P19334: Transient receptor potential protein (trp)

Transient receptor potential protein (trp) is a 1275-residue protein from Drosophila melanogaster. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19334.

Gene
trp
Organism
Drosophila melanogaster
Length
1275 residues
Mean pLDDT
67.9
Model
AF-P19334-F1 v6
Model created
1 Aug 2025
PDB structures
3

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 67.9 (low 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 accurate25%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Ca(2+) influx may then feed back and inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in the light response, though it is unclear whether as heteromultimers or as distinct units, and are activated by fatty acids and metabolic stress. Also required for olfactory adaptation and may be involved in olfactory system development

Subunit structure

The C-terminus interacts with a PDZ domain of inaD to form the core of the inaD signaling complex. Other members of the complex include norpA (PLC), inaC (PKC), and possibly trpl, ninaC, Fkbp59, calmodulin and rhodopsin. Forms homomultimers and heteromultimers with trpl. Interaction with trpl is mediated in part by the N-terminal region and the transmembrane domains. Also interacts, though to a…

Subcellular location

Cell membrane, Cell projection, rhabdomere membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5F67X-ray1.76 ÅC/D=1259-1275
7CQVX-ray1.78 ÅB=783-862
7CQHX-ray2.15 ÅA=899-940

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.