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Here, we report a novel member of the c\u2010type LYZ family, the seminal vesicle\u2010secreted LYZ c\u2010like protein (SVLLP). Three forms of SVLLP were purified from mouse seminal vesicle secretions and characterized as glycoproteins with the same protein core but different N\u2010linked glycans. SVLLP is structurally similar to c\u2010type LYZ proteins. Only one of the 20 invariant residues was altered in the consensus sequence of c\u2010type LYZs; however, the changed residue (N53S) is one of two essential catalytic residues. LYZ activity assays demonstrated that the three glycoforms of SVLLP lacked enzyme activity. SVLLP is primarily expressed in seminal vesicles. Immunohistochemistry revealed that it occurs in the luminal fluid and mucosal epithelium of the seminal vesicles. Testosterone is not the primary regulator for its expression in the seminal vesicle. SVLLP binds to sperm and suppresses bovine serum albumin\u2010induced sperm capacitation, inhibits the acrosome reaction, and blocks sperm\u2013oocyte interactions in vitro, suggesting that SVLLP is a sperm capacitation inhibitor.<\/jats:p>","DOI":"10.1002\/jcb.29894","type":"journal-article","created":{"date-parts":[[2021,1,20]],"date-time":"2021-01-20T05:17:55Z","timestamp":1611119875000},"page":"653-666","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["A mouse seminal vesicle\u2010secreted lysozyme c\u2010like protein modulates sperm capacitation"],"prefix":"10.1002","volume":"122","author":[{"given":"Chung\u2010Mao","family":"Ou","sequence":"first","affiliation":[{"name":"Chemistry Division Institute of Nuclear Energy Research Taoyuan City Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert Kuo\u2010Kuang","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of 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