ID GPX4_MACFU Reviewed; 197 AA. AC Q4AEH0; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-JUN-2009, entry version 29. 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 Macaca fuscata fuscata (Japanese macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9543; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. 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=Q4AEH0-1; Sequence=Displayed; CC Name=Cytoplasmic; CC IsoId=Q4AEH0-2; Sequence=VSP_018742; CC -!- TISSUE SPECIFICITY: Expressed very intensively in the testis and CC weakly in lung, heart, and cerebellum. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB121012; BAE17020.1; -; mRNA. DR SMR; Q4AEH0; 36-197. DR PeroxiBase; 3708; MfGPx04. DR HOVERGEN; Q4AEH0; -. DR BRENDA; 1.11.1.12; 276174. 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 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_0000042611. 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_018742. SQ SEQUENCE 197 AA; 22187 MW; D2C65F9DADAC0098 CRC64; MNLGRLCRLL KPALLCGALA APGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVNLDKYR GFVCIVTNVA SQUGKTEVNY TQLVDLHARY AECGVRILAF PCNQFGKQEP GSNEKIKEFA AGYNVKFDMF SKICVNGDDA HPLWKWMKIQ PKGKGILGNA IKWNFTKFLI DKNGCVVKRY GPMEEPLVIE KDLPHYF //