IED ID | IndEnz0002009631 |
Enzyme Type ID | protease009631 |
Protein Name |
Plasmepsin V EC 3.4.23.- Plasmepsin 5 |
Gene Name | PMV CK202_2868 PFNF54_04321 |
Organism | Plasmodium falciparum (isolate NF54) |
Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate NF54) |
Enzyme Sequence | MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDVIVSNNVEDIVWQAITRKYYYYIKIYGLDLYGTNIMDKKELDMLVDSGSTFTHIPENIYNQINYYLDILCIHDMTNIYEINKRLKLTNESLNKPLVYFEDFKTALKNIIQNENLCIKIVDGVQCWKSLENLPNLYITLSNNYKMIWKPSSYLYKKESFWCKGLEKQVNNKPILGLTFFKNKQVIFDLQQNQIAFIESKCPSNLTSSRPRTFNEYREKENIFLKVSYINLYCLWLLLALTILLSLILYVRKMFYMDYFPLSDQNKSPIQEST |
Enzyme Length | 590 |
Uniprot Accession Number | W7JPD9 |
Absorption | |
Active Site | ACT_SITE 118; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 365; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: 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 (PubMed:32069391). 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 (PubMed:31851913). {ECO:0000250|UniProtKB:Q8I6Z5, ECO:0000269|PubMed:31851913, ECO:0000269|PubMed:32069391}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Coiled coil (1); Disulfide bond (7); Domain (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | Aspartyl protease;Coiled coil;Disulfide bond;Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31851913}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8I6Z5}. Note=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. {ECO:0000269|PubMed:31851913}. |
Modified Residue | |
Post Translational Modification | PTM: It is not clear if the zymogen has a cleavable propeptide (By similarity). In vitro, appears to be cleaved between Asn-80 and Ala-81 (By similarity). Cleavage of the putative propeptide is dispensable for catalytic activity (By similarity). {ECO:0000250|UniProtKB:Q8I6Z5}. |
Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000305 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 68,480 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |