P35700 (PRDX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Prdx1
Synonyms:	Msp23, Paga, Tdpx2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Regulates GDPD5 function by reducing an intramolecular disulfide bond By similarity. Cooperates with GDPD5 to drive postmitotic motor neuron differentiation. Ref.9
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.9
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	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell 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: Compara 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
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI nuclear euchromatin Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara peroxisomal matrix Inferred from electronic annotation. Source: Compara
Molecular_function	heme binding Inferred from electronic annotation. Source: Compara thioredoxin peroxidase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-444948,EBI-444948
STK4	Q13043	3	EBI-444948,EBI-367376	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 199	198	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	2	1	N-acetylserine By similarity
	Modified residue	7	1	N6-acetyllysine By similarity
	Modified residue	10	1	Phosphotyrosine Ref.8
	Modified residue	16	1	N6-acetyllysine By similarity
	Modified residue	27	1	N6-acetyllysine By similarity
	Modified residue	35	1	N6-acetyllysine By similarity
	Modified residue	90	1	Phosphothreonine 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 [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] [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, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, MASS SPECTROMETRY. Tissue: Brain.
[9]	"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.
+	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.
IPI	IPI00121788.
PIR	A48513.
RefSeq	NP_035164.1. NM_011034.4.
UniGene	Mm.30929.
3D structure databases
ProteinModelPortal	P35700.
SMR	P35700. Positions 3-199.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35700. 11 interactions.
MINT	MINT-1863043.
Protein family/group databases
PeroxiBase	4555. Mm2CysPrx01-1.
PTM databases
PhosphoSite	P35700.
2D gel databases
REPRODUCTION-2DPAGE	P35700.
SWISS-2DPAGE	P35700.
Proteomic databases
PaxDb	P35700.
PRIDE	P35700.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691. ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
GeneID	18477.
KEGG	mmu:18477.
Organism-specific databases
CTD	5052.
MGI	MGI:99523. Prdx1.
Phylogenomic databases
eggNOG	COG0450.
GeneTree	ENSGT00390000004653.
HOGENOM	HOG000022343.
HOVERGEN	HBG000286.
InParanoid	P35700.
KO	K13279.
OMA	TISTDYG.
Gene expression databases
ArrayExpress	P35700.
Bgee	P35700.
CleanEx	MM_PRDX1.
Genevestigator	P35700.
GermOnline	ENSMUSG00000028691. Mus musculus.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PIRSF	PIRSF000239. AHPC. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	April 3, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program