{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe seminal vesicle secretion protein I (SVS I) is a major protein in mouse seminal vesicle secretions that plays an important role in male reproductive physiology. SVS I is initially synthesized as an 820–amino acid precursor containing a 24–residue signal peptide and is processed into a mature glycoprotein of approximately 91 kDa. Although the protein is homologous to amiloride-binding protein 1 and diamine oxidases, a key substitution at the active site (His for Tyr) suggests that SVS I has lost classical oxidase enzymatic activity. Instead, conserved histidine residues imply a role in copper binding, which may contribute to the protein’s structural or regulatory functions. Its gene structure, with five exons, and conserved genomic region in rodents highlight its evolutionary importance despite divergence from primate lineages."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSVS I expression is highly specific to the seminal vesicle, where its localization to the luminal epithelium of mucosal folds is indicative of a secretory and structural function. The mRNA levels are androgen-dependent and increase with sexual maturation, emphasizing its reproductive role. Functionally, SVS I is a target for type 4 transglutaminase (TG4), which mediates the covalent incorporation of substrates into the protein. Detailed fragment analyses of SVS I revealed that a central region (residues 79–259) undergoes efficient cross-linking at glutamine residues Q232 and Q254, suggesting that TG4-catalyzed crosslinking of SVS I is pivotal for the formation or stabilization of the seminal coagulum essential for sperm viability and fertility."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ake Lundwall, Johan Malm, Adam Clauss, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular cloning of complementary DNA encoding mouse seminal vesicle-secreted protein SVS I and demonstration of homology with copper amine oxidases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biol Reprod (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1095/biolreprod.103.019984"}], "href": "https://doi.org/10.1095/biolreprod.103.019984"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12930721"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12930721"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Huan-Chin Tseng, Han-Jia Lin, Jyh-Bing Tang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of the major TG4 cross-linking sites in the androgen-dependent SVS I exclusively expressed in mouse seminal vesicle."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.22190"}], "href": "https://doi.org/10.1002/jcb.22190"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19452452"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19452452"}]}]}]}