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In animals, malectin is well known to play an essential role in endoplasmic reticulum quality control (ERQC) by interacting with ribophorin I, one unit of the oligosaccharyltransferase (OST) complex. However, the functions of malectin in plants remain largely unknown. Here, we demonstrate the rice <i>OsMLD1</i> is an ER- and Golgi-associated malectin protein and physically interacts with rice homolog of ribophorin I (OsRpn1), and its disruption leads to spontaneous lesion mimic lesions, enhanced disease resistance, and prolonged ER stress. In addition, there are many more <i>N</i>-glycosites and <i>N</i>-glycoproteins identified from the <i>mld1</i> mutant than wildtype. Furthermore, OsSERK1 and OsSERK2, which have more <i>N</i>-glycosites in <i>mld1</i>, were demonstrated to interact with OsMLD1. <i>OsMLD1</i> can suppress OsSERK1- or OsSERK2-induced cell death. Thus, <i>OsMLD1</i> may play a similar role to its mammalian homologs in glycoprotein quality control, thereby regulating cell death and immunity of rice, which uncovers the function of malectin in plants.