High impact information on Svs2

• As a result, the 100-kDa protein was identified as the seminal vesicle secretory protein II (SVS-II), a major constituent of the seminal coagulum [1].
• The gene encoding rat seminal vesicle secretion II (SVS II) protein has been cloned from a rat genomic DNA library using a cDNA probe generated from rat dorsal prostate androgen-dependent mRNA [2].
• A 13-residue structure with the consensus sequence GSQLKSFGQVKSS is repeated 13 times within the SVS II protein and appears to be involved in the formation of the rat copulatory plug via a transglutaminase reaction cross-linking glutamine and lysine residues [2].
• The cloned 7.3-kilobase pair genomic fragment contains approximately 5000 base pairs (bp) of the 5'-flanking region and the entire coding region of the SVS II protein within two exons [2].
• The 5'-flanking region contains three conserved elements found in other seminal vesicle secretion genes (SVS IV-VI proteins) within 250 bp of the transcription start site as well as a glucocorticoid response element at position -314 in the SVS II gene [2].

Biological context of Svs2

• Concomitant with the gene analysis, the rat SVS II protein was purified to homogeneity, and 333 residues (85%) of the amino acid sequence were determined by automated Edman degradation [2].
• SVS II affects the kinetics of actin polymerization in the same way as do barbed end capping proteins [3].
• Monospecific polyclonal antibodies directed against the N-terminus of actin cross-react with SVS II, but there is no cross-reaction by a monoclonal antibody directed against a C-terminal epitope on actin [3].
• Rat seminal-vesicle secretory protein SVS II binds DNA with a preference for the 5' regulatory region of secretory protein SVS IV gene: co-isolation with components of the nuclear matrix [4].
• SVS II binding to SVS IV-7S DNA was greater than its binding to either a comparable fragment of the C3 gene or linearized pUC-19 plasmid, and it was not eliminated by a 100-fold competition [4].

Anatomical context of Svs2

• When seminal-vesicle fluid was mixed with rat liver, some SVS II co-isolated with the nuclear-matrix proteins, indicating that nonspecific interactions contribute to its association with the nucleoskeleton [4].
• The secreted polypeptide is a protein of Mr 38442 and is similar in sequence but smaller than the major clot-forming protein of rat semen, SVS II [5].
• However, these interactions may not represent the intracellular behavior of SVS II in seminal-vesicle epithelium [4].
• The subcellular distribution of both proteins was clearly different: SVS II was exclusively confined to the electron dense core of the secretory vacuoles, while SVS IV was detected only in the clear halo surrounding the central granule [6].
• Using an antibody against the SVS II polypeptide from rat seminal vesicles, an intrinsic immunoreactive protein was detected in the principal piece of the sperm tail as well as an extrinsic protein (presumably secreted by the epididymis) on the sperm head [7].

Associations of Svs2 with chemical compounds

• Reducing agent (10 mM dithiothreitol) and acidic (pH 6.5) buffer did not eliminate SVS II, but isolation of nuclear matrices with ammonium sulfate, nucleases, and urea decreased SVS II immunoreactivity and removed actin-like protein [4].
• A glycoprotein, designated SVS II, is secreted in an androgen-dependent manner from lateral prostate and seminal vesicles of the rat [8].

Analytical, diagnostic and therapeutic context of Svs2

• Sequencing revealed that this band was a seminal-vesicle secretory protein, SVS II, whose identity was confirmed with an anti-SVS II antiserum in western blots [4].
• Recent sequence analysis of SVS II shows a sequence of about 14 residues that is repeated 13 times between residues 86 and 298 [3].
• Expression of lobe-specific proteins for the ventral (prostatic steroid binding protein [PSBP]) lateral (seminal vesicle secretion II [SVS II]), and dorsal prostate (secretory transglutaminase [TGase]) were examined by immunocytochemistry [9].

References