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protein

Amine oxidase [copper-containing] 3

AOC3
protein:Q16853disease:adad:direction:up

Gene

AOC3

Organism

Homo sapiens(9606)

Length

763 aa

Mass

84,622 Da

AI summarysource-grounded · cited inline
claude-haiku-4-5-20251001

AOC3 (amine oxidase [copper-containing] 3) is a copper-dependent enzyme that catalyzes the oxidative deamination of primary amines, particularly methylamine and benzylamine, generating aldehydes, hydrogen peroxide, and ammonia (UniProt: Q16853). Beyond its enzymatic role, AOC3 functions as a cell adhesion protein at endothelial cell surfaces, facilitating lymphocyte extravasation and recirculation through interaction with peripheral lymph node vascular endothelial cells.

AOC3 is expressed on endothelial cells and participates in immune cell trafficking and vascular biology. UniProt records indicate no annotated disease associations in standard curated databases, though the protein's involvement in vascular and immune processes suggests potential relevance to conditions affecting these systems (UniProt: Q16853).

In Alzheimer's Disease, AOC3 shows increased abundance in post-mortem AD brain tissue compared to age-matched controls, with a mean log2 fold-change of 1.14 across examined subcellular fractions (Chaparral AD proteomics). This upregulation may reflect altered amine metabolism or vascular inflammatory responses in the AD brain, though the functional significance of this elevation remains to be determined.

Generated from the curated entity record below. May contain errors — verify against source links.

Proteomics Evidence · AD

↑ Up in AD

P3

not detected

P2

not detected

S2

not detected

S3

+1.136

Mean log₂FC across detected fractions: +1.1355 (1 of 4 fractions detected)

Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.

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Function

Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076, PubMed:24304424, PubMed:9653080). Has a preference for the primary monoamines methylamine and benzylamine (PubMed:19588076, PubMed:9653080). Could also act on 2-phenylethylamine but much less efficiently (PubMed:19588076). At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion (PubMed:9254657, PubMed:9653080)

Has no semicarbazide-sensitive amine oxidase (SSAO) activity

Sources

Last updated 5/8/2026, 6:32:39 AM