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Database: UniProt
Entry: Q4AEI2
LinkDB: Q4AEI2
Original site: Q4AEI2 
ID   GPX1_HYLLA              Reviewed;         201 AA.
AC   Q4AEI2;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   01-OCT-2014, entry version 49.
DE   RecName: Full=Glutathione peroxidase 1;
DE            Short=GPx-1;
DE            Short=GSHPx-1;
DE            EC=1.11.1.9;
DE   AltName: Full=Cellular glutathione peroxidase;
GN   Name=GPX1;
OS   Hylobates lar (Common gibbon) (White-handed 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 the hemoglobin in erythrocytes from oxidative
CC       breakdown. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer. Interacts with MIEN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: During periods of oxidative stress, Sec-47 may react with a
CC       superoxide radical, irreversibly lose hydroselenide and be
CC       converted to dehydroalanine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB120998; BAE17008.1; -; mRNA.
DR   ProteinModelPortal; Q4AEI2; -.
DR   PeroxiBase; 3696; HlGPx01.
DR   HOVERGEN; HBG004333; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 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   Acetylation; Cytoplasm; Oxidoreductase; Peroxidase; Selenocysteine.
FT   CHAIN         1    201       Glutathione peroxidase 1.
FT                                /FTId=PRO_0000066611.
FT   ACT_SITE     47     47       {ECO:0000250}.
FT   SITE         47     47       Subject to oxidation and hydroselenide
FT                                loss to dehydroalanine. {ECO:0000250}.
FT   NON_STD      47     47       Selenocysteine.
FT   MOD_RES      86     86       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      86     86       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     112    112       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     112    112       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     146    146       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     146    146       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
SQ   SEQUENCE   201 AA;  21990 MW;  2ACA430A3E45AEBF CRC64;
     MCAARLAAAA AQSVYAFSAR PLTGGEPVSL GSLRGKILLI ENVASLUGTT VRDYTQMNEL
     QRRLGPRGLV VLGFPCNQFG HQENAKNEEI LNSLKYVRPG GGFEPNFMLF EKCEVNGAGA
     HPLFAFLREA LPAPSDDATA LMTDPKLITW SPVCRNDVAW NFEKFLVGPD GVPLRRYSRR
     FQTIDIEPDI EALLSQGPSC A
//
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