Q7Z3J2: VPS35 endosomal protein-sorting factor-like (VPS35L)

VPS35 endosomal protein-sorting factor-like (VPS35L) is a 963-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7Z3J2.

Gene
VPS35L
Organism
Homo sapiens
Length
963 residues
Mean pLDDT
84.8
Model
AF-Q7Z3J2-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate64%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Acts as a component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:28892079). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes (PubMed:28892079). In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply…

Subunit structure

Component of the heterotrimeric retriever complex formed by VPS26C, VPS29 and VPS35L (PubMed:28892079). Interacts with VPS29 (PubMed:31712251). Interacts with COMMD1, CCDC93 and CCDC22; associates with the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22 and CCDC93 (PubMed:25355947, PubMed:28892079). Interacts with…

Subcellular location

Membrane, Endosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8ESEX-ray1.35 ÅX=16-38
8SYNEM2.94 ÅA=1-963
8SYOEM2.94 ÅA=1-963
8SYMEM3.2 ÅA=1-963
9AU7EM3.4 ÅA=1-963
8P0VEM6.5 ÅO=1-963
8P0XEM7.5 ÅO=1-963

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