Q9BUN8: Derlin-1 (DERL1)

Derlin-1 (DERL1) is a 251-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BUN8.

Gene
DERL1
Organism
Homo sapiens
Length
251 residues
Mean pLDDT
80.0
Model
AF-Q9BUN8-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.0 (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 accurate39%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins (PubMed:15215856, PubMed:33658201). Forms homotetramers which encircle a large channel traversing the endoplasmic reticulum (ER) membrane (PubMed:33658201). This allows the retrotranslocation of misfolded proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome (PubMed:33658201). The channel has a lateral gate within the membrane which provides direct access to membrane proteins with no need to reenter the ER lumen first (PubMed:33658201). May mediate the interaction between VCP and the misfolded protein (PubMed:15215856). Also involved in…

Subunit structure

Homotetramer (PubMed:33658201). The four subunits of the tetramer are arranged in a twofold symmetry (PubMed:33658201). Forms heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts (via SHP-box motif) with VCP (PubMed:16186509, PubMed:16186510, PubMed:16289116, PubMed:16449189, PubMed:27714797). Interacts with AMFR, SELENOS, SEL1L, SELENOK…

Subcellular location

Endoplasmic reticulum membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5GLFX-ray2.25 ÅB/D/F/H=239-250
9LLKEM3.55 ÅU/V/W/X/Y/Z=1-251
7Y53EM3.61 ÅW/X/Y/Z=1-251
7Y4WEM3.67 ÅW/X/Y/Z=1-251
7CZBEM3.8 ÅA/B/C/D=1-251
7Y59EM4.51 ÅW/X/Y/Z=1-251

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