P08575: Receptor-type tyrosine-protein phosphatase C (PTPRC)

Receptor-type tyrosine-protein phosphatase C (PTPRC) is a 1306-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08575.

Gene
PTPRC
Organism
Homo sapiens
Length
1306 residues
Mean pLDDT
76.1
Model
AF-P08575-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.1 (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 accurate49%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor (PubMed:35767951). Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). Interacts with CLEC10A at antigen presenting cell-T cell contact; CLEC10A on immature dendritic cells recognizes Tn antigen-carrying PTPRC/CD45 receptor on effector T cells and modulates T cell activation threshold to limit autoreactivity

Subunit structure

Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1 (PubMed:11909961). Interacts with DPP4; the interaction is enhanced in an interleukin-12-dependent manner in activated lymphocytes (PubMed:12676959). Interacts with CD53; this interaction stabilizes PTPRC on the membrane and is required for optimal phosphatase activity (PubMed:35767951)

Subcellular location

Cell membrane, Membrane raft, Synapse

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5FN7X-ray2.3 ÅA/B=225-394
1YGRX-ray2.9 ÅA/B=624-1233
1YGUX-ray2.9 ÅA/B=624-1233
5FMVX-ray2.9 ÅA/B=225-573
5FN6X-ray3.3 ÅA=225-481
8VSEEM3.8 ÅA/B=26-576

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