3.4.21.B26	alpha-dystroglycan + H2O	cleavage site (ANKKPPLPKRVRR312-/-QIHATPTP). Full-length alpha-dystroglycan in the human endometrial epithelium is a barrier for embryo attachment and removal of the N-terminus by proprotein convertase 5/6 regulates receptivity. Removal of alpha-dystroglycan N-terminus is an important posttranslational control of endometrial receptivity and uterine fluid	
3.4.21.B26	human immunodeficiency virus type 1 Vpr + H2O	undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr	
3.4.21.B26	additional information	death at birth of the PC5/6-deficient embryos	
3.4.21.B26	osteopontin + H2O	Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype	
3.4.21.B26	preprohepcidin + H2O	key role of the convertases furin, PACE4, PC5 and/or PC7 in the generation and secretion of active hepcidin	
3.4.21.B26	pro-integrin-alpha5 + H2O	cleavage of the substrate into its heavy and light chains	
3.4.21.B26	pro-integrin-alphaV + H2O	cleavage of the substrate into its heavy and light chains	
3.4.21.B26	proform bone morphogenetic protein-2 + H2O	-	
3.4.21.B26	proform platelet-derived growth factor A + H2O	activation, the substrate is localized specifically to the apical surface of the luminal and glandular epithelium of uterine endometrium in the receptive phase, but barely detectable in the non-receptive phase	
3.4.21.B26	protein tyrosine phosphatase kappa + H2O	the enzyme cleaves the ectodomain of protein tyrosine phosphatase kappa