Reviewed, UniProtKB/Swiss-Prot Q61171 (PRDX2_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-2
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Thiol-specific antioxidant protein
      Short name=TSA

Gene names

Name:	Prdx2
Synonyms:	Tdpx1, Tpx

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	198 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. It is not able to receive electrons 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. Interacts with TIPIN.
Subcellular location	Cytoplasm.
Tissue specificity	Widely expressed with highest levels in bone marrow. High levels also found in heart, brain, kidney and skeletal muscle. Lower levels in liver, lung and thymus.
Miscellaneous	The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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-51 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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	T cell proliferation Inferred from mutant phenotype. Source: MGI activation of MAPK activity Inferred from mutant phenotype. Source: MGI anti-apoptosis Ref.1 Inferred from direct assay. Source: MGI cell redox homeostasis Inferred from electronic annotation. Source: InterPro homeostasis of number of cells Inferred from mutant phenotype. Source: MGI hydrogen peroxide catabolic process Inferred from mutant phenotype. Source: MGI negative regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: MGI negative regulation of T cell differentiation Inferred from mutant phenotype. Source: MGI negative regulation of lipopolysaccharide-mediated signaling pathway Inferred from mutant phenotype. Source: MGI negative regulation of oxygen and reactive oxygen species metabolic process Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of hydrogen peroxide metabolic process Inferred from mutant phenotype. Source: MGI respiratory burst during acute inflammatory response Inferred from mutant phenotype. Source: MGI response to lipopolysaccharide Inferred from mutant phenotype. Source: MGI thymus development Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	selenium binding Traceable author statement. Source: MGI thioredoxin peroxidase activity Ref.4 Traceable author statement. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 198	197	Peroxiredoxin-2		PRO_0000135081
Regions
	Domain	6 – 164	159	Thioredoxin
Sites
	Active site	51	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Disulfide bond	51		Interchain (with C-172); in linked form By similarity
	Disulfide bond	172		Interchain (with C-51); in linked form By similarity
Experimental info
	Sequence conflict	38	1	V → M in BAB27093. Ref.5
	Sequence conflict	39	1	V → D in BAB23893. Ref.5
	Sequence conflict	69	1	G → R in BAB23893. Ref.5
	Sequence conflict	97	1	G → A in AAA69475. Ref.3
	Sequence conflict	113	1	Q → H in BAB23893. Ref.5
	Sequence conflict	124	1	I → V in BAB23893. Ref.5
	Sequence conflict	135	1	K → S in BAB23893. Ref.5
	Sequence conflict	182	1	T → N Ref.3
	Sequence conflict	182	1	T → N Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q61171-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FE216F5426F7174D	FASTA	198	21,779
	10 20 30 40 50 60 MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD 70 80 90 100 110 120 HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN 130 140 150 160 170 180 DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 190 DTIKPNVDDS KEYFSKHN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury." Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I. DNA Cell Biol. 16:311-321(1997) [PubMed: 9115640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	Oberbaeumer I. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129.
[3]	Chae H.Z., Kim H., Rhee S. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[4]	"The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution." Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I. Gene 216:197-205(1998) [PubMed: 9714804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: 129/SvJ.
[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: NOD. Tissue: Cerebellum, Small intestine and Thymus.
[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/6J. Tissue: Brain and Mammary gland.
[7]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[8]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[9]	"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors." Gotter A.L., Suppa C., Emanuel B.S. J. Mol. Biol. 366:36-52(2007) [PubMed: 17141802] [Abstract] Cited for: INTERACTION WITH TIPIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51679 mRNA. Translation: AAB01941.1. X82067 mRNA. Translation: CAA57566.1. U20611 mRNA. Translation: AAA69475.1. AF032722 , AF032718, AF032719, AF032720, AF032721 Genomic DNA. Translation: AAC35744.1. AK005225 mRNA. Translation: BAB23893.1. AK008433 mRNA. Translation: BAB25666.1. AK010653 mRNA. Translation: BAB27093.1. AK088280 mRNA. Translation: BAC40255.1. BC002034 mRNA. Translation: AAH02034.1. BC081454 mRNA. Translation: AAH81454.1.
IPI	IPI00117910.
RefSeq	NP_035693.3.
UniGene	Mm.347009 Mm.393373
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
SMR	Q61171. Positions 2-197, 3-198.
ModBase	Search...
Protein family/group databases
PeroxiBase	4474. Mm2CysPrx02.
PTM databases
PhosphoSite	Q61171.
2-D gel databases
SWISS-2DPAGE	Q61171.
REPRODUCTION-2DPAGE	Q61171.
Proteomic databases
PRIDE	Q61171.
Genome annotation databases
Ensembl	ENSMUSG00000005161. Mus musculus. [Contig view]
GeneID	21672.
KEGG	mmu:21672.
NMPDR	fig|10090.3.peg.18891.
Organism-specific databases
MGI	MGI:109486. Prdx2.
Phylogenomic databases
HOGENOM	Q61171.
HOVERGEN	Q61171.
OMA	Q61171. EISAAYN.
Enzyme and pathway databases
BRENDA	1.11.1.15. 244.
Gene expression databases
ArrayExpress	Q61171.
Bgee	Q61171.
CleanEx	MM_PRDX2.
GermOnline	ENSMUSG00000005161. 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	300952.
SOURCE	Search...

Entry information

Entry name

PRDX2_MOUSE

Accession

Primary (citable) accession number: Q61171
Secondary accession number(s): O88376 , Q60796, Q9CWJ4, Q9DB49

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)