P28799: Progranulin (GRN)

Progranulin (GRN) is a 593-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P28799.

Gene
GRN
Organism
Homo sapiens
Length
593 residues
Mean pLDDT
77.0
Model
AF-P28799-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.0 (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 accurate21%
70 to 90Confident: backbone generally right58%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (PubMed:12526812, PubMed:18378771, PubMed:28073925, PubMed:28453791, PubMed:28541286). Regulates protein trafficking to lysosomes, and also the activity of lysosomal enzymes (PubMed:28453791, PubMed:28541286). Also facilitates the acidification of lysosomes, causing degradation of mature CTSD by CTSB (PubMed:28073925). In addition, functions as a wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity).…

Subunit structure

Progranulin is secreted as a homodimer (PubMed:23364791). Interacts with SLPI; interaction protects progranulin from proteolysis (PubMed:12526812). Interacts (via region corresponding to granulin-7 peptide) with CTSD; stabilizes CTSD and increases its proteolytic activity (PubMed:28453791). Interacts (via region corresponding to granulin-7 peptide) with SORT1; this interaction mediates…

Subcellular location

Secreted, Lysosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8T8RX-ray2.87 ÅB=578-593
8T8SX-ray2.99 ÅC/D=578-593
1G26NMRA=281-311
2JYENMRA=281-337
2JYTNMRA=364-417
2JYUNMRA=364-417
2JYVNMRA=123-179
6NUGNMRA=284-307

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