Q9BSA9: Endosomal/lysosomal proton channel TMEM175 (TMEM175)

Endosomal/lysosomal proton channel TMEM175 (TMEM175) is a 504-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BSA9.

Gene
TMEM175
Organism
Homo sapiens
Length
504 residues
Mean pLDDT
81.8
Model
AF-Q9BSA9-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.8 (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 accurate45%
70 to 90Confident: backbone generally right37%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Proton-activated proton channel that catalyzes proton efflux from endosomes and lysosomes to maintain a steady-state pH (PubMed:35333573, PubMed:35750034, PubMed:37390818). Activated at low pH (under pH 4.6) by luminal side protons: selectively mediates lysosomal proton release from lysosomes, eliciting a proton leak that balances V-ATPase activity to maintain pH homeostasis (PubMed:35750034). Regulation of lumenal pH stability is required for autophagosome-lysosome fusion (PubMed:26317472, PubMed:32267231). Also acts as a potassium channel at higher pH, regulating potassium conductance in endosomes and lysosomes (PubMed:26317472, PubMed:28723891, PubMed:32228865, PubMed:32267231,…

Subunit structure

Homodimer (PubMed:28723891, PubMed:32228865, PubMed:35608336). Interacts with AKT (AKT1, AKT2 or AKT3); leading to formation of the lysoK(GF) complex, which activates the channel (PubMed:33505021). Interacts with LAMP1; inhibiting the proton channel activity of TMEM175 (PubMed:37390818). Interacts with LAMP2; inhibiting the proton channel activity of TMEM175 (PubMed:37390818)

Subcellular location

Endosome membrane, Lysosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7UNLEM2.45 ÅA/B=1-504
7UNMEM2.61 ÅA/B=1-504
6WC9EM2.64 ÅA/B=1-504
8DHMEM2.73 ÅA/B=1-504
9VSQEM2.74 ÅA/B=1-504
9VSREM2.92 ÅA/B=1-504
6WCAEM3.03 ÅA/B=1-504
6WCBEM3.17 ÅA/B=1-504
6W8NEM3.2 ÅA/B=1-504
6WCCEM3.24 ÅA/B=1-504
6W8OEM3.4 ÅA/B=1-504
8FY5EM3.4 ÅA/B=1-504
8FYFEM3.4 ÅA/B=1-504
9VSPEM3.4 ÅA/B=1-504
8VICEM3.48 ÅA/B=1-504
7LF6EM3.5 ÅA/B=1-504
8VIEEM3.52 ÅA/B=1-504
6W8PEM3.6 ÅA/B=1-504

More AlphaFold highlights

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