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P35700

- PRDX1_MOUSE

UniProt

P35700 - PRDX1_MOUSE

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Protein

Peroxiredoxin-1

Gene
Prdx1, Msp23, Paga, Tdpx2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 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) intermediate By similarity

GO - Molecular functioni

  1. heme binding Source: Ensembl
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct
  4. thioredoxin peroxidase activity Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: MGI
  2. erythrocyte homeostasis Source: MGI
  3. hydrogen peroxide catabolic process Source: Ensembl
  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
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. cytosol Source: Ensembl
  2. melanosome Source: UniProtKB-SubCell
  3. mitochondrial matrix Source: Ensembl
  4. mitochondrion Source: MGI
  5. nuclear euchromatin Source: Ensembl
  6. nucleolus Source: Ensembl
  7. 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 – 11Removed By similarity
Chaini2 – 199198Peroxiredoxin-1PRO_0000135077Add
BLAST

Amino acid modifications

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

ArrayExpressiP35700.
BgeeiP35700.
CleanExiMM_PRDX1.
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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi202018. 5 interactions.
IntActiP35700. 18 interactions.
MINTiMINT-1863043.

Structurei

3D structure databases

ProteinModelPortaliP35700.
SMRiP35700. Positions 3-199.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 165160ThioredoxinAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35700.
KOiK13279.
OMAiFKKINCE.
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

MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF    50
VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM 100
NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG 150
RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK 199
Length:199
Mass (Da):22,176
Last modified:June 1, 1994 - v1
Checksum:iBEF5C995A86124D1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961S → F in BAB27120. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18515.1.
PIRi A48513.
RefSeqi NP_035164.1. NM_011034.4.
UniGenei Mm.30929.

3D structure databases

ProteinModelPortali P35700.
SMRi P35700. Positions 3-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202018. 5 interactions.
IntActi P35700. 18 interactions.
MINTi MINT-1863043.

Protein family/group databases

PeroxiBasei 4555. Mm2CysPrx01-1.

PTM databases

PhosphoSitei P35700.

2D gel databases

REPRODUCTION-2DPAGE P35700.
SWISS-2DPAGE P35700.

Proteomic databases

MaxQBi P35700.
PaxDbi P35700.
PRIDEi P35700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000106470 ; ENSMUSP00000102078 ; ENSMUSG00000028691 .
ENSMUST00000135573 ; ENSMUSP00000114159 ; ENSMUSG00000028691 .
GeneIDi 18477.
KEGGi mmu:18477.
UCSCi uc008uhd.1. mouse.

Organism-specific databases

CTDi 5052.
MGIi MGI:99523. Prdx1.

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00390000004653.
HOGENOMi HOG000022343.
HOVERGENi HBG000286.
InParanoidi P35700.
KOi K13279.
OMAi FKKINCE.
OrthoDBi EOG7T1RCD.
PhylomeDBi P35700.
TreeFami TF105181.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 294178.
PROi P35700.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35700.
Bgeei P35700.
CleanExi MM_PRDX1.
Genevestigatori P35700.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000239. AHPC. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 148 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.
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.

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

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