ID   PRDX4_MOUSE             Reviewed;         274 AA.
AC   O08807; Q3U8E4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 89.
DE   RecName: Full=Peroxiredoxin-4;
DE            EC=1.11.1.15;
DE   AltName: Full=Prx-IV;
DE   AltName: Full=Thioredoxin peroxidase AO372;
DE   AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
DE   AltName: Full=Antioxidant enzyme AOE372;
GN   Name=Prdx4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21121079; PubMed=11229364; DOI=10.1089/15230860050192288;
RA   Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F.,
RA   Jeang K.-T., Jin D.-Y.;
RT   "Characterization of human and mouse peroxiredoxin IV: evidence for
RT   inhibition by Prx-IV of epidermal growth factor- and p53-induced
RT   reactive oxygen species.";
RL   Antioxid. Redox Signal. 2:507-518(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NMRI; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 190-203 AND 216-226.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Probably involved in redox regulation of the cell.
CC       Regulates the activation of NF-kappa-B in the cytosol by a
CC       modulation of I-kappa-B-alpha phosphorylation.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked,
CC       upon oxidation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-127
CC       oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-SH of the
CC       other subunit to form an intermolecular disulfide with a
CC       concomitant homodimer formation. The enzyme may be subsequently
CC       regenerated by reduction of the disulfide by thioredoxin (By
CC       similarity).
CC   -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-
CC       127 (to Cys-SO(3)H) upon oxidative stress (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; U96746; AAB57846.1; -; mRNA.
DR   EMBL; AK005031; BAB23758.1; -; mRNA.
DR   EMBL; AK146402; BAE27143.1; -; mRNA.
DR   EMBL; AK152255; BAE31074.1; -; mRNA.
DR   EMBL; BC003349; AAH03349.1; -; mRNA.
DR   EMBL; BC019578; AAH19578.1; -; mRNA.
DR   IPI; IPI00116254; -.
DR   RefSeq; NP_058044.1; -.
DR   UniGene; Mm.247542; -.
DR   HSSP; Q63716; 1QQ2.
DR   PeroxiBase; 4532; Mm2CysPrx04.
DR   PMMA-2DPAGE; O08807; -.
DR   REPRODUCTION-2DPAGE; O08807; -.
DR   PRIDE; O08807; -.
DR   Ensembl; ENSMUSG00000025289; Mus musculus.
DR   GeneID; 53381; -.
DR   KEGG; mmu:53381; -.
DR   NMPDR; fig|10090.3.peg.22366; -.
DR   MGI; MGI:1859815; Prdx4.
DR   HOGENOM; O08807; -.
DR   HOVERGEN; O08807; -.
DR   OMA; O08807; YLEEAGH.
DR   BRENDA; 1.11.1.15; 244.
DR   NextBio; 310209; -.
DR   ArrayExpress; O08807; -.
DR   Bgee; O08807; -.
DR   CleanEx; MM_PRDX4; -.
DR   GermOnline; ENSMUSG00000025289; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; Alkyl_hydroperoxide_Rdtase.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN         1    274       Peroxiredoxin-4.
FT                                /FTId=PRO_0000135099.
FT   DOMAIN       82    240       Thioredoxin.
FT   ACT_SITE    127    127       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID    127    127       Interchain (with C-248); in linked form
FT                                (By similarity).
FT   DISULFID    248    248       Interchain (with C-127); in linked form
FT                                (By similarity).
SQ   SEQUENCE   274 AA;  31053 MW;  73DB5374EC46241C CRC64;
     MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG
     QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP
     LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL
     SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY
     TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN
//