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 13-FEB-2019, entry version 156. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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) RT transcripts are incorrectly spliced: implications for the role of GPX5 RT in the male 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 CC glutathione peroxidase-like protective system against peroxide CC damage in sperm 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 Note=No experimental confirmation available.; 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/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.248129; -. DR PDB; 2I3Y; X-ray; 2.00 A; A=28-220. DR PDBsum; 2I3Y; -. DR ProteinModelPortal; O75715; -. DR SMR; O75715; -. DR STRING; 9606.ENSP00000392398; -. DR DrugBank; DB00143; Glutathione. DR PeroxiBase; 3604; HsGPx05-A. DR PeroxiBase; 3629; HsGPx05-B. DR iPTMnet; O75715; -. DR PhosphoSitePlus; O75715; -. DR BioMuta; GPX5; -. DR PaxDb; O75715; -. DR PeptideAtlas; O75715; -. DR PRIDE; O75715; -. DR ProteomicsDB; 50172; -. DR ProteomicsDB; 50173; -. [O75715-2] DR DNASU; 2880; -. DR Ensembl; ENST00000412168; ENSP00000392398; ENSG00000224586. [O75715-1] DR Ensembl; ENST00000469384; ENSP00000419935; ENSG00000224586. [O75715-2] DR Ensembl; ENST00000550775; ENSP00000450365; ENSG00000257770. [O75715-1] DR Ensembl; ENST00000551639; ENSP00000449271; ENSG00000257770. [O75715-2] DR GeneID; 2880; -. DR KEGG; hsa:2880; -. DR UCSC; uc003nlm.3; human. [O75715-1] DR CTD; 2880; -. DR DisGeNET; 2880; -. DR EuPathDB; HostDB:ENSG00000224586.6; -. DR GeneCards; GPX5; -. DR HGNC; HGNC:4557; GPX5. DR MIM; 603435; gene. DR neXtProt; NX_O75715; -. DR OpenTargets; ENSG00000224586; -. DR PharmGKB; PA28953; -. DR eggNOG; KOG1651; Eukaryota. DR eggNOG; COG0386; LUCA. DR GeneTree; ENSGT00940000164550; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG101716; -. DR InParanoid; O75715; -. DR KO; K00432; -. DR OMA; KHISWEP; -. DR OrthoDB; 1102119at2759; -. DR PhylomeDB; O75715; -. DR TreeFam; TF105318; -. DR BRENDA; 1.11.1.9; 2681. DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species. DR EvolutionaryTrace; O75715; -. DR GeneWiki; GPX5; -. DR GenomeRNAi; 2880; -. DR PRO; PR:O75715; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000224586; Expressed in 20 organ(s), highest expression level in caput epididymis. 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; Complete proteome; Oxidoreductase; KW Peroxidase; Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 221 Epididymal secretory glutathione FT peroxidase. FT /FTId=PRO_0000013076. FT ACT_SITE 73 73 {ECO:0000250}. FT VAR_SEQ 81 221 ELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLKY FT VRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEI FT LGTFKSISWDPVKVHDIRWNFEKFLVGPDGIPVMRWSHRAT FT VSSVKTDILAYLKQFKTK -> GMSVQGEDLYLVSSFLRKG FT M (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_043046. FT VARIANT 85 85 L -> P (in dbSNP:rs58554303). FT /FTId=VAR_061206. FT VARIANT 85 85 L -> V (in dbSNP:rs769188). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_012040. FT HELIX 40 42 {ECO:0000244|PDB:2I3Y}. FT STRAND 44 51 {ECO:0000244|PDB:2I3Y}. FT STRAND 53 55 {ECO:0000244|PDB:2I3Y}. FT HELIX 56 59 {ECO:0000244|PDB:2I3Y}. FT STRAND 62 69 {ECO:0000244|PDB:2I3Y}. FT STRAND 71 73 {ECO:0000244|PDB:2I3Y}. FT HELIX 74 78 {ECO:0000244|PDB:2I3Y}. FT HELIX 79 89 {ECO:0000244|PDB:2I3Y}. FT HELIX 90 92 {ECO:0000244|PDB:2I3Y}. FT STRAND 94 100 {ECO:0000244|PDB:2I3Y}. FT HELIX 112 114 {ECO:0000244|PDB:2I3Y}. FT HELIX 115 121 {ECO:0000244|PDB:2I3Y}. FT STRAND 131 135 {ECO:0000244|PDB:2I3Y}. FT STRAND 140 142 {ECO:0000244|PDB:2I3Y}. FT HELIX 147 155 {ECO:0000244|PDB:2I3Y}. FT TURN 166 168 {ECO:0000244|PDB:2I3Y}. FT STRAND 171 173 {ECO:0000244|PDB:2I3Y}. FT STRAND 185 188 {ECO:0000244|PDB:2I3Y}. FT STRAND 194 198 {ECO:0000244|PDB:2I3Y}. FT HELIX 204 214 {ECO:0000244|PDB:2I3Y}. FT HELIX 215 217 {ECO:0000244|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 //