AFM
Domain
The second albumin domain forms a deep binding pocket that contains palmitoleic acid (in vitro) (PubMed:29153507). Palmitoleic acid is most likely not the physiological ligand. Instead, this pocket may accomodate the covalently bound lipid moiety of Wnt family members (Probable).
Function
Functions as a carrier for hydrophobic molecules in body fluids (Probable). Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds vitamin E (PubMed:12463752, PubMed:15952736). May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient (PubMed:15952736). May be involved in the transport of vitamin E across the blood-brain barrier (PubMed:19046407).
Post-translational modifications
N-glycosylated; more than 90% of the glycans are sialylated.
Sequence Similarities
Belongs to the ALB/AFP/VDB family.
Tissue Specificity
High level detected in plasma but also in extravascular fluids such as follicular and cerebrospinal fluids (at protein level).
Cellular localization
- Secreted
Alternative names
ALB2, ALBA, AFM, Afamin, Alpha-albumin, Alpha-Alb