Q9H492: Microtubule-associated protein 1 light chain 3 alpha (MAP1LC3A)

Microtubule-associated protein 1 light chain 3 alpha (MAP1LC3A) is a 121-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H492.

Gene
MAP1LC3A
Organism
Homo sapiens
Length
121 residues
Mean pLDDT
91.3
Model
AF-Q9H492-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.3 (very high 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 accurate78%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20713600). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538)

Subunit structure

3 different light chains, LC1 (a cleavage product of MAP1B), LC2 (a cleavage product of MAP1A) and LC3 (produced by one of the MAP1LC3 genes), can associate with the MAP1A or MAP1B heavy chains (By similarity). Interacts with TP53INP1 and TP53INP2 (PubMed:19056683, PubMed:22470510). Directly interacts with SQSTM1; this interaction leads to MAP1LC3A recruitment to inclusion bodies containing…

Subcellular location

Cytoplasmic vesicle, autophagosome membrane, Endomembrane system, Cytoplasm, cytoskeleton

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7RA0X-ray1.36 ÅA=1-120
6TBEX-ray1.67 ÅA=4-119
7R9ZX-ray1.72 ÅA=1-120
7R9WX-ray1.75 ÅA=1-120
3WANX-ray1.77 ÅA/B=2-121
4ZDVX-ray1.8 ÅA=2-120
8T36X-ray1.85 ÅA=1-121
8T35X-ray1.9 ÅA/B=1-121
3WALX-ray2.0 ÅA=2-121
8T2LX-ray2.24 ÅA/B=1-121
5CX3X-ray2.3 ÅA/B/C/D=1-121
8T4TX-ray2.36 ÅA/B=1-121
5DPRX-ray2.5 ÅA/B/C/D=3-121
3ECIX-ray2.65 ÅA/B=1-121

More AlphaFold highlights

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