GPX5_HUMAN
ID GPX5_HUMAN Reviewed; 221 AA.
AC O75715; A1A4Y0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Epididymal secretory glutathione peroxidase;
DE EC=1.11.1.9;
DE AltName: Full=Epididymis-specific glutathione peroxidase-like protein;
DE Short=EGLP;
DE AltName: Full=Glutathione peroxidase 5;
DE Short=GPx-5;
DE Short=GSHPx-5;
DE Flags: Precursor;
GN Name=GPX5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Epididymis;
RX PubMed=9639555; DOI=10.1042/bj3330005;
RA Hall L., Williams K., Perry A.C.F., Frayne J., Jury J.A.;
RT "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are
RT incorrectly spliced: implications for the role of GPX5 in the male
RT reproductive tract.";
RL Biochem. J. 333:5-9(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-85.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-220.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human glutathione peroxidase 5.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC organic hydroperoxide, by glutathione. May constitute a glutathione
CC peroxidase-like protective system against peroxide damage in sperm
CC membrane lipids.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75715-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75715-2; Sequence=VSP_043046;
CC -!- TISSUE SPECIFICITY: Epididymis.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpx5/";
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DR EMBL; AJ005277; CAA06463.1; -; mRNA.
DR EMBL; AY882013; AAW56939.1; -; Genomic_DNA.
DR EMBL; AL049543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03168.1; -; Genomic_DNA.
DR EMBL; BC128159; AAI28160.1; -; mRNA.
DR EMBL; BC128160; AAI28161.1; -; mRNA.
DR CCDS; CCDS4652.1; -. [O75715-1]
DR CCDS; CCDS4653.1; -. [O75715-2]
DR RefSeq; NP_001500.1; NM_001509.2. [O75715-1]
DR RefSeq; NP_003987.2; NM_003996.3. [O75715-2]
DR PDB; 2I3Y; X-ray; 2.00 A; A=28-220.
DR PDBsum; 2I3Y; -.
DR AlphaFoldDB; O75715; -.
DR SMR; O75715; -.
DR IntAct; O75715; 1.
DR STRING; 9606.ENSP00000392398; -.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR PeroxiBase; 3604; HsGPx05-A.
DR PeroxiBase; 3629; HsGPx05-B.
DR iPTMnet; O75715; -.
DR PhosphoSitePlus; O75715; -.
DR BioMuta; GPX5; -.
DR MassIVE; O75715; -.
DR PaxDb; O75715; -.
DR PeptideAtlas; O75715; -.
DR PRIDE; O75715; -.
DR ProteomicsDB; 50172; -. [O75715-1]
DR Antibodypedia; 25906; 100 antibodies from 18 providers.
DR DNASU; 2880; -.
DR Ensembl; ENST00000412168.7; ENSP00000392398.2; ENSG00000224586.7. [O75715-1]
DR Ensembl; ENST00000469384.1; ENSP00000419935.1; ENSG00000224586.7. [O75715-2]
DR GeneID; 2880; -.
DR KEGG; hsa:2880; -.
DR MANE-Select; ENST00000412168.7; ENSP00000392398.2; NM_001509.3; NP_001500.1.
DR UCSC; uc003nlm.3; human. [O75715-1]
DR CTD; 2880; -.
DR DisGeNET; 2880; -.
DR GeneCards; GPX5; -.
DR HGNC; HGNC:4557; GPX5.
DR HPA; ENSG00000224586; Tissue enriched (epididymis).
DR MIM; 603435; gene.
DR neXtProt; NX_O75715; -.
DR OpenTargets; ENSG00000224586; -.
DR PharmGKB; PA28953; -.
DR VEuPathDB; HostDB:ENSG00000224586; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000164550; -.
DR HOGENOM; CLU_029507_2_1_1; -.
DR InParanoid; O75715; -.
DR OMA; HELMNGI; -.
DR PhylomeDB; O75715; -.
DR TreeFam; TF105318; -.
DR BRENDA; 1.11.1.9; 2681.
DR PathwayCommons; O75715; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 2880; 30 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; O75715; -.
DR GeneWiki; GPX5; -.
DR GenomeRNAi; 2880; -.
DR Pharos; O75715; Tbio.
DR PRO; PR:O75715; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75715; protein.
DR Bgee; ENSG00000224586; Expressed in right testis and 16 other tissues.
DR ExpressionAtlas; O75715; baseline and differential.
DR Genevisible; O75715; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
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 3D-structure; Alternative splicing; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..221
FT /note="Epididymal secretory glutathione peroxidase"
FT /id="PRO_0000013076"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT VAR_SEQ 81..221
FT /note="ELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLKYVRPGGGFVPSF
FT QLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIRWNFEKFLVGPD
FT GIPVMRWSHRATVSSVKTDILAYLKQFKTK -> GMSVQGEDLYLVSSFLRKGM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043046"
FT VARIANT 85
FT /note="L -> P (in dbSNP:rs58554303)"
FT /id="VAR_061206"
FT VARIANT 85
FT /note="L -> V (in dbSNP:rs769188)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_012040"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:2I3Y"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2I3Y"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:2I3Y"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2I3Y"
SQ SEQUENCE 221 AA; 25202 MW; CE3E7BFD53CE979F CRC64;
MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK NEYVSFKQYV
GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP CNQFGKQEPG DNKEILPGLK
YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS FLKHSCPHPS EILGTFKSIS WDPVKVHDIR
WNFEKFLVGP DGIPVMRWSH RATVSSVKTD ILAYLKQFKT K
