During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence (By similarity). Specifically, cleaves after the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including RESA, EMP2, EMP3, KAHRP, RIF/Rifin and STEVOR (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity). Component of a complex composed of SPC25 and PMV; the interaction is mediated via the transmembrane domains. The complex interacts with the SEC61 channel-forming translocon complex and is involved in the recognition and import of PEXEL motif-containing proteins into the ER for subsequent export. During gametogenesis, localizes to the perinuclear ER in stage I-II gametocytes, and relocalizes towards the cell periphery as the ER redistributes in the cell in stage III-IV gametocytes (By similarity). Partially colocalizes with SPC25 in the endoplasmic reticulum (By similarity). Expressed during the asexual blood stage; expression is low at the ring stage and then increases through the trophozoite and schizont stages (at protein level). The transmembrane domain is essential for localization to the endoplasmic reticulum. It is not clear if the zymogen has a cleavable propeptide (PubMed:16024107). In vitro, appears to be cleaved between Asn-87 and Ala-88 (By similarity). Cleavage of the putative propeptide is dispensable for catalytic activity (By similarity). Belongs to the peptidase A1 family. It is unclear if PMV is glycosylated as other members of the same enzyme family, ie. PMI and PMII, are not.