ID   PRDX6_BOVIN             Reviewed;         224 AA.
AC   O77834; Q5E9F3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Peroxiredoxin-6;
DE            EC=1.11.1.15;
DE   AltName: Full=Antioxidant protein 2;
DE   AltName: Full=1-Cys peroxiredoxin;
DE            Short=1-Cys PRX;
DE   AltName: Full=Acidic calcium-independent phospholipase A2;
DE            Short=aiPLA2;
DE            EC=3.1.1.-;
DE   AltName: Full=Non-selenium glutathione peroxidase;
DE            Short=NSGPx;
DE            EC=1.11.1.7;
DE   AltName: Full=PHGPx;
DE   AltName: Full=Ciliary body glutathione peroxidase;
GN   Name=PRDX6; Synonyms=AOP2, GPX, PHGPX;
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=Ocular ciliary body;
RX   MEDLINE=98421546; PubMed=9748299; DOI=10.1074/jbc.273.40.26171;
RA   Singh A.K., Shichi H.;
RT   "A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA
RT   level, and translation.";
RL   J. Biol. Chem. 273:26171-26178(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   MEDLINE=99340074; PubMed=10409692; DOI=10.1074/jbc.274.30.21326;
RA   Fisher A.B., Dodia C., Manevich Y., Chen J.-W., Feinstein S.I.;
RT   "Phospholipid hydroperoxides are substrates for non-selenium
RT   glutathione peroxidase.";
RL   J. Biol. Chem. 274:21326-21334(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oviduct;
RA   Rojas Garcia P.P., Einspanier R.;
RT   "Glutathione peroxidase in the bovine oviduct.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 2-30.
RX   MEDLINE=90323120; PubMed=2373154; DOI=10.1016/0014-4835(90)90040-2;
RA   Shichi H., Demar J.C.;
RT   "Non-selenium glutathione peroxidase without glutathione S-transferase
RT   activity from bovine ciliary body.";
RL   Exp. Eye Res. 50:513-520(1990).
CC   -!- FUNCTION: Involved in redox regulation of the cell. Can reduce
CC       H(2)O(2) and short chain organic, fatty acid, and phospholipid
CC       hydroperoxides. May play a role in the regulation of phospholipid
CC       turnover as well as in protection against oxidative injury.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer. May interact with HTR2A. Interacts with STH
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By
CC       similarity). Cytoplasmic vesicle (By similarity). Note=And also
CC       found in lung secretory organelles (By similarity).
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized
CC       to Cys-SOH. Cys-SOH may rapidly react with a Cys-SH of the other
CC       subunit to form an intermolecular disulfide with a concomitant
CC       homodimer formation. The enzyme may be subsequently regenerated by
CC       reduction of the disulfide by thioredoxin (By similarity).
CC   -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-47
CC       (to Cys-SO(3)H) upon oxidative stress (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family. Rehydrin subfamily.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AF080228; AAC63016.1; -; mRNA.
DR   EMBL; AF090194; AAC84043.1; -; mRNA.
DR   EMBL; AJ243848; CAB64802.1; -; mRNA.
DR   EMBL; BT020967; AAX08984.1; -; mRNA.
DR   EMBL; BC102172; AAI02173.1; -; mRNA.
DR   IPI; IPI00689857; -.
DR   RefSeq; NP_777068.1; -.
DR   UniGene; Bt.49705; -.
DR   HSSP; P30041; 1PRX.
DR   SMR; O77834; 5-224.
DR   PeroxiBase; 4423; Bt1CysPrx.
DR   Ensembl; ENSBTAG00000004855; Bos taurus.
DR   GeneID; 282438; -.
DR   KEGG; bta:282438; -.
DR   HOVERGEN; O77834; -.
DR   OMA; O77834; TARVVFI.
DR   BRENDA; 1.11.1.15; 251.
DR   BRENDA; 1.11.1.7; 251.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:AgBase.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:AgBase.
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; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lysosome; Multifunctional enzyme; Oxidoreductase;
KW   Peroxidase; Phosphoprotein; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    224       Peroxiredoxin-6.
FT                                /FTId=PRO_0000135101.
FT   DOMAIN        5    169       Thioredoxin.
FT   ACT_SITE     32     32       For phospholipase activity (By
FT                                similarity).
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   MOD_RES      44     44       Phosphothreonine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine (By similarity).
FT   DISULFID     47     47       Interchain; in linked form (By
FT                                similarity).
SQ   SEQUENCE   224 AA;  25067 MW;  4013D59C4D9FC05E CRC64;
     MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
     FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF PIIDDKNRDL AIQLGMLDPA
     EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVIISLQLT AEKRVATPVD
     WKNGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP
//