P35221: Catenin alpha-1 (CTNNA1)

Catenin alpha-1 (CTNNA1) is a 906-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35221.

Gene
CTNNA1
Organism
Homo sapiens
Length
906 residues
Mean pLDDT
82.9
Model
AF-P35221-F1 v6
Model created
1 Aug 2025
PDB structures
10

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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 accurate55%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties (PubMed:40983751). Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage…

Subunit structure

Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin (By similarity). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (PubMed:28051089). Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or…

Subcellular location

Cytoplasm, cytoskeleton, Cell junction, adherens junction, Cell membrane, Cell junction, Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6V2OX-ray1.27 ÅC=850-859
6V2PX-ray1.3 ÅC=850-859
9BL4X-ray1.75 ÅC=850-859
9BL3X-ray2.0 ÅC=850-859
9BL2X-ray2.1 ÅC=850-859
1H6GX-ray2.2 ÅA/B=377-632
4EHPX-ray2.66 ÅB=277-382
7UTJEM2.77 ÅG/H/I/K/L/Z=22-906
6UPVEM3.2 ÅL/M=1-906
4IGGX-ray3.66 ÅA/B=82-906

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