P51654: Glypican-3 (GPC3)

Glypican-3 (GPC3) is a 580-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51654.

Gene
GPC3
Organism
Homo sapiens
Length
580 residues
Mean pLDDT
75.1
Model
AF-P51654-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.1 (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 accurate52%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions28%

What pLDDT means and how to read it

Function

Cell surface proteoglycan (PubMed:14610063). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (PubMed:16227623, PubMed:24496449). Positively regulates the non-canonical Wnt signaling pathway (By similarity). Binds to CD81 which…

Subunit structure

Heterodimer; disulfide-linked (PubMed:14610063). Cleavage by a furin-like convertase results in production of alpha and beta chains which form a disulfide-linked heterodimer (PubMed:14610063). Interacts with DPP4 (PubMed:17549790). Interacts with FGF2 (By similarity). Interacts with WNT5A (PubMed:14610063). Also interacts with WNT3A and WNT7B (PubMed:16227623). Interacts with hedgehog protein…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7ZAWX-ray2.58 ÅA=32-483
9NTQEM4.04 ÅA=35-477
7ZA1X-ray4.1 ÅA/B/C/D=32-483
9NTTEM7.45 ÅA=57-477

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