O75762: Transient receptor potential cation channel subfamily A member 1 (TRPA1)

Transient receptor potential cation channel subfamily A member 1 (TRPA1) is a 1119-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75762.

Gene
TRPA1
Organism
Homo sapiens
Length
1119 residues
Mean pLDDT
81.9
Model
AF-O75762-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.9 (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 accurate36%
70 to 90Confident: backbone generally right50%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Ligand-activated Ca(2+)-permeable, nonselective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (PubMed:17259981, PubMed:21195050, PubMed:21873995, PubMed:23199233, PubMed:25389312, PubMed:33152265). Has a relatively high Ca(2+) selectivity, with a preference for divalent over monovalent cations (Ca(2+) > Ba(2+) > Mg(2+) > NH4(+) > Li(+) > K(+)), the influx of cation into the cytoplasm leads to membrane depolarization (PubMed:19202543, PubMed:21195050). Has a central role in the pain response to endogenous inflammatory mediators, such as bradykinin and to a diverse array of irritants.…

Subunit structure

Homotetramer (PubMed:25389312, PubMed:25855297, PubMed:31866091, PubMed:32641835). Interacts with TMEM100 (By similarity). Interacts with EGLN1 (By similarity). Interacts with the scorpion wasabi receptor toxin at the same site that electrophiles but in a non-covalent manner (PubMed:31447178)

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
6HC8X-ray1.9 ÅE=313-339
6V9VEM2.6 ÅA/B/C/D=1-1119
7OR0EM2.64 ÅA/B/C/D=1-1119
7OR1EM2.64 ÅA/B/C/D=1-1119
9MOEEM2.7 ÅA/B/D/E=2-1119
6PQQEM2.81 ÅA/B/C/D=2-1119
6PQOEM2.88 ÅA/B/C/D=2-1119
6X2JEM3.0 ÅA/B/C/D=448-1078
7JUPEM3.05 ÅA/B/C/D=448-1078
6PQPEM3.06 ÅA/B/C/D=2-1119
6V9WEM3.1 ÅA/B/C/D=1-1119
9M8SEM3.1 ÅA/B/C/D=1-1119
6V9XEM3.3 ÅA/B/C/D=1-1119
6V9YEM3.6 ÅA/B/C/D=1-1119
6WJ5EM3.6 ÅA/B/C/D=448-1078
9M8NEM3.81 ÅA/B/C/D=1-1119
3J9PEM4.24 ÅA/B/C/D=2-1119

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