|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-46.
TISSUE=Epididymis;
DOI=10.1016/S0304-4165(97)00016-0; PubMed=9271255 [NCBI, ExPASy, EBI, Israel, Japan]
Okamura N.,
Iwaki Y.,
Hiramoto S.,
Tamba M.,
Bannai S.,
Sugita Y.,
Syntin P.,
Dacheux F.,
Dacheux J.-L.;
"Molecular cloning and characterization of the epididymis-specific glutathione peroxidase-like protein secreted in the porcine epididymal fluid.";
Biochim. Biophys. Acta 1336:99-109(1997).
|
|
|
|
- FUNCTION: May constitute a glutathionine peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction.
- CATALYTIC ACTIVITY: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
- SUBUNIT: Homotetramer.
- SUBCELLULAR LOCATION: Secreted.
- TISSUE SPECIFICITY: Proximal caput epididymis.
- SIMILARITY: Belongs to the glutathione peroxidase family.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 219 AA [This is the length of the unprocessed precursor] |
Molecular weight: 24936 Da [This is the MW of the unprocessed precursor] |
CRC64: A22850A6477A262D [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MTVQLGAFYL FPLFMAGFVQ TNSNLEKMDC YKDVTGTIYD YDAFTLNGNE HIQFKQYAGK
70 80 90 100 110 120
HVLFVNVATY CGLTAQYPEL NTLQEELKPF GLVVLGFPCN QFGKQEPGEN SEILLGLKYV
130 140 150 160 170 180
RPGGGYVPNF QLFEKGDVNG EKEQKVFTFL KHSCPHPSEL IGSIGYISWE PIRVHDIRWN
190 200 210
FEKFLVGPDG VPVMRWVHET PISTVKSDIL AYLKQFKTE
|
O18994 in FASTA format |
|
ExPASy Home page
APAF Australia