Detail Information for IndEnz0002009628
IED ID IndEnz0002009628
Enzyme Type ID protease009628
Protein Name Plasmepsin V
PfPMV
EC 3.4.23.-
Plasmepsin 5
Gene Name PMV PF3D7_1323500
Organism Plasmodium falciparum (isolate 3D7)
Taxonomic Lineage cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7)
Enzyme Sequence MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDVIVSNNVEDIVWQAITRKYYYYIKIYGLDLYGTNIMDKKELDMLVDSGSTFTHIPENIYNQINYYLDILCIHDMTNIYEINKRLKLTNESLNKPLVYFEDFKTALKNIIQNENLCIKIVDGVQCWKSLENLPNLYITLSNNYKMIWKPSSYLYKKESFWCKGLEKQVNNKPILGLTFFKNKQVIFDLQQNQIAFIESKCPSNLTSSRPRTFNEYREKENIFLKVSYINLYCLWLLLALTILLSLILYVRKMFYMDYFPLSDQNKSPIQEST
Enzyme Length 590
Uniprot Accession Number Q8I6Z5
Absorption
Active Site ACT_SITE 118; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 365; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
Activity Regulation ACTIVITY REGULATION: Inhibited by peptidomimetic inhibitor WEHI-842 (PubMed:26214367). Inhibited by Cu(2+) and Hg(2+) (PubMed:25447707). {ECO:0000269|PubMed:25447707, ECO:0000269|PubMed:26214367}.
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:20130643, PubMed:20130644, PubMed:24983235, PubMed:30127496, PubMed:30517136). 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 (PubMed:20130643, PubMed:20130644, PubMed:23387285, PubMed:25447707, PubMed:25986559, PubMed:24983235). Also, by regulating protein export, plays an essential role in gametocyte development and thus, parasite transmission to the mosquito vector (By similarity). {ECO:0000250|UniProtKB:W7JPD9, ECO:0000269|PubMed:20130643, ECO:0000269|PubMed:20130644, ECO:0000269|PubMed:23387285, ECO:0000269|PubMed:24983235, ECO:0000269|PubMed:25447707, ECO:0000269|PubMed:25986559, ECO:0000269|PubMed:30127496, ECO:0000269|PubMed:30517136}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5.5 and 7. {ECO:0000269|PubMed:25447707, ECO:0000269|PubMed:25986559};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Coiled coil (1); Disulfide bond (7); Domain (1); Mutagenesis (4); 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:20117149, ECO:0000269|PubMed:20130643, ECO:0000269|PubMed:20130644, ECO:0000269|PubMed:24983235, ECO:0000269|PubMed:25849462, ECO:0000269|PubMed:30127496}; Single-pass type I membrane protein {ECO:0000269|PubMed:25849462}. 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 (By similarity). Partially colocalizes with SPC25 in the endoplasmic reticulum (PubMed:30127496). {ECO:0000250|UniProtKB:W7JPD9, ECO:0000269|PubMed:30127496}.
Modified Residue
Post Translational Modification PTM: It is not clear if the zymogen has a cleavable propeptide (PubMed:25447707). In vitro, appears to be cleaved between Asn-80 and Ala-81 (PubMed:25447707). Cleavage of the putative propeptide is dispensable for catalytic activity (PubMed:25447707, PubMed:25986559). {ECO:0000269|PubMed:25447707, ECO:0000269|PubMed:25986559}.
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 3.4.23.B19;