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    PF3D7_1323500 plasmepsin V [ Plasmodium falciparum 3D7 ]

    Gene ID: 814104, updated on 12-Sep-2024

    Summary

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    Gene symbol
    PF3D7_1323500
    Gene description
    plasmepsin V
    Locus tag
    PF3D7_1323500
    See related
    PlasmoDB:PF3D7_1323500; VEuPathDB:PF3D7_1323500
    Gene type
    protein coding
    RNA name
    plasmepsin V
    RefSeq status
    PROVISIONAL
    Organism
    Plasmodium falciparum 3D7 (isolate: 3D7)
    Lineage
    Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania)
    Orthologs
    all
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    Genomic context

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    See PF3D7_1323500 in Genome Data Viewer
    Location:
    chromosome: 13
    Exon count:
    1
    Sequence:
    Chromosome: 13; NC_004331.3 (975403..977175)

    Chromosome 13 - NC_004331.3Genomic Context describing neighboring genes Neighboring gene N-acetyltransferase, GNAT family, putative Neighboring gene 60S ribosomal protein L23 Neighboring gene conserved protein, unknown function Neighboring gene glideosome associated protein with multiple membrane spans 1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_004331.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Yield improvement and enzymatic dissection of Plasmodium falciparum plasmepsin V. Loymunkong C, et al. Mol Biochem Parasitol, 2019 Jul. PMID 31108131
    2. Targeting the Plasmodium falciparum plasmepsin V by ligand-based virtual screening. Meissner KA, et al. Chem Biol Drug Des, 2019 Mar. PMID 30320974
    3. Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors. Bedi RK, et al. Sci Rep, 2016 Aug 17. PMID 27531685, Free PMC Article
    4. Flap flexibility amongst plasmepsins I, II, III, IV, and V: Sequence, structural, and molecular dynamics analyses. McGillewie L, et al. Proteins, 2015 Sep. PMID 26146842
    5. Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin V. Tarr SJ, et al. PLoS One, 2015. PMID 25849462, Free PMC Article

    See all (12) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Mutation of D365 of plasmepsin V had more pronounced effects on the catalytic efficiency than that of D11.
      Title: Yield improvement and enzymatic dissection of Plasmodium falciparum plasmepsin V.
    2. The presence of a flexible group at P2 and a bulky hydrophobic group at P3 position of the inhibitor is preferred in the PfPMV substrate binding pocket. Results from the present study will aid in the design of potent inhibitors of PM
      Title: Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors.
    3. Data show that the flap-structure in plasmepsins is made up of a flip tip in the N-terminal lying perpendicular to the active site, adjacent to the flexible loop region in the C-terminal.
      Title: Flap flexibility amongst plasmepsins I, II, III, IV, and V: Sequence, structural, and molecular dynamics analyses.
    4. Prior to export, the Host-Targeting motif is cleaved by the endoplasmic reticulum-resident protease Plasmepsin V and the newly generated N-terminus is N-alpha-acetylated by an unidentified enzyme.
      Title: Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin V.
    5. Data indicate that WEHI-842 inhibited plasmepsin V activity on erythrocyte membrane protein 3 (PfEMP3-GFP) expressed in parasites expressed in parasites.
      Title: Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes.
    6. findings demonstrate that PMV activity is essential for protein export, PfEMP1 surface display, cytoadherence, and parasite survival in human erythrocytes
      Title: Inhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasites.
    7. plasmepsin V has a role in export of diverse protein families from the Plasmodium falciparum exportome
      Title: Role of plasmepsin V in export of diverse protein families from the Plasmodium falciparum exportome.
    8. Two aspartic protease precursor high-activity binding peptides specifically bind to human erythrocytes and could be implicated in erythrocyte invasion by malarial parasite P. falciparum.
      Title: P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by GeneDB

    Function Evidence Code Pubs
    enables aspartic-type endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within response to xenobiotic stimulus IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in perinuclear endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    plasmepsin V
    XP_001349975.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_004331.3 Reference assembly

      Range
      975403..977175
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_001349939.1 → XP_001349975.1  plasmepsin V [Plasmodium falciparum 3D7]

      See identical proteins and their annotated locations for XP_001349975.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      Q8I6Z5, W7JPD9
      UniProtKB/TrEMBL
      A0A024WM86, A0A024X3I9, A0A8S9VMK5, Q17SA7, W4IXB5, W7J719
      Conserved Domains (2) summary
      cd06096
      Location:97 → 519
      Plasmepsin_5; Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite
      PTZ00147
      Location:8 → 149
      PTZ00147; plasmepsin-1; Provisional
    Nucleotide Protein
    Heading Accession and Version

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