ID   GPX4_PIG                Reviewed;         197 AA.
AC   P36968;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   25-NOV-2008, entry version 73.
DE   RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, mitochondrial;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   AltName: Full=GPX-4;
DE   Flags: Precursor;
GN   Name=GPX4;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93312346; PubMed=8323565; DOI=10.1006/bbrc.1993.1711;
RA   Sunde R.A., Dyer J.A., Moran T., Evenson J.K., Sugimoto M.;
RT   "Phospholipid hydroperoxide glutathione peroxidase: full-length pig
RT   blastocyst cDNA sequence and regulation by selenium status.";
RL   Biochem. Biophys. Res. Commun. 193:905-911(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   TISSUE=Heart, and Liver;
RX   MEDLINE=94171752; PubMed=8125951;
RA   Brigelius-Flohe R., Aumann K.-D., Bloecker H., Gross G.,
RA   Kloeppel K.-D., Maiorino M., Roveri A., Schuckelt R., Ursini F.,
RA   Wingender E., Flohe L.;
RT   "Phospholipid-hydroperoxide glutathione peroxidase. Genomic DNA, cDNA,
RT   and deduced amino acid sequence.";
RL   J. Biol. Chem. 269:7342-7348(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 40-197, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   MEDLINE=92137773; PubMed=1778506;
RA   Schuckelt R., Brigelius-Flohe R., Maiorino M., Roveri A., Reumkens J.,
RA   Strassburger W., Ursini F., Wolf B., Flohe L.;
RT   "Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme
RT   distinct from the classical glutathione peroxidase as evident from
RT   cDNA and amino acid sequencing.";
RL   Free Radic. Res. Commun. 14:343-361(1991).
CC   -!- FUNCTION: Could play a major role in protecting mammals from the
CC       toxicity of ingested lipid hydroperoxides. Essential for embryonic
CC       development. Protects from radiation and oxidative damage (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide =
CC       glutathione disulfide + lipid + 2 H(2)O.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P36968-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=P36968-2; Sequence=VSP_018744;
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; L12743; AAA31099.2; -; mRNA.
DR   EMBL; L12743; AAA31098.2; -; mRNA.
DR   EMBL; X76009; CAA53596.1; ALT_INIT; mRNA.
DR   EMBL; X76008; CAA53595.1; ALT_INIT; Genomic_DNA.
DR   EMBL; S80257; AAB21327.2; -; mRNA.
DR   PIR; JN0608; JN0608.
DR   RefSeq; NP_999572.1; -.
DR   UniGene; Ssc.11742; -.
DR   HSSP; P00435; 1GP1.
DR   SMR; P36968; 36-197.
DR   PeroxiBase; 3723; SscGPx04.
DR   GeneID; 399537; -.
DR   KEGG; ssc:399537; -.
DR   HOVERGEN; P36968; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione pero...; IEA:EC.
DR   GO; GO:0008430; F:selenium binding; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glut_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Cytoplasm; Developmental protein;
KW   Direct protein sequencing; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Selenium; Selenocysteine; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    197       Phospholipid hydroperoxide glutathione
FT                                peroxidase, mitochondrial.
FT                                /FTId=PRO_0000013071.
FT   ACT_SITE     73     73
FT   NON_STD      73     73       Selenocysteine.
FT   VAR_SEQ       1     27       Missing (in isoform Cytoplasmic).
FT                                /FTId=VSP_018744.
SQ   SEQUENCE   197 AA;  22337 MW;  34865B0BEBFA69D0 CRC64;
     MSFSRLFRLL KPTLLCGTLA VPGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVNLDKYR
     GYVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSDAEIKEFA
     AGYNVKFDMF SKICVNGDDA HPLWKWMKVQ PKGRGMLGNA IKWNFTKFLI DKNGCVVKRY
     GPMEEPQVIE KDLPCYL
//