Annexin A11 (ANXA11)

Annexin A11 is a multi-domain, cytosolic, calcium-dependent phospholipid-binding protein that belongs to the annexin family[2][4][5]. It has a unique, long disordered N-terminal domain that mediates specific protein-protein and protein-RNA interactions and a conserved C-terminal core with four annexin repeats that bind calcium and phospholipids[1][2][3]. Annexin A11 participates in membrane trafficking, cytokinesis, apoptosis, and is implicated in the formation and tethering of membraneless RNA granules in neurons[1]. Its interactions include binding to S100A6 (calcyclin), PDCD6/ALG-2, and other S100 proteins in a calcium-dependent manner[1][2][4]. Mutations in Annexin A11 have been linked to ALS, with disease-associated variants disrupting its normal phase separation functions in neurons[1]. Alterations in expression or mutation also associate with cancers and autoimmune diseases, indicating a role in cell proliferation, survival, and immune recognition[2][4].

Other names

Annexin A11ANXA11ANX11CAP-5056 kDa autoantigenAnnexin XIAnnexin-11Calcyclin-associated annexin 50ALS23CAP50IBMWMAepididymis secretory sperm binding protein

Not established for specific drugs; mechanisms would potentially include modulation of membrane interactions, calcium binding interference, and protein-protein/RNA binding (no approved targeted drugs as of now)