Detail Information for IndEnz0002009631
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