About Gene List

PF3D7_1107000 (LSM4)

Genome location: Pf3D7_11_v3:290,954..292,740(+)

Genome classification: Core

Function and Localization

Product Description: U6 snRNA-associated Sm-like protein LSm4, putative

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: None

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0000932 P-body
Component GO:0046540 U4/U6 x U5 tri-snRNP complex
Component GO:0005688 U6 snRNP
Component GO:0005634 nucleus
Component GO:0005732 sno(s)RNA-containing ribonucleoprotein complex
Component GO:0097526 spliceosomal tri-snRNP complex
Function GO:0003723 RNA binding
Function GO:0017070 U6 snRNA binding
Process GO:0033962 P-body assembly
Process GO:0000398 mRNA splicing, via spliceosome
Process GO:0000387 spliceosomal snRNP assembly

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 0.05 0.98
Trophozoite expressed 0.14 0.91
Schizont expressed 0.04 0.97
Gametocyte expressed 0.09 0.95

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1107000

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 *tentative

MIS: 0.808 | MFS: -2.083 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_0939900)

  • Relative Growth Rate: 0.07 ± 0.13
  • Confidence: 5.44

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8IIT3

"Best" AlphaFill ligand hit: No AlphaFill hits

No associated EC numbers

No evidence of orthology to BindingDB entries

Orthology Information

Ortholog Group (OrthoMCL): OG6_102392

Most Similar Human Ortholog: Q9Y4Z0

TM-align score: 0.73 | RMSD: 2.04

Seq Identity: 0.47 | Length: 104 / 126

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000130520 LSM4 homolog, U6 small nuclear RNA and mRNA degradation associated

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 3 6 4 12
disruptive 3 9 6 12
missense 3 8 4 10

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 4 12 6 12
disruptive 4 23 13 35
missense 4 19 11 22

PlasmoDB Total SNPs: 66

Non-coding: 61 | Synonymous: 3 | Nonsynonymous: 1 | Stop Codon: 1

Protein Information

Protein Length: 126 | Molecular Weight (kDa): 14.202

UniProt ID(s): Q8IIT3

PDB ID(s): None

Isoelectric Point: 10.71

Protein Domain Annotations:

Source Family ID Description
InterPro IPR001163 LSM domain, eukaryotic/archaea-type
InterPro IPR010920 LSM domain superfamily
InterPro IPR027141 Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3
InterPro IPR034101 Sm-like protein Lsm4
PFam PF01423 LSM domain, eukaryotic/archaea-type
Superfamily SSF50182 LSM domain superfamily

Associated Publications

PMID Title Authors DOI/Link
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
16267556 A protein interaction network of the malaria parasite Plasmodium falciparum. LaCount DJ, Vignali M, ..., Hughes RE 10.1038/nature04104
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
37762007 Yeast Lsm Pro-Apoptotic Mutants Show Defects in Autophagy Caraba B, Stirpe M, ..., Mazzoni C 10.3390/ijms241813708
29615482 Defining essential elements and genetic interactions of the yeast Lsm2-8 ring anddemonstration that essentiality of Lsm2-8 is bypassed via overexpression of U6snRNA or the U6 snRNP subunit Prp24 Roth AJ, Shuman S, Schwer B 10.1261/rna.066175.118
27543059 The decapping activator Edc3 and the Q/N-rich domain of Lsm4 function together toenhance mRNA stability and alter mRNA decay pathway dependence in Saccharomycescerevisiae Huch S, Muller M, ..., Nissan T 10.1242/bio.020487
29078371 Numerous interactions act redundantly to assemble a tunable size of P bodies inSaccharomyces cerevisiae Rao BS, Parker R 10.1073/pnas.1712396114
26582754 Protein localisation by electron microscopy reveals the architecture of the yeastspliceosomal B complex Rigo N, Sun C, ..., Luhrmann R 10.15252/embj.201592022