O08807 (PRDX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-4
EC=1.11.1.15

Alternative name(s):
Antioxidant enzyme AOE372
Peroxiredoxin IV
Short name=Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372

Gene names

Name:

Prdx4

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 › Mus

Protein attributes

Sequence length	274 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	Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.
Subcellular location	Cytoplasm By similarity. Secreted By similarity.
Miscellaneous	The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-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. Irreversibly inactivated by overoxidation of Cys-127 (to Cys-SO3H) upon oxidative stress By similarity.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm Secreted
Domain	Redox-active center Signal
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW 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
	Signal peptide	1 – 40	40	By similarity
	Chain	41 – 274	234	Peroxiredoxin-4		PRO_0000135099
Regions
	Domain	82 – 240	159	Thioredoxin
Sites
	Active site	127	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	127		Interchain (with C-248); in linked form By similarity
	Disulfide bond	248		Interchain (with C-127); in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08807 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 73DB5374EC46241C	FASTA	274	31,053
	10 20 30 40 50 60 MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG 70 80 90 100 110 120 QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP 130 140 150 160 170 180 LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL 190 200 210 220 230 240 SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY 250 260 270 TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human and mouse peroxiredoxin IV: evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species." Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F., Jeang K.-T., Jin D.-Y. Antioxid. Redox Signal. 2:507-518(2000) [PubMed: 11229364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"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 and DBA/2. Tissue: Bone marrow and Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	"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 and NMRI. Tissue: Mammary gland and Mammary tumor.
[5]	Lubec G., Kang S.U., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 190-203 AND 216-226. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U96746 mRNA. Translation: AAB57846.1. AK005031 mRNA. Translation: BAB23758.1. AK146402 mRNA. Translation: BAE27143.1. AK152255 mRNA. Translation: BAE31074.1. BX005263 Genomic DNA. Translation: CAM23139.1. BC003349 mRNA. Translation: AAH03349.1. BC019578 mRNA. Translation: AAH19578.1.
IPI	IPI00116254.
RefSeq	NP_058044.1. NM_016764.4.
UniGene	Mm.247542.
3D structure databases
ProteinModelPortal	O08807.
SMR	O08807. Positions 78-274.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08807. 1 interaction.
STRING	O08807.
Protein family/group databases
PeroxiBase	4532. Mm2CysPrx04.
2D gel databases
PMMA-2DPAGE	O08807.
REPRODUCTION-2DPAGE	O08807.
Proteomic databases
PRIDE	O08807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289.
GeneID	53381.
KEGG	mmu:53381.
NMPDR	fig|10090.3.peg.22366.
UCSC	uc009uru.1. mouse.
Organism-specific databases
CTD	10549.
MGI	MGI:1859815. Prdx4.
Phylogenomic databases
eggNOG	roNOG06597.
GeneTree	ENSGT00390000004653.
HOGENOM	HBG493509.
HOVERGEN	HBG000286.
InParanoid	O08807.
OrthoDB	EOG4CC424.
PhylomeDB	O08807.
Gene expression databases
ArrayExpress	O08807.
Bgee	O08807.
CleanEx	MM_PRDX4.
Genevestigator	O08807.
GermOnline	ENSMUSG00000025289. Mus musculus.
Family and domain databases
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03386.
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	310209.
SOURCE	Search...

Entry information

Entry name

PRDX4_MOUSE

Accession

Primary (citable) accession number: O08807
Secondary accession number(s): B1AZS7, Q3U8E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program