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CHARACTERIZATION OF SELENOPROTEIN V
Author(s) -
Moustafa Mohamed ElSayed,
ElSrouji Rowan
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.916.12
Subject(s) - selenocysteine , selenoprotein , function (biology) , residue (chemistry) , genetics , biochemistry , chemistry , biology , cysteine , enzyme , glutathione , glutathione peroxidase
Selenoprotein V (SelV) is a mammalian selenoprotein encoded on chromosome 19. SelV is a globular protein that occurs in the seminiferous tubules of the testes. Its function is yet unknown. We used bioinformatics programs to study structure‐function relationship of SelV. Protein calculator program revealed that the molecular weight of SelV in human is about 37 kDa. Human SelV is a basic protein with isoelectric point of 9.65. Using bioinformatics programs, we predicted that SelV contains 5 exons, where the selenocysteine (sec) residue was predicted to be in exon 2. SECISearch 2.19 program revealed that the selenocysteine insertion sequence (SECIS) element belongs to type I structure. We also predicted that SelV contains three domains: The N‐terminal domain is proline‐rich; the second domain is the hydrophobic domain containing 20 amino acid residues as well as the selenocysteine residue; and the C‐terminal domain which is rich in glutamate and lysine. Further studies are required to understand why mammalian SelV is rich in proline residues and why selenocysteine residue resides in hydrophobic domain in this selenoprotein.