ID   PRDX5_PAPHA             Reviewed;         215 AA.
AC   Q9GLW9;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2008, entry version 49.
DE   RecName: Full=Peroxiredoxin-5, mitochondrial;
DE            EC=1.11.1.15;
DE   AltName: Full=Prx-V;
DE   AltName: Full=Thioredoxin reductase;
DE   Flags: Precursor;
GN   Name=PRDX5;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Knoops B., Cherif H.;
RT   "Cloning and characterization of baboon AOEB166/PRDX5.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with
CC       reducing equivalents provided through the thioredoxin system.
CC       Involved in intracellular redox signaling (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By
CC       similarity). Peroxisome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=Q9GLW9-1; Sequence=Displayed;
CC       Name=Cytoplasmic+peroxisomal;
CC         IsoId=Q9GLW9-2; Sequence=VSP_018831;
CC   -!- SIMILARITY: Belongs to the peroxiredoxin 2 family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AF110734; AAG13451.2; -; mRNA.
DR   HSSP; P30044; 1HD2.
DR   SMR; Q9GLW9; 55-215.
DR   HOVERGEN; Q9GLW9; -.
DR   LinkHub; Q9GLW9; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative initiation; Antioxidant; Cytoplasm; Mitochondrion;
KW   Oxidoreductase; Peroxidase; Peroxisome; Redox-active center;
KW   Transit peptide.
FT   TRANSIT       1     53       Mitochondrion (Potential).
FT   CHAIN        54    215       Peroxiredoxin-5, mitochondrial.
FT                                /FTId=PRO_0000023797.
FT   DOMAIN       57    215       Thioredoxin.
FT   MOTIF       213    215       Microbody targeting signal (By
FT                                similarity).
FT   ACT_SITE    101    101       Cysteine sulfenic acid (-SOH)
FT                                intermediate (Potential).
FT   DISULFID    101    205       Redox-active (By similarity).
FT   VAR_SEQ       1     53       Missing (in isoform
FT                                Cytoplasmic+peroxisomal).
FT                                /FTId=VSP_018831.
SQ   SEQUENCE   215 AA;  22166 MW;  65183A24535C1617 CRC64;
     MGLAGVCVLR RSAGYILGGA AGQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG
     DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG
     VQVLACLSVN DAFVTGEWGR AHKVEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK
     RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL
//