Q9Y6N9: Harmonin (USH1C)

Harmonin (USH1C) is a 552-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y6N9.

Gene
USH1C
Organism
Homo sapiens
Length
552 residues
Mean pLDDT
79.4
Model
AF-Q9Y6N9-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.4 (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 accurate37%
70 to 90Confident: backbone generally right46%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles (By similarity). As part of the intermicrovillar adhesion complex/IMAC plays a role in brush border differentiation, controlling microvilli organization and length. Probably plays a central regulatory role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the microvilli tips (PubMed:24725409, PubMed:26812018)

Subunit structure

Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5 (PubMed:24725409, PubMed:26812018, PubMed:32209652). Part of a complex composed of USH1C, USH1G and MYO7A (PubMed:21709241). Interacts with F-actin (By similarity). Interacts with USH2A (PubMed:16301216). Interacts with SLC4A7 (PubMed:16301216). Interacts (via…

Subcellular location

Cytoplasm, cytosol, Cytoplasm, cytoskeleton, Cell projection, microvillus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5XBFX-ray1.8 ÅB=428-552
7X2EX-ray1.85 ÅA=193-370
5MV8X-ray1.88 ÅB=428-552
3K1RX-ray2.3 ÅA=1-192
5MV9X-ray2.6 ÅB=428-552
5F3XX-ray2.65 ÅA/C=1-194
1X5NNMRA=201-301
2KBQNMRA=1-80
2KBRNMRA=1-80
2KBSNMRA=208-299
2LSRNMRA=1-80

More AlphaFold highlights

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