About Gene List

PF3D7_1323500 (PMV)

Genome location: Pf3D7_13_v3:973,969..977,910(+)

Genome classification: Core

Function and Localization

Product Description: plasmepsin V

SignalP Peptide: N/A

# Transmembrane Domains: 2

EC Numbers: 3.4.23.- (Aspartic endopeptidases.)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005783 endoplasmic reticulum
Component GO:0016021 integral component of membrane
Component GO:0016020 membrane
Component GO:0097038 perinuclear endoplasmic reticulum
Function GO:0004190 aspartic-type endopeptidase activity
Function GO:0005515 protein binding
Process GO:0006508 proteolysis
Process GO:0009410 response to xenobiotic stimulus

Expression by stage (LR - Le Roch et al., and MCA - Malaria Cell Atlas):

Stage LR class MCA mean MCA prop. zeros
Sporozoite not expressed N/A N/A
Ring expressed 0.13 0.93
Trophozoite expressed 0.22 0.85
Schizont expressed 0.16 0.89
Gametocyte not expressed 0.18 0.89

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1323500

Resistome Missense Mutations: None

Resistome Compounds with Missense Mutations: None

Resistome # Samples with Disruptive Mutations: 0 (0 missense, 0 "interesting" missense)

Essentiality (ABS)

Zhang Phenotype: Non - Mutable in CDS

MIS: 0.136 | MFS: -2.863 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1338700)

  • Relative Growth Rate: 0.02 ± 0.10
  • Confidence: 6.05

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8I6Z5

"Best" AlphaFill ligand hit: CPS (chaps, Local RMSD=0.08) with 7VE0 (Global RMSD=6.94)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
3.4.23.- Ex: renin I2YYKCNSDSIAANBSDANEDTAPI-3DMSOPCMBTLCK...

Orthology to BindingDB Entries:

UniProt Protein Name Species Homology Source BindingDB Ligands
Q8I6Z5 Plasmepsin V HOGENOM, OMA, OrthoDB, OrthoMCL, OrthoMCL BLAST CHEMBL3344151CHEMBL3344152CHEMBL3344153CHEMBL3344154...
A0A0H4FQ60 Plasmepsin V OrthoMCL BLAST CHEMBL3344272

Orthology Information

Ortholog Group (OrthoMCL): OG6_107443

No human ortholog(s)

Protein Information

Protein Length: 590 | Molecular Weight (kDa): 68.48

UniProt ID(s): Q17SA7, Q17SA8, Q17SA9, Q8I6Z5

PDB ID(s): None

Isoelectric Point: 7.58

Protein Domain Annotations:

Source Family ID Description
InterPro IPR001461 Aspartic peptidase A1 family
InterPro IPR001969 Aspartic peptidase, active site
InterPro IPR021109 Aspartic peptidase domain superfamily
InterPro IPR032861 Xylanase inhibitor, N-terminal
InterPro IPR033121 Peptidase family A1 domain
InterPro IPR033866 Plasmepsin 5
PFam PF00026 Peptidase family A1 domain
PFam PF14543 Xylanase inhibitor, N-terminal
Superfamily SSF50630 Aspartic peptidase domain superfamily

Genetic Variation

MalariaGEN Pf7 (worldwide samples) # unique SNV/indels:

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 5 42 14 27
disruptive 14 63 28 70
missense 12 52 24 49

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 13 64 20 34
disruptive 27 124 56 126
missense 20 86 37 79

PlasmoDB Total SNPs: 262

Non-coding: 186 | Synonymous: 42 | Nonsynonymous: 34 | Stop Codon: 0

Associated Publications

PMID Title Authors DOI/Link
15899698 P. falciparum pro-histoaspartic protease (proHAP) protein peptides bindspecifically to erythrocytes and inhibit the invasion process in vitro. Valbuena J, Vera R, ..., Patarroyo ME 10.1515/BC.2005.043
16024107 Characterization of plasmepsin V, a membrane-bound aspartic protease homolog inthe endoplasmic reticulum of Plasmodium falciparum. Klemba M, Goldberg DE https://pubmed.ncbi.nlm.nih.gov/16024107/
23387285 Role of plasmepsin V in export of diverse protein families from the Plasmodiumfalciparum exportome. Boddey JA, Carvalho TG, ..., Cowman AF 10.1111/tra.12053
24983235 Inhibition of Plasmepsin V activity demonstrates its essential role in proteinexport, PfEMP1 display, and survival of malaria parasites. Sleebs BE, Lopaticki S, ..., Boddey JA 10.1371/journal.pbio.1001897
25849462 Experimental determination of the membrane topology of the Plasmodium proteasePlasmepsin V. Tarr SJ, Osborne AR 10.1371/journal.pone.0121786
26146842 Flap flexibility amongst plasmepsins I, II, III, IV, and V: Sequence, structural,and molecular dynamics analyses. McGillewie L, Soliman ME 10.1002/prot.24855
26214367 Structural basis for plasmepsin V inhibition that blocks export of malariaproteins to human erythrocytes. Hodder AN, Sleebs BE, ..., Cowman AF 10.1038/nsmb.3061
27531685 Understanding the structural basis of substrate recognition by Plasmodiumfalciparum plasmepsin V to aid in the design of potent inhibitors. Bedi RK, Patel C, ..., Bhaumik P 10.1038/srep31420
30127496 Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmicreticulum translocation interactome for export to the erythrocyte. Marapana DS, Dagley LF, ..., Cowman AF 10.1038/s41564-018-0219-2
30320974 Targeting the Plasmodium falciparum plasmepsin V by ligand-based virtualscreening. Meissner KA, Kronenberger T, ..., Wrenger C 10.1111/cbdd.13416
31108131 Yield improvement and enzymatic dissection of Plasmodium falciparum plasmepsin V. Loymunkong C, Sittikul P, ..., Boonyalai N 10.1016/j.molbiopara.2019.111188
31851913 Inhibition of Plasmepsin V Activity Blocks Plasmodium falciparumGametocytogenesis and Transmission to Mosquitoes. Jennison C, Lucantoni L, ..., Boddey JA 10.1016/j.celrep.2019.11.073
38334391 PEXEL is a proteolytic maturation site for both exported and non-exported Plasmodium proteins Fierro MA, Muheljic A, ..., Beck JR 10.1128/msphere.00393-23