IED ID | IndEnz0002008306 |
Enzyme Type ID | protease008306 |
Protein Name |
Plasmepsin X EC 3.4.23.- Plasmepsin 10 |
Gene Name | PMX CK202_2307 PFNF54_02086 |
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 | MKRISPLNTLFYLSLFFSYTFKGLKCTRIYKIGTKALPCSECHDVFDCTGCLFEEKESSHVIPLKLNKKNPNDHKKLQKHHESLKLGDVKYYVNRGEGISGSLGTSSGNTLDDMDLINEEINKKRTNAQLDEKNFLDFTTYNKNKAQDISDHLSDIQKHVYEQDAQKGNKNFTNNENNSDNENNSDNENNSDNENNLDNENNLDNENNSDNSSIEKNFIALENKNATVEQTKENIFLVPLKHLRDSQFVGELLVGTPPQTVYPIFDTGSTNVWVVTTACEEESCKKVRRYDPNKSKTFRRSFIEKNLHIVFGSGSISGSVGTDTFMLGKHLVRNQTFGLVESESNNNKNGGDNIFDYISFEGIVGLGFPGMLSAGNIPFFDNLLKQNPNVDPQFSFYISPYDGKSTLIIGGISKSFYEGDIYMLPVLKESYWEVKLDELYIGKERICCDEESYVIFDTGTSYNTMPSSQMKTFLNLIHSTACTEQNYKDILKSYPIIKYVFGELIIELHPEEYMILNDDVCMPAYMQIDVPSERNHAYLLGSLSFMRNFFTVFVRGTESRPSMVGVARAKSKN |
Enzyme Length | 573 |
Uniprot Accession Number | W7JWW5 |
Absorption | |
Active Site | ACT_SITE 266; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 457; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by aminohydantoin compounds such as CWHM-117. {ECO:0000269|PubMed:29074774}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: During the asexual blood stage, processes key proteins essential for merozoite egress and invasion of host erythrocytes (PubMed:29074774). Cleaves and activates proteases SUB1 and SUB2 (PubMed:29074774). May process members of the EBL and Rh protein families (By similarity). Also cleaves apical membrane protein AMA1 (By similarity). During the mosquito vector stage and probably in ookinetes, cleaves CelTOS (By similarity). {ECO:0000250|UniProtKB:Q8IAS0, ECO:0000269|PubMed:29074774}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Mutagenesis (1); Propeptide (1); Signal peptide (1) |
Keywords | Aspartyl protease;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to exonemes which are secretory vesicles that discharge their content during egress into the parasitophorous vacuole. {ECO:0000269|PubMed:29074774}. |
Modified Residue | |
Post Translational Modification | PTM: Autocleaved into a p16 prodomain form and two mature forms p44 and p51. {ECO:0000250|UniProtKB:Q8IAS0}. |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 65,114 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |