PF3D7_1438900 thioredoxin peroxidase 1 [Plasmodium falciparum 3D7] - Gene

Summary

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Gene symbol: PF3D7_1438900
Gene description: thioredoxin peroxidase 1
Locus tag: PF3D7_1438900
See related: PlasmoDB:PF3D7_1438900; VEuPathDB:PF3D7_1438900
Gene type: protein coding
RNA name: thioredoxin peroxidase 1
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_1438900 in Genome Data Viewer

Location:: chromosome: 14

Exon count:: 1

Sequence:: Chromosome: 14; NC_037283.1 (1575984..1576571)

Chromosome 14 - NC_037283.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_037283.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Gene expression of peroxiredoxin genes, pf1-cys-prx and pftpx-1, during erythrocytic stage is regulated by interactions of unique cis-elements and trans-acting factors and chromatin modifications.
Title: 5' sequence- and chromatin modification-dependent gene expression in Plasmodium falciparum erythrocytic stage.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

C14M53 (e-PCR)
- UniSTS:108936

Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by GeneDB

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables antioxidant activity	IDA Inferred from Direct Assay more info	PubMed
enables antioxidant activity	ISO Inferred from Sequence Orthology more info	PubMed
enables double-stranded DNA binding	ISO Inferred from Sequence Orthology more info	PubMed
enables double-stranded RNA binding	ISO Inferred from Sequence Orthology more info	PubMed
enables lncRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables thioredoxin peroxidase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within DNA protection	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within protein folding	ISO Inferred from Sequence Orthology more info	PubMed
acts_upstream_of_or_within response to heat	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in Maurer's cleft	RCA inferred from Reviewed Computational Analysis more info	PubMed
located_in cell surface	ISO Inferred from Sequence Orthology more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleolus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: thioredoxin peroxidase 1

XP_001348542.1

EC 1.11.1.15

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

NC_037283.1 Reference assembly

Range

1575984..1576571

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_001348506.1 → XP_001348542.1 thioredoxin peroxidase 1 [Plasmodium falciparum 3D7]

See identical proteins and their annotated locations for XP_001348542.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A024V058, A0A024VZ28, A0A024WGD8, A0A024WZM5, A0A0L1I9G3, A0A0L7K644, A0A0L7M1G7, Q8IL80, Q9N699, W4IA13, W4IXF8, W7F7C6, W7FPU2, W7JQN9, W7K747

Conserved Domains (1) summary

cd03015
Location:5 → 177

PRX_Typ2cys; Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. ...