Shell matrix proteins (SMPs) are key components for the Mollusk shell biomineralization. SMPs function has been hypothesized in several proteins by bioinformatics analysis, and through in vitro crystallization assays. However, studies of the post-translational modifications (PTMs) of SMPs, which contribute to their structure and the function, are limited. This review provides the current status of the SMPs with the most common PTMs described (glycosylation, phosphorylation, and disulfide bond formation) and their role in shell biomineralization. Also, recent studies based on recombinant production of SMPs are discussed. Finally, recommendations for the study of SMPs and their PTMs are provided. The review showed that PTMs are widely distributed in SMPs, and their presence on SMPs may contribute to the modulation of their activity in some SMPs, contributing to the crystal growth formation and differentiation through different mechanisms, however, in a few cases the lack of the PTMs do not alter their inherent function.

壳基质蛋白 (SMP) 是软体动物壳生物矿化的关键成分。已经通过生物信息学分析和体外实验假设了 SMP 在几种蛋白质中的功能结晶测定。然而，对 SMP 的翻译后修饰 (PTM) 的研究对其结构和功能有贡献，但研究有限。本综述提供了 SMP 的当前状态以及所描述的最常见的 PTM（糖基化、磷酸化和二硫键形成）及其在壳生物矿化中的作用。此外，还讨论了最近基于 SMP 重组生产的研究。最后，提供了研究 SMP 及其 PTM 的建议。综述表明，PTMs 广泛分布于 SMPs 中，它们在 SMPs 上的存在可能有助于调节它们在某些 SMPs 中的活性，通过不同的机制促进晶体生长形成和分化，然而，在少数情况下，缺乏PTM 不会改变其固有功能。