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Database: UniProt
Entry: G1M1M8_AILME
LinkDB: G1M1M8_AILME
Original site: G1M1M8_AILME 
ID   G1M1M8_AILME            Unreviewed;       207 AA.
AC   G1M1M8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   Name=GPX1 {ECO:0000313|Ensembl:ENSAMEP00000013239.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000013239.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000013239.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000013239.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC         glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90680; Evidence={ECO:0000256|ARBA:ARBA00036482};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC         Evidence={ECO:0000256|ARBA:ARBA00036482};
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:0000256|ARBA:ARBA00036108};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC         Evidence={ECO:0000256|ARBA:ARBA00036108};
CC   -!- SUBUNIT: Homotetramer. Interacts with MIEN1.
CC       {ECO:0000256|ARBA:ARBA00038541}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   AlphaFoldDB; G1M1M8; -.
DR   STRING; 9646.ENSAMEP00000013239; -.
DR   Ensembl; ENSAMET00000013796.2; ENSAMEP00000013239.2; ENSAMEG00000012590.2.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000156150; -.
DR   HOGENOM; CLU_029507_2_0_1; -.
DR   InParanoid; G1M1M8; -.
DR   TreeFam; TF105318; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0097413; C:Lewy body; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR   GO; GO:0001885; P:endothelial cell development; IEA:Ensembl.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0019372; P:lipoxygenase pathway; IEA:Ensembl.
DR   GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
DR   GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR   GO; GO:0009609; P:response to symbiotic bacterium; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR   GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR   GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF41; GLUTATHIONE PEROXIDASE 1; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..207
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5031056867"
SQ   SEQUENCE   207 AA;  22459 MW;  53ED44DC79ED2B24 CRC64;
     MCAAPLAAAA AAALAAAPRS VYAFSARPLT GGEPLSLGSL RGKVLLIENV ASLGTTVRDY
     TQMNELQRRL GPRGLVVLGF PCNQFGHQEN AKNEEILNSL KYVRPGGGFE PNFTLFEKCE
     VNGAQAHPLF AFLREALPVP SDDATALMTD PKFIIWSPVC RNDVAWNFEK FLVGPDGVPV
     RRYSRRFPTI DIEPDIEALL SQAPSCA
//
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