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Protein

Peroxiredoxin-1

Gene

Prdx1

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

Functioni

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.By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  1. heme binding Source: Ensembl
  2. identical protein binding Source: IntAct
  3. peroxidase activity Source: MGI
  4. poly(A) RNA binding Source: MGI
  5. thioredoxin peroxidase activity Source: MGI

GO - Biological processi

  1. cell proliferation Source: MGI
  2. erythrocyte homeostasis Source: MGI
  3. hydrogen peroxide catabolic process Source: MGI
  4. natural killer cell mediated cytotoxicity Source: MGI
  5. regulation of NF-kappaB import into nucleus Source: MGI
  6. regulation of stress-activated MAPK cascade Source: MGI
  7. removal of superoxide radicals Source: MGI
  8. response to oxidative stress Source: MGI
  9. response to reactive oxygen species Source: MGI
  10. retina homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4555. Mm2CysPrx01-1.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Prdx1
Synonyms:Msp23, Paga, Tdpx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:99523. Prdx1.

Subcellular locationi

Cytoplasm. Melanosome By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Ensembl
  3. extracellular space Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. melanosome Source: UniProtKB-SubCell
  6. mitochondrial matrix Source: Ensembl
  7. mitochondrion Source: MGI
  8. myelin sheath Source: UniProtKB
  9. nuclear euchromatin Source: Ensembl
  10. nucleolus Source: Ensembl
  11. nucleus Source: MGI
  12. peroxisomal matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 199198Peroxiredoxin-1PRO_0000135077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei27 – 271N6-acetyllysineBy similarity
Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
Modified residuei35 – 351N6-succinyllysine; alternate1 Publication
Disulfide bondi52 – 52Interchain (with C-173); in linked formBy similarity
Modified residuei90 – 901PhosphothreonineBy similarity
Modified residuei136 – 1361N6-acetyllysine1 Publication
Disulfide bondi173 – 173Interchain (with C-52); in linked formBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP35700.
PaxDbiP35700.
PRIDEiP35700.

2D gel databases

REPRODUCTION-2DPAGEP35700.
SWISS-2DPAGEP35700.

PTM databases

PhosphoSiteiP35700.

Expressioni

Tissue specificityi

Found in various tissues; high concentration in liver.

Inductioni

By oxidative and sulfhydryl-reactive agents.

Gene expression databases

BgeeiP35700.
CleanExiMM_PRDX1.
ExpressionAtlasiP35700. baseline and differential.
GenevestigatoriP35700.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-444948,EBI-444948
STK4Q130433EBI-444948,EBI-367376From a different organism.

Protein-protein interaction databases

BioGridi202018. 5 interactions.
IntActiP35700. 19 interactions.
MINTiMINT-1863043.

Structurei

3D structure databases

ProteinModelPortaliP35700.
SMRiP35700. Positions 3-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 165160ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35700.
KOiK13279.
OMAiKKINCEI.
OrthoDBiEOG7T1RCD.
PhylomeDBiP35700.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35700-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM
110 120 130 140 150
NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG
160 170 180 190
RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK
Length:199
Mass (Da):22,176
Last modified:June 1, 1994 - v1
Checksum:iBEF5C995A86124D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961S → F in BAB27120. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18515.1.
PIRiA48513.
RefSeqiNP_035164.1. NM_011034.4.
UniGeneiMm.30929.

Genome annotation databases

EnsembliENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691.
ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
GeneIDi18477.
KEGGimmu:18477.
UCSCiuc008uhd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18515.1.
PIRiA48513.
RefSeqiNP_035164.1. NM_011034.4.
UniGeneiMm.30929.

3D structure databases

ProteinModelPortaliP35700.
SMRiP35700. Positions 3-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202018. 5 interactions.
IntActiP35700. 19 interactions.
MINTiMINT-1863043.

Protein family/group databases

PeroxiBasei4555. Mm2CysPrx01-1.

PTM databases

PhosphoSiteiP35700.

2D gel databases

REPRODUCTION-2DPAGEP35700.
SWISS-2DPAGEP35700.

Proteomic databases

MaxQBiP35700.
PaxDbiP35700.
PRIDEiP35700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691.
ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
GeneIDi18477.
KEGGimmu:18477.
UCSCiuc008uhd.1. mouse.

Organism-specific databases

CTDi5052.
MGIiMGI:99523. Prdx1.

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35700.
KOiK13279.
OMAiKKINCEI.
OrthoDBiEOG7T1RCD.
PhylomeDBiP35700.
TreeFamiTF105181.

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi294178.
PROiP35700.
SOURCEiSearch...

Gene expression databases

BgeeiP35700.
CleanExiMM_PRDX1.
ExpressionAtlasiP35700. baseline and differential.
GenevestigatoriP35700.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPRDX1_MOUSE
AccessioniPrimary (citable) accession number: P35700
Secondary accession number(s): Q3UBV4, Q9CWI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 4, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).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).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.