ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O75715


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GPX5_HUMAN
Primary accession number O75715
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 66)
Name and origin of the protein
Protein name Epididymal secretory glutathione peroxidase [Precursor]
Synonyms EC 1.11.1.9
Epididymis-specific glutathione peroxidase-like protein
EGLP
Gene name
Name: GPX5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epididymis;
PubMed=9639555 [NCBI, ExPASy, EBI, Israel, Japan]
Hall L., Williams K., Perry A.C.F., Frayne J., Jury J.A.;
"The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract.";
Biochem. J. 333:5-9(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-85.
Livingston R.J., Rieder M.J., Chung M.-W., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ005277; CAA06463.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY882013; AAW56939.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049543; CAB71121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001500.1; -.
NP_003987.2; -.
UniGene Hs.248129
3D structure databases
PDB
2I3Y; X-ray; 2.00 A; A=26-220.[ExPASy / RCSB / EBI]
PDBsum 2I3Y; -.
ModBase O75715.
Protein family/group databases
PeroxiBase 3604; HsGPx05-a.
3629; HsGPx05-b.
Polymorphism databases
NIEHS-SNPs GPX5.
Organism-specific databases
H-InvDB HIX0005673; -.
HGNC HGNC:4557; GPX5.
GenAtlas GPX5.
MIM 603435; gene. [NCBI / EBI]
PharmGKB PA28953; -.
GeneCards O75715.
Gene expression databases
ArrayExpress O75715; -.
CleanEx HS_GPX5; -.
GermOnline ENSG00000079782; Homo sapiens.
Ontologies
GO
GO:0006629; Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O75715.
Genome annotation databases
Ensembl ENSG00000079782; Homo sapiens. [Contig view]
GeneID 2880; -.
KEGG hsa:2880; -.
Phylogenomic databases
HOGENOM O75715; -.
HOVERGEN O75715; -.
Other
DrugBank DB00143; Glutathione.
LinkHub O75715; -.
SOURCE GPX5; Homo sapiens.
ProtoNet O75715.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Oxidoreductase; Peroxidase; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
CHAIN   22   221  200     Epididymal secretory glutathione peroxidase. PRO_0000013076
ACT_SITE   73    73        By similarity. 
VARIANT   85    85  1     L -> V (in dbSNP:rs769188 [NCBI]). VAR_012040 
HELIX   40    42  3      
STRAND   44    51  8      
STRAND   53    55  3      
HELIX   56    59  4      
STRAND   62    69  8      
STRAND   71    73  3      
HELIX   74    78  5      
HELIX   79    89  11      
HELIX   90    92  3      
STRAND   94   100  7      
HELIX   112   114  3      
HELIX   115   121  7      
STRAND   131   135  5      
STRAND   140   142  3      
HELIX   147   155  9      
STRAND   161   164  4      
TURN   166   168  3      
STRAND   171   175  5      
STRAND   185   188  4      
STRAND   194   198  5      
HELIX   204   214  11      
HELIX   215   217  3      
Sequence information
Length: 221 AA [This is the length of the unprocessed precursor] Molecular weight: 25202 Da [This is the MW of the unprocessed precursor] CRC64: CE3E7BFD53CE979F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK NEYVSFKQYV 

        70         80         90        100        110        120 
GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP CNQFGKQEPG DNKEILPGLK 

       130        140        150        160        170        180 
YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS FLKHSCPHPS EILGTFKSIS WDPVKVHDIR 

       190        200        210        220 
WNFEKFLVGP DGIPVMRWSH RATVSSVKTD ILAYLKQFKT K 

O75715 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!