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1.A.71 The Brain Acid-soluble Protein Channel (BASP1 Channel) Family

BASP1 (also known as CAP-23 and NAP-22) is a brain abundant myristoylated protein localized at the inner surface of the presynaptic plasma membrane. Emerging evidence suggests that BASP1 is critically involved in various cellular processes, in particular, in the accumulation of phosphatidylinositol-4,5-diphosphate (PIP(2)) in lipid raft microdomains. Ostroumova et al. (2011) showed that BASP1 forms heterogeneously-sized oligomers and higher aggregates with an outward similarity to oligomers and protofibrils of amyloid proteins. BASP1 induces single channel currents across negatively-charged planar lipid bilayers. In this respect, BASP1 channels are similar to amyloid protein channels. BASP1 channels exhibit multiple conductance levels, in the range 10-3000 pS, with the most frequently observed conductance state of approximately 50 pS. The channels demonstrate a linear current-voltage relationship with voltage-independent kinetics of opening and closing. Their K+ to Cl- permeability ratio is approximately 14, showing that BASP1 channels are cation-selective. The ion channel activity of BASP1 is in accordance with the pore-like structure of BASP1 oligomers observed by electron microscopy on a lipid monolayer. Neuronal protein GAP-43, which is functionally related to BASP1 and also forms oligomers, elicited no ion channel currents under the conditions used.

The generalized reaction catalyzed by BASP1 is:

ions (in) %u21CC ions(out) (cation-selective)

References associated with 1.A.71 family:

Holahan, M.R. (2017). A Shift from a Pivotal to Supporting Role for the Growth-Associated Protein (GAP-43) in the Coordination of Axonal Structural and Functional Plasticity. Front Cell Neurosci 11: 266. 28912688
Ostroumova, O.S., L.V. Schagina, M.I. Mosevitsky, and V.V. Zakharov. (2011). Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers. FEBS J. 278: 461-469. 21156029