Plays an essential role during the asexual blood stage development by controlling the kinetics of merozoite egress from host erythrocytes (By similarity). Specifically, prevents premature rupture of the parasitophorous vacuole and host erythrocyte membranes (By similarity). May prevent merozoite phagocytosis by host monocytes via interaction with host VTN at the merozoite surface (By similarity). Plays a role in parasite growth (PubMed:12244052). May interact (via C-terminus) with PTKL (via SAM domain). Interacts (via C-terminus) with human VTN (via hemopexin repeat 2); may form heterotetramers of two VTN and SERA5 P47 heterodimers; the interaction may protect merozoites from phagocytosis by host monocytes; VTN glycosylation appears to be dispensable for the interaction. Monomer. Interacts with kinase CPK1/CDPK1 at the schizont stage. Secreted in large amount into the parasitophorous vacuole. Secreted during merozoite egress from erythrocytes. Secreted during merozoite egress from erythrocytes. Secreted during merozoite egress from erythrocytes. Secreted during merozoite egress from erythrocytes (By similarity). Colocalizes at the merozoite surface with human VTN (By similarity). Secreted during egress from host erythrocytes. Secreted during egress from host erythrocytes. Expressed during parasite asexual blood stages, specifically at the late trophozoite and schizont stages (at protein level). Phosphorylation by CPK1/CDPK1 increases SERA5 protease activity towards a synthetic peptide in vitro. Just prior to merozoite egress from host erythrocytes, proteolytically cleaved into multiple fragments (PubMed:1501648). Cleaved by SUB1 into p47 and p73, p73 is further cleaved by SUB1 into p56 and p18 and p56 is further processed into p50 by an unidentified protease (PubMed:1501648). p47 remains covalently associated with p18 via disulfide bond (By similarity). p47 can be processed into p25n and p25c by SUB1 (By similarity). p25c and p25n remain associated with p18 (By similarity). Proteolytic processing is essential for merozoite egress from host erythrocytes (By similarity). The cleavage of the propeptide to produce p50 is necessary for protease activity and to promote merozoite egress (By similarity). Potential candidate for the development of parasite blood stage vaccines (PubMed:12244052). In vitro and in vivo, induces antibodies capable of inhibiting parasite growth (PubMed:12244052). Belongs to the peptidase C1 family. In contrast to other serine-repeat antigen proteins (SERA) of the peptidase C1 family, contains a serine residue at the position of the canonical catalytic cysteine and has been shown to lack protease activity (By similarity). However, other studies show that it has protease activity towards synthetic peptides in vitro (By similarity).