E3 ubiquitin-protein ligase ring finger protein 133 (RNF133)

E3 ubiquitin-protein ligase ring finger protein 133 (RNF133) is an enzyme that catalyzes the transfer of ubiquitin from E2 conjugating enzymes to substrate proteins. It is specifically expressed in the testis and is essential for the proper morphological development and motility of sperm cells during spermiogenesis. RNF133 is a membrane-associated protein localized to the endoplasmic reticulum and facilitates selective protein degradation as part of the ER-associated degradation pathway. Loss of RNF133 activity in mice leads to severely reduced sperm fertility, abnormal sperm morphology, and impaired motility, highlighting its critical physiological role in male reproductive biology[1][2][4][5][7]. RNF133 is a member of the RING finger protein family of E3 ligases and interacts with UBE2J1, an ER-localized E2 ubiquitin-conjugating enzyme[1][2][5]. Currently, there are no drugs, established biomarkers, or clinical safety concerns directly linked to RNF133, though its essential role in spermatogenesis makes it a candidate for research in male fertility and contraceptive development.

Other names

RING finger protein 133RING-type E3 ubiquitin transferase RNF133E3 ubiquitin-protein ligase RNF133RNF133

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