ID   GPX5_HUMAN              Reviewed;         221 AA.
AC   O75715;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   07-JUL-2009, entry version 76.
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   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].
RC   TISSUE=Epididymis;
RX   MEDLINE=98306046; PubMed=9639555;
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   MEDLINE=22935763; 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   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       glutathionine peroxidase-like protective system against peroxide
CC       damage in sperm membrane lipids.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Epididymis.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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; CAB71121.1; -; Genomic_DNA.
DR   IPI; IPI00026802; -.
DR   RefSeq; NP_001500.1; -.
DR   UniGene; Hs.248129; -.
DR   PDB; 2I3Y; X-ray; 2.00 A; A=28-220.
DR   PDBsum; 2I3Y; -.
DR   PeroxiBase; 3604; HsGPx05-a.
DR   PeroxiBase; 3629; HsGPx05-b.
DR   PRIDE; O75715; -.
DR   Ensembl; ENSG00000079782; Homo sapiens.
DR   GeneID; 2880; -.
DR   KEGG; hsa:2880; -.
DR   UCSC; uc003nll.1; human.
DR   GeneCards; GC06P028604; -.
DR   H-InvDB; HIX0005673; -.
DR   HGNC; HGNC:4557; GPX5.
DR   MIM; 603435; gene.
DR   PharmGKB; PA28953; -.
DR   HOGENOM; O75715; -.
DR   HOVERGEN; O75715; -.
DR   OMA; O75715; TIYDYEA.
DR   BRENDA; 1.11.1.9; 247.
DR   DrugBank; DB00143; Glutathione.
DR   NextBio; 11375; -.
DR   ArrayExpress; O75715; -.
DR   CleanEx; HS_GPX5; -.
DR   GermOnline; ENSG00000079782; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EC.
DR   GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
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; Complete proteome; Oxidoreductase; Peroxidase;
KW   Polymorphism; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    221       Epididymal secretory glutathione
FT                                peroxidase.
FT                                /FTId=PRO_0000013076.
FT   ACT_SITE     73     73       By similarity.
FT   VARIANT      85     85       L -> V (in dbSNP:rs769188).
FT                                /FTId=VAR_012040.
FT   HELIX        40     42
FT   STRAND       44     51
FT   STRAND       53     55
FT   HELIX        56     59
FT   STRAND       62     69
FT   STRAND       71     73
FT   HELIX        74     78
FT   HELIX        79     89
FT   HELIX        90     92
FT   STRAND       94    100
FT   HELIX       112    114
FT   HELIX       115    121
FT   STRAND      131    135
FT   STRAND      140    142
FT   HELIX       147    155
FT   STRAND      161    164
FT   TURN        166    168
FT   STRAND      171    175
FT   STRAND      185    188
FT   STRAND      194    198
FT   HELIX       204    214
FT   HELIX       215    217
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
//