O43707: Alpha-actinin-4 (ACTN4)

Alpha-actinin-4 (ACTN4) is a 911-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43707.

Gene
ACTN4
Organism
Homo sapiens
Length
911 residues
Mean pLDDT
84.1
Model
AF-O43707-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.1 (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 accurate47%
70 to 90Confident: backbone generally right41%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA…

Subunit structure

Homodimer; antiparallel. Binds TRIM3 at the N-terminus (PubMed:15772161). Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation (By similarity). Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Component of the…

Subcellular location

Nucleus, Cytoplasm, Cell junction, Cytoplasm, cytoskeleton, stress fiber, Cytoplasm, perinuclear region

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6OA6X-ray1.37 ÅA=47-271
6O31X-ray1.51 ÅA=47-271
1YDIX-ray1.8 ÅB=734-757
2R0OX-ray2.2 ÅA/B=47-271
1WLXNMRA=519-645

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