Q9H6L5: Reticulophagy regulator 1 (RETREG1)

Reticulophagy regulator 1 (RETREG1) is a 497-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H6L5.

Gene
RETREG1
Organism
Homo sapiens
Length
497 residues
Mean pLDDT
59.7
Model
AF-Q9H6L5-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.7 (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 accurate0%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution41%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Endoplasmic reticulum (ER)-anchored autophagy regulator which mediates ER delivery into lysosomes through sequestration into autophagosomes (PubMed:26040720, PubMed:31930741, PubMed:34338405). Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins (PubMed:26040720, PubMed:31930741, PubMed:34338405). Active under basal conditions (PubMed:34338405). Required for collagen quality control in a LIR motif-dependent manner (By similarity). Required for long-term survival of nociceptive and autonomic ganglion neurons (PubMed:19838196, PubMed:26040720)

Subunit structure

Homooligomer; oligomerization is enhanced following endoplasmic reticulum stress and is mediated by the reticulon homology domain (PubMed:31930741). Interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and GABARAPL2 (PubMed:26040720, PubMed:34338405, PubMed:34854256). Shows higher affinity for GABARAPL1 than for MAP1LC3A or MAP1LC3B (PubMed:34854256)

Subcellular location

Golgi apparatus, cis-Golgi network membrane, Endoplasmic reticulum membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7BRQX-ray1.4 ÅA=450-468
7FB5X-ray2.84 ÅB=451-476

More AlphaFold highlights

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