ID   PRDX4_BOVIN             Reviewed;         274 AA.
AC   Q9BGI2; Q32L06;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Peroxiredoxin-4;
DE            EC=1.11.1.15;
DE   AltName: Full=Prx-IV;
GN   Name=PRDX4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Leyens G., Donnay I., Knoops B.;
RT   "Cloning of 4 new bovine peroxiredoxins, and screening of the complete
RT   peroxiredoxin family in different bovine tissues.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
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 (By similarity).
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; AF305563; AAG53660.1; -; mRNA.
DR   EMBL; BC109824; AAI09825.1; -; mRNA.
DR   IPI; IPI00691994; -.
DR   RefSeq; NP_776858.1; -.
DR   UniGene; Bt.5203; -.
DR   HSSP; Q63716; 1QQ2.
DR   PeroxiBase; 4531; Bt2CysPrx04.
DR   Ensembl; ENSBTAG00000006165; Bos taurus.
DR   GeneID; 281999; -.
DR   KEGG; bta:281999; -.
DR   HOVERGEN; Q9BGI2; -.
DR   OMA; Q9BGI2; AINTEVV.
DR   BRENDA; 1.11.1.15; 251.
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   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN         1    274       Peroxiredoxin-4.
FT                                /FTId=PRO_0000135097.
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;  30741 MW;  AE14176CF1C70E37 CRC64;
     MEAPPPPPPL PATTLAPGRS RKLLLLPLLL FLLRAEAVRG FEAEERPRTR EEECHFYAGG
     QVYPGEVSRV SVAEHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP
     LDFTFVCPTE IIAFGDRIDE FRSINTEVVA CSVDSQFTHL AWINTPRRQG GLGSINIPLL
     ADLNHQISKD YGVYLEDSGH TLRGLFIIDD KGILRQITLN DLPVGRSVDE TLRLVQAFQY
     TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN
//