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Human phospholipid scramblase 4 (hPLSCR4), an isoform of the scramblase family, is a type II single-pass transmembrane protein whose function remains unknown. To understand its role, recombinant hPLSCR4 was obtained by cloning the ORF into a pET28 a(+) vector and overexpressed in  Escherichia coli . Functional assay showed that Ca 2+ , Mg 2+ , and Zn 2+  activate hPLSCR4 and mediate scrambling activity independent of the phospholipid head group. Far-UV-CD and fluorescence spectroscopy revealed that Ca 2+  and Mg 2+  binding induces conformation change in hPLSCR4, exposing hydrophobic patches of the protein, and Ca 2+  has more affinity than Mg 2+  and Zn 2+ . Stains-all studies further confirm that hPLSCR4 is a Ca 2+ -binding protein. Point mutation (Asp 290 →Ala) in hPLSCR4 decreased the Ca 2+ -binding affinity as well as Tb 3+  luminescence, suggesting residues of the predicted Ca 2+ -binding motif are involved in Ca 2+  binding. Functional reconstitution with (Asp 290 →Ala) mutant led to ∼50% and ∼40% decrease in scramblase activity in the presence of Ca 2+  and Mg 2+ , respectively.

Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)