May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion. Interacts with PUM2, SNAPIN and CTNNB1. Interacts (via N-terminal region) with CTNND1. Interacts with DDX20 (via N-terminal region). Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ cells. Testis and ovary (at protein level). Predominantly expressed in testis. Specifically expressed during germline development. In adult tissues, it is mainly expressed in spermatogonia, the stem cells of the germline. Also expressed during meiosis in spermatocytes. Not present in late, post-meiotic stage germ cells. Expressed in fetal ovaries, while it is weakly or not expressed in mature postmeiotic oocytes, suggesting that it may be expressed in premeiotic female germ cells. Expressed at high levels only in the E-cadherin deficient cell lines. Highly expressed in lung carcinomas and mostly detected in invasive tumor cells and its expression correlates with tumor aggressiveness. Fetal ovary and fetal testis (at protein level). Down-regulated by E-cadherin. The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. It is essential for the translation repression activity of the protein. The N-terminal region and C-terminal zinc-finger RNA-binding domain are both necessary for interaction with SNAPIN. The disease is caused by variants affecting the gene represented in this entry. Belongs to the nanos family.