ID   GPX4_HYLLA              Reviewed;         197 AA.
AC   Q4AEH1;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, mitochondrial;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   AltName: Full=Glutathione peroxidase 4;
DE            Short=GPx-4;
DE   Flags: Precursor;
GN   Name=GPX4;
OS   Hylobates lar (Common gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; Hylobates.
OX   NCBI_TaxID=9580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA   Fukuhara R., Kageyama T.;
RT   "Structure, gene expression, and evolution of primate glutathione
RT   peroxidases.";
RL   Comp. Biochem. Physiol. 141B:428-436(2005).
CC   -!- FUNCTION: Protects cells against membrane lipid peroxidation and
CC       cell death. Required for normal sperm development and male
CC       fertility. 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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=Q4AEH1-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=Q4AEH1-2; Sequence=VSP_018741;
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AB121011; BAE17019.1; -; mRNA.
DR   SMR; Q4AEH1; 36-197.
DR   PeroxiBase; 3699; HlGPx04.
DR   HOVERGEN; Q4AEH1; -.
DR   BRENDA; 1.11.1.12; 285274.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; Glutathione_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   2: Evidence at transcript level;
KW   Alternative initiation; Cytoplasm; Developmental protein;
KW   Mitochondrion; Oxidoreductase; Peroxidase; Selenium; Selenocysteine;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    197       Phospholipid hydroperoxide glutathione
FT                                peroxidase, mitochondrial.
FT                                /FTId=PRO_0000042609.
FT   ACT_SITE     73     73       By similarity.
FT   NON_STD      73     73       Selenocysteine.
FT   VAR_SEQ       1     27       Missing (in isoform Cytoplasmic).
FT                                /FTId=VSP_018741.
SQ   SEQUENCE   197 AA;  22101 MW;  6CBB9A94841AE444 CRC64;
     MSLGRLCRLL MPALLCGALA APGLAGTMCA SRDDWRCAGS MHEFSAKVLD GHTVNLDKYR
     GFVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGLRFLAF PCNQFGKQEP GSNEEIKEFA
     AGYNVKFDMF SKICVNGDDA HPLWKWMKIQ PKGKGILGNA IKWNFTKFLF DKNGCVVKRY
     GPMEEPLVLE KDLPHYF
//