O43866: CD5 antigen-like (CD5L)

CD5 antigen-like (CD5L) is a 347-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43866.

Gene
CD5L
Organism
Homo sapiens
Length
347 residues
Mean pLDDT
85.9
Model
AF-O43866-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.9 (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 accurate55%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs with progression of obesity: participates in obesity-associated inflammation following recruitment of inflammatory macrophages into adipose…

Subunit structure

Interacts with FASN; the interaction is direct (By similarity). Interacts (via SRCR2 and SRCR3) with pentameric IgM (via Fc region); disulfide-linked (PubMed:24804991, PubMed:8034987). Interacts with HAVCR1/KIM-1; interaction with HAVCR1 expressed on the surface of injured kidney tubular epithelial cells promotes HAVCR1-mediated phagocytosis of intraluminal necrotic debris and contributes to…

Subcellular location

Secreted, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8WYREM3.39 ÅM=20-347
8WYSEM3.41 ÅM=20-347
8R83EM3.57 ÅN=20-347
8R84EM3.6 ÅN=20-347

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