APOC3

Chr 11q23.3

apolipoprotein C3

Aliases:: Apo-CIII, ApoC-III, APOCIII, Apo-C3, ApoC-3
MANE:: ENST00000227667.8

OMIM: 107720 ↗NCBI: 345 ↗Ensembl ↗

Annotations refreshed 9 hours ago.

Predicted protein structure

AlphaFold predicted structure

APOC3 · P02656

v62025-08-01

Predicted Aligned Error matrix for APOC3 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

67.6/ 100

Low

99 residues

Confidence breakdown

Very high(≥ 90)0%
Confident(70–90)33%
Low(50–70)64%
Very low(< 50)3%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Moderate Evidence (Amber)

Hereditary systemic amyloidosis
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Periodic fever syndromes
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Familial hypercholesterolaemia

Disease associations (Open Targets)

apolipoprotein c-III deficiency
0.61
hypertriglyceridemia
0.55
coronary artery disorder
0.53
familial chylomicronemia syndrome
0.51
Hypercholesterolemia
0.43
cardiovascular disorder
0.41
cholesterol-ester transfer protein deficiency
0.41
metabolic disease
0.40
diabetes mellitus
0.39
hyperalphalipoproteinemia
0.37

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Apolipoprotein C-III

Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013)