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However, other proteins bearing this modification in vivo are still largely unknown. Here, we describe a highly reliable method combining glycosidase treatment with LC\u2013MS analyses to identify mammalian <jats:italic>O<\/jats:italic>\u2010mannosylated proteins from tissue sources. Our workflow identified T\u2010cadherin (H\u2010cadherin, CDH13) as a novel <jats:italic>O<\/jats:italic>\u2010mannosylated protein. In contrast to known <jats:italic>O<\/jats:italic>\u2010mannosylated proteins, single mannose residues (Man\u2010\u03b1\u2010Ser\/Thr) are attached to this cell adhesion molecule. Conserved <jats:italic>O<\/jats:italic>\u2010glycosylation sites in T\u2010, E\u2010 and N\u2010cadherins from different species, point to a general role of <jats:italic>O<\/jats:italic>\u2010mannosyl glycans for cadherin function.<\/jats:p>","DOI":"10.1016\/j.febslet.2013.09.041","type":"journal-article","created":{"date-parts":[[2013,10,7]],"date-time":"2013-10-07T15:45:18Z","timestamp":1381160718000},"page":"3715-3721","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["<i>O<\/i>\u2010glycosylation of the non\u2010canonical T\u2010cadherin from rabbit skeletal muscle by single mannose residues"],"prefix":"10.1002","volume":"587","author":[{"given":"Patrick 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