Reviewed, UniProtKB/Swiss-Prot P35700 (PRDX1_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-1
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 2
    Thioredoxin-dependent peroxide reductase 2
    Osteoblast-specific factor 3
      Short name=OSF-3
    Macrophage 23 kDa stress protein

Gene names

Name:	Prdx1
Synonyms:	Msp23, Paga, Tdpx2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
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.
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 component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Inferred from mutant phenotype. Source: MGI cell redox homeostasis Inferred from electronic annotation. Source: InterPro erythrocyte homeostasis Inferred from mutant phenotype. Source: MGI natural killer cell mediated cytotoxicity Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of NF-kappaB import into nucleus Inferred from mutant phenotype. Source: MGI regulation of stress-activated MAPK cascade Inferred from mutant phenotype. Source: MGI removal of superoxide radicals Inferred from mutant phenotype. Source: MGI response to reactive oxygen species Inferred from mutant phenotype. Source: MGI
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 199	199	Peroxiredoxin-1		PRO_0000135077
Regions
	Domain	6 – 165	160	Thioredoxin
Sites
	Active site	52	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	10	1	Phosphotyrosine Ref.8
	Modified residue	90	1	Phosphothreonine By similarity
	Modified residue	183	1	Phosphothreonine By similarity
	Modified residue	194	1	Phosphotyrosine By similarity
	Disulfide bond	52		Interchain (with C-173); in linked form By similarity
	Disulfide bond	173		Interchain (with C-52); in linked form By similarity
Experimental info
	Sequence conflict	196	1	S → F in BAB27120. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P35700-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: BEF5C995A86124D1	FASTA	199	22,176
	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

References

	« Hide 'large scale' referencesShow '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: 8360158] [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: 8089076] [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: 10548725] [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: 16141072] [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: 15489334] [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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[8]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00121788.
PIR	A48513.
RefSeq	NP_035164.1.
UniGene	Mm.30929
3D structure databases
HSSP	HSSP built from PDB template 1QQ2 based on UniProtKB Q63716.
SMR	P35700. Positions 3-175.
ModBase	Search...
Protein family/group databases
PeroxiBase	4555. Mm2CysPrx01-1.
PTM databases
PhosphoSite	P35700.
2-D gel databases
SWISS-2DPAGE	P35700.
REPRODUCTION-2DPAGE	P35700.
Proteomic databases
PRIDE	P35700.
Genome annotation databases
Ensembl	ENSMUSG00000028691. Mus musculus. [Contig view]
GeneID	18477.
KEGG	mmu:18477.
NMPDR	fig|10090.3.peg.10171.
Organism-specific databases
MGI	MGI:99523. Prdx1.
Phylogenomic databases
HOGENOM	P35700.
HOVERGEN	P35700.
OMA	P35700. IPLVSDT.
Enzyme and pathway databases
BRENDA	1.11.1.15. 244.
Gene expression databases
ArrayExpress	P35700.
Bgee	P35700.
CleanEx	MM_PRDX1.
GermOnline	ENSMUSG00000028691. Mus musculus.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	294178.
SOURCE	Search...

Entry information

Entry name

PRDX1_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)