About Gene List

PF3D7_1423300 (PP7)

Genome location: Pf3D7_14_v3:935,849..941,730(+)

Genome classification: Core

Function and Localization

Product Description: serine/threonine protein phosphatase 7

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 3.1.3.16 (Protein-serine/threonine phosphatase)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005737 cytoplasm
Component GO:0005829 cytosol
Component GO:0005634 nucleus
Function GO:0004722 protein serine/threonine phosphatase activity
Process GO:0006470 protein dephosphorylation

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 not expressed 0.23 0.90
Trophozoite not expressed 0.07 0.96
Schizont expressed 1.77 0.39
Gametocyte not expressed 0.36 0.80

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1423300

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: 0.357 | MFS: -2.633 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1020100)

  • Relative Growth Rate: 0.12 ± 0.17
  • Confidence: 4.90

RMgmDB ABS Phenotype: Different from wild type (Pb ortholog: PBANKA_1020100)

Modification: Tagged | RMgm-1071

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8ILL9

"Best" AlphaFill ligand hit: NHE (2-[n-cyclohexylamino]ethane sulfonic acid, Local RMSD=0.30) with 6GHM (Global RMSD=3.37)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
3.1.3.16 protein-serine/threonine phosphatase ATPADPUDPAMPGTPUTPUMPNaFEDTAEGTAcAMPNADPH...

No evidence of orthology to BindingDB entries

Orthology Information

Ortholog Group (OrthoMCL): OG6_113318

No human ortholog(s)

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 5 33 30 63
disruptive 5 33 20 68
missense 5 33 19 62

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 10 88 46 65
disruptive 11 100 69 173
missense 8 84 58 117

PlasmoDB Total SNPs: 432

Non-coding: 385 | Synonymous: 42 | Nonsynonymous: 4 | Stop Codon: 1

Protein Information

Protein Length: 959 | Molecular Weight (kDa): 112.585

UniProt ID(s): Q8ILL9, Q9U493

PDB ID(s): None

Isoelectric Point: 6.94

Protein Domain Annotations:

Source Family ID Description
InterPro IPR000048 IQ motif, EF-hand binding site
InterPro IPR002048 EF-hand domain
InterPro IPR004843 Calcineurin-like phosphoesterase domain, ApaH type
InterPro IPR006186 Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
InterPro IPR011992 EF-hand domain pair
PFam PF00149 Calcineurin-like phosphoesterase domain, ApaH type
PFam PF13499 EF-hand domain
Superfamily SSF47473 EF-hand domain pair
Superfamily SSF56300

Associated Publications

PMID Title Authors DOI/Link
11377737 Characterization of a novel serine/threonine protein phosphatase (PfPPJ) from themalaria parasite, Plasmodium falciparum. Dobson S, Bracchi V, Chakrabarti D, Barik S 10.1016/s0166-6851(01)00260-2
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
16629662 Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, anovel leucine-rich repeat protein of the human malaria parasite Plasmodiumfalciparum. Daher W, Browaeys E, ..., Khalife J 10.1111/j.1365-2958.2006.05119.x
23181666 Organellar proteomics reveals hundreds of novel nuclear proteins in the malariaparasite Plasmodium falciparum. Oehring SC, Woodcroft BJ, ..., Voss TS 10.1186/gb-2012-13-11-r108
25011111 Genome-wide functional analysis of Plasmodium protein phosphatases reveals keyregulators of parasite development and differentiation. Guttery DS, Poulin B, ..., Tewari R 10.1016/j.chom.2014.05.020
38026848 Quantitative and modularized CRISPR/dCas9-dCpf1 dual function system in Saccharomyces cerevisiae Feng Q, Ning X, ..., Li C 10.3389/fbioe.2023.1218832