found in various tissues; high concentration in liver.

Induction

By oxidative and sulfhydryl-reactive agents.

Post-translational modification

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity By similarity.

Disruption phenotype

Mice embryos loss approximately 50% of Islet1/Islet2+ and HB9+ motor neurons, whereas dorsal-ventral patterning events and the numbers of Olig2+ progenitors are normal. Toward the end of the cell death phase they have equivalent numbers of motor neurons as wild type embryos. Ref.8

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.

Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized By similarity.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype PubMed 12891360. Source: MGI

erythrocyte homeostasis

Inferred from mutant phenotype PubMed 12891360. Source: MGI

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: Ensembl

natural killer cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 12891360. Source: MGI

regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype PubMed 15858817. Source: MGI

regulation of stress-activated MAPK cascade

Inferred from mutant phenotype PubMed 16880205. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 16170382PubMed 16880205. Source: MGI

response to oxidative stress

Inferred from direct assay Ref.1. Source: MGI

response to reactive oxygen species

Inferred from mutant phenotype PubMed 12891360PubMed 16170382PubMed 16297875. Source: MGI

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

nuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheme binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 21516123. Source: IntAct

protein binding

Inferred from physical interaction PubMed 21516123. Source: IntAct

thioredoxin peroxidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-444948,EBI-444948
STK4Q130433EBI-444948,EBI-367376From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 199198Peroxiredoxin-1
PRO_0000135077

Regions

Domain6 – 165160Thioredoxin

Sites

Active site521Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue71N6-acetyllysine By similarity
Modified residue161N6-acetyllysine By similarity
Modified residue271N6-acetyllysine By similarity
Modified residue351N6-acetyllysine; alternate By similarity
Modified residue351N6-succinyllysine; alternate Ref.9
Modified residue901Phosphothreonine By similarity
Modified residue1361N6-acetyllysine Ref.9
Disulfide bond52Interchain (with C-173); in linked form By similarity
Disulfide bond173Interchain (with C-52); in linked form By similarity

Experimental info

Sequence conflict1961S → F in BAB27120. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P35700 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: BEF5C995A86124D1

FASTA19922,176
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein."
Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., Sugita Y., Bannai S.
J. Biol. Chem. 268:18633-18636(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peritoneal macrophage.
[2]"Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells."
Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E.
J. Biochem. 115:641-643(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Osteoblast.
[3]"Characterization of mouse peroxiredoxin I genomic DNA and its expression."
Lee T.-H., Yu S.-L., Kim S.-U., Lee K.-K., Rhee S.G., Yu D.-Y.
Gene 239:243-250(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
[4]"Characterization of mouse type I peroxiredoxin gene and pseudogenes."
Hino K., Sato H., Bannai S.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
Tissue: Liver.
[5]"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.
Tissue: Bone marrow, Hippocampus, Kidney, Liver, Mammary gland and Stomach.
[6]"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: C57BL/6.
Tissue: Brain.
[7]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 17-27; 94-109; 111-120; 141-151; 159-168 AND 173-190, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[8]"The antioxidant enzyme Prdx1 controls neuronal differentiation by thiol-redox-dependent activation of GDE2."
Yan Y., Sabharwal P., Rao M., Sockanathan S.
Cell 138:1209-1221(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"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 LYS-136, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16142 mRNA. Translation: BAA03713.1.
D21252 mRNA. Translation: BAA04796.1.
AF157331, AF157329, AF157330 Genomic DNA. Translation: AAD45323.1.
AB023564 Genomic DNA. Translation: BAA86992.1.
AK002287 mRNA. Translation: BAB21990.1.
AK008711 mRNA. Translation: BAB25847.1.
AK010688 mRNA. Translation: BAB27120.1.
AK083243 mRNA. Translation: BAC38827.1.
AK145138 mRNA. Translation: BAE26255.1.
AK150797 mRNA. Translation: BAE29860.1.
AK151459 mRNA. Translation: BAE30417.1.
AK167624 mRNA. Translation: BAE39676.1.
AK169154 mRNA. Translation: BAE40933.1.
BC083348 mRNA. Translation: AAH83348.1.
BC086648 mRNA. Translation: AAH86648.1.
CCDSCCDS18515.1.
PIRA48513.
RefSeqNP_035164.1. NM_011034.4.
UniGeneMm.30929.

3D structure databases

ProteinModelPortalP35700.
SMRP35700. Positions 3-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202018. 5 interactions.
IntActP35700. 18 interactions.
MINTMINT-1863043.

Protein family/group databases

PeroxiBase4555. Mm2CysPrx01-1.

PTM databases

PhosphoSiteP35700.

2D gel databases

REPRODUCTION-2DPAGEP35700.
SWISS-2DPAGEP35700.

Proteomic databases

MaxQBP35700.
PaxDbP35700.
PRIDEP35700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691.
ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
GeneID18477.
KEGGmmu:18477.
UCSCuc008uhd.1. mouse.

Organism-specific databases

CTD5052.
MGIMGI:99523. Prdx1.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00390000004653.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidP35700.
KOK13279.
OMAFKKINCE.
OrthoDBEOG7T1RCD.
PhylomeDBP35700.
TreeFamTF105181.

Gene expression databases

ArrayExpressP35700.
BgeeP35700.
CleanExMM_PRDX1.
GenevestigatorP35700.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294178.
PROP35700.
SOURCESearch...

Entry information

Entry namePRDX1_MOUSE
AccessionPrimary (citable) accession number: P35700
Secondary accession number(s): Q3UBV4, Q9CWI2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 147 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

MGD cross-references

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