ID A0A0D9R6S2_CHLSB Unreviewed; 221 AA.
AC A0A0D9R6S2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=GPX5 {ECO:0000313|Ensembl:ENSCSAP00000004311.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000004311.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000004311.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000004311.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00000217};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; AQIB01159635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007971533.1; XM_007973342.1.
DR AlphaFoldDB; A0A0D9R6S2; -.
DR STRING; 60711.ENSCSAP00000004311; -.
DR Ensembl; ENSCSAT00000006100.1; ENSCSAP00000004311.1; ENSCSAG00000008050.1.
DR GeneID; 103221912; -.
DR KEGG; csab:103221912; -.
DR CTD; 2880; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000164550; -.
DR OMA; HELMNGI; -.
DR OrthoDB; 67394at2759; -.
DR BioGRID-ORCS; 103221912; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 17.
DR Bgee; ENSCSAG00000008050; Expressed in blood.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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:SF127; EPIDIDYMAL SECRETORY GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000029965};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..221
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002344479"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 221 AA; 25238 MW; A727738095936DF0 CRC64;
MTRQLRVVHL LPLLLACFVQ TSPKQETMKM DCHKDEKGTI YDYEAIALNK NEYVPFKQYV
GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP CNQFGKQEPG DNKEILPGLK
YVRPGGGFVP NFQLFEKGDV NGEKEQKVFS FLKHSCPHPS EILGTFKSIS WNPVKVHDIR
WNFEKFLVGP DGIPVMRWSH QATVSSVKTD ILAYLKQFKT K
//
