ID   GPX1_CHLRE              Reviewed;         201 AA.
AC   P83564; A8IAD7;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glutathione peroxidase 1, mitochondrial {ECO:0000303|PubMed:11973339};
DE            Short=CrGPx1 {ECO:0000303|PubMed:11973339};
DE            EC=1.11.1.9;
DE   Flags: Precursor;
GN   Name=GPX {ECO:0000312|EMBL:AAL14348.1};
GN   Synonyms=PHGPX1 {ECO:0000303|PubMed:12110581}; ORFNames=CHLREDRAFT_206090;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP   SELENOCYSTEINE AT SEC-75, AND MASS SPECTROMETRY.
RC   STRAIN=2137;
RX   PubMed=11973339; DOI=10.1074/jbc.m202912200;
RA   Fu L.-H., Wang X.-F., Eyal Y., She Y.-M., Donald L.J., Standing K.G.,
RA   Ben-Hayyim G.;
RT   "A selenoprotein in the plant kingdom. Mass spectrometry confirms that an
RT   opal codon (UGA) encodes selenocysteine in Chlamydomonas reinhardtii
RT   glutathione peroxidase.";
RL   J. Biol. Chem. 277:25983-25991(2002).
RN   [2] {ECO:0000312|EMBL:EDP06633.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SELENOCYSTEINE AT SEC-75.
RX   PubMed=12110581; DOI=10.1093/emboj/cdf372;
RA   Novoselov S.V., Rao M., Onoshko N.V., Zhi H., Kryukov G.V., Xiang Y.,
RA   Weeks D.P., Hatfield D.L., Gladyshev V.N.;
RT   "Selenoproteins and selenocysteine insertion system in the model plant cell
RT   system, Chlamydomonas reinhardtii.";
RL   EMBO J. 21:3681-3693(2002).
CC   -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC       system against oxidative stresses. Hydrogen peroxide, tert-butyl
CC       hydroperoxide and cumene, but not phosphatidylcholine hydroperoxide,
CC       can act as acceptors. {ECO:0000269|PubMed:11973339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000269|PubMed:11973339};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- INDUCTION: By selenium, particularly under autotrophic conditions.
CC       {ECO:0000269|PubMed:11973339}.
CC   -!- MASS SPECTROMETRY: Mass=18496; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11973339};
CC   -!- MASS SPECTROMETRY: Mass=18571; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11973339};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AY051144; AAL14348.1; -; mRNA.
DR   EMBL; DS496114; EDP06633.1; -; Genomic_DNA.
DR   RefSeq; XP_001701658.1; XM_001701606.1.
DR   STRING; 3055.EDP06633; -.
DR   PeroxiBase; 2590; CreGPx02.
DR   PaxDb; P83564; -.
DR   EnsemblPlants; PNW86237; PNW86237; CHLRE_02g078300v5.
DR   GeneID; 5727250; -.
DR   Gramene; PNW86237; PNW86237; CHLRE_02g078300v5.
DR   KEGG; cre:CHLRE_02g078300v5; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; P83564; -.
DR   OrthoDB; 1483113at2759; -.
DR   GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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   1: Evidence at protein level;
KW   Mitochondrion; Oxidoreductase; Peroxidase; Selenium; Selenocysteine;
KW   Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT   CHAIN           28..201
FT                   /note="Glutathione peroxidase 1, mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000013089"
FT   NON_STD         75
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000269|PubMed:11973339,
FT                   ECO:0000269|PubMed:12110581"
SQ   SEQUENCE   201 AA;  21499 MW;  1030F45EBA62C219 CRC64;
     MLLTRKNVAV RPARAARRDV RAMSLLGNLF GGGSKPTSST SNFHQLSALD IDKKNVDFKS
     LNNRVVLVVN VASKUGLTAA NYKEFATLLG KYPATDLTIV AFPCNQFGGQ EPGTNAEIKA
     FASARGFSGA GALLMDKVDV NGANASPVYN FLKVAAGDTS DIGWNFGKFL VRPDGTVFGR
     YAPTTGPLSL EKYIVELINS R