Signal recognition particle subunit SRP72 (SRP72)

SRP72 is the largest protein subunit of the mammalian signal recognition particle (SRP), a ribonucleoprotein complex that recognizes and targets nascent secretory and membrane proteins to the endoplasmic reticulum (ER) during translation[1][2][3][5][11]. SRP72 forms a heterodimer with SRP68, and together these two proteins constitute most of the protein mass of the SRP S domain, playing pivotal roles in SRP assembly, function, and protein translocation[1][3]. Structurally, SRP72 contains tetratricopeptide repeats enabling protein-protein interaction, especially with SRP68[3]. SRP72 is post-translationally regulated via phosphorylation and caspase-mediated cleavage during apoptosis, with this processing implicated in autoimmunity[1]. Pathogenic mutations in SRP72 are linked to familial bone marrow failure syndromes and an increased risk of acute myeloid leukemia[1][2]. Although SRP72 itself is not a therapeutic target (such as a receptor, enzyme, or direct drug target), its essential role in cellular protein trafficking, disease association, and structural uniqueness make it significant in biology and medicine[1][2][3][5].

Other names

Signal recognition particle 72 kDa proteinBMFFBMFS1HEL103epididymis luminal protein 103signal recognition particle 72kDsignal recognition particle 72kDa