Q13769: THO complex subunit 5 (THOC5)

THO complex subunit 5 (THOC5) is a 683-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13769.

Gene
THOC5
Organism
Homo sapiens
Length
683 residues
Mean pLDDT
82.9
Model
AF-Q13769-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.9 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate45%
70 to 90Confident: backbone generally right40%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Plays a key structural role in the oligomerization of the THO-DDX39B complex (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825,…

Subunit structure

Component of the THO subcomplex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7 (PubMed:33191911, PubMed:37020021). The THO subcomplex interacts with DDX39B to form the THO-DDX39B complex which multimerizes into a 28-subunit tetrameric assembly (PubMed:33191911, PubMed:37020021). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B,…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7APKEM3.3 ÅE/M/e/m=1-683
7ZNLEM3.45 ÅE/M/e/m=1-683
7ZNKEM3.9 ÅE/M/e/m=1-683

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