About Gene List

PF3D7_0113700 (HSP40)

Genome location: Pf3D7_01_v3:519,766..523,106(+)

Genome classification: Core

Function and Localization

Product Description: heat shock protein 40, type II

SignalP Peptide: N/A

# Transmembrane Domains: 1

EC Numbers: None

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0020036 Maurer's cleft
Component GO:0005829 cytosol
Component GO:0044164 host cell cytosol
Function GO:0051087 chaperone binding
Function GO:0015485 cholesterol binding
Function GO:0042393 histone binding
Function GO:0005515 protein binding
Function GO:0051082 unfolded protein binding
Process GO:0051085 chaperone cofactor-dependent protein refolding
Process GO:0020035 cytoadherence to microvasculature, mediated by symbiont protein
Process GO:0009408 response to heat

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 0.37 0.82
Trophozoite possibly expressed 0.18 0.90
Schizont possibly expressed 0.09 0.94
Gametocyte not expressed 0.07 0.96

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_0113700

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: Mutable in CDS

MIS: 1 | MFS: -0.674 | #Insertions: 2

PlasmoGEM Phenotype: Dispensable (Pb ortholog: PBANKA_0310000)

  • Relative Growth Rate: 0.90 ± 0.13
  • Confidence: 5.53

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8I2E1

"Best" AlphaFill ligand hit: No AlphaFill hits

No associated EC numbers

Orthology to BindingDB Entries:

UniProt Protein Name Species Homology Source BindingDB Ligands
P31689 DnaJ homolog subfamily A member 1 Homo sapiens OrthoDB CHEMBL52073CHEMBL159171

Orthology Information

Ortholog Group (OrthoMCL): OG6_100302

Most Similar Human Ortholog: H0Y4S1

TM-align score: 0.85 | RMSD: 1.51

Seq Identity: 0.46 | Length: 33 / 402

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000132002 DnaJ heat shock protein family (Hsp40) member B1
ENSG00000137094 DnaJ heat shock protein family (Hsp40) member B5
ENSG00000162616 DnaJ heat shock protein family (Hsp40) member B4
ENSG00000187726 DnaJ heat shock protein family (Hsp40) member B13

Protein Information

Protein Length: 402 | Molecular Weight (kDa): 46.988

UniProt ID(s): Q8I2E1

PDB ID(s): 6RZY

Isoelectric Point: 8.39

Protein Domain Annotations:

Source Family ID Description
InterPro IPR001623 DnaJ domain
InterPro IPR002939 Chaperone DnaJ, C-terminal
InterPro IPR008971 HSP40/DnaJ peptide-binding
InterPro IPR018253 DnaJ domain, conserved site
InterPro IPR036869 Chaperone J-domain superfamily
PFam PF00226 DnaJ domain
PFam PF01556 Chaperone DnaJ, C-terminal
Superfamily SSF46565 Chaperone J-domain superfamily
Superfamily SSF49493 HSP40/DnaJ peptide-binding

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 4 14 7 23
disruptive 4 20 11 46
missense 4 20 10 41

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 4 33 15 31
disruptive 8 55 50 99
missense 7 45 42 77

PlasmoDB Total SNPs: 245

Non-coding: 225 | Synonymous: 14 | Nonsynonymous: 6 | Stop Codon: 0

Associated Publications

PMID Title Authors DOI/Link
12368867 Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13. Hall N, Pain A, ..., Barrell BG 10.1038/nature01095
20482550 Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol ofthe P. falciparum-infected erythrocyte. Kulzer S, Rug M, ..., Przyborski JM 10.1111/j.1462-5822.2010.01477.x
26845441 The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x. Daniyan MO, Boshoff A, ..., Blatch GL 10.1371/journal.pone.0148517
30804381 Cholesterol bound Plasmodium falciparum co-chaperone 'PFA0660w' complexes withmajor virulence factor 'PfEMP1' via chaperone 'PfHsp70-x'. Behl A, Kumar V, ..., Mishra PC 10.1038/s41598-019-39217-y
31430682 Structural insights into the binding mechanism of Plasmodium falciparum exportedHsp40-Hsp70 chaperone pair. Behl A, Mishra PC 10.1016/j.compbiolchem.2019.107099
31631203 A network-based approach reveals novel invasion and Maurer's clefts-relatedproteins in Plasmodium falciparum. Das D, Krishnan SR, Roy A, Bulusu G 10.1039/c9mo00124g
34614006 Co-chaperone involvement in knob biogenesis implicates host-derived chaperones inmalaria virulence. Diehl M, Roling L, ..., Przyborski JM 10.1371/journal.ppat.1009969
38418371 Plasmodium falciparum J-dot localized J domain protein A8iJp modulates thechaperone activity of human HSPA8 Sahu W, Bai T, ..., Reddy KS 10.1002/1873-3468.14836
38377589 The Regulatory Effect of Huangshui Polysaccharides on Intestinal Microbiota andMetabolites during In Vitro Fermentation Li M, Su J, ..., Liang H 10.1021/acs.jafc.3c08658