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1.C.127.1.1
Human Apolipooprotein A1, APOL1, a tripanolytic factor of 398 aas and 4 possible α-helical TMSs in a 1 + 2 + 1 TMS arrangement. Pore-formation has been demonstrated in planar bilayer membranes. APOL1 inserts into such bilayers at acidic pH to form pH-gated non-selective cation channels that open upon pH neutralization. This corresponds to the pH changes encountered during endocytic-recycling, suggesting that APOL1 forms a cytotoxic cation channel in the parasite plasma membrane. Pore-formation is blocked by the serum resistance-associated VSG protein, SRA. See family discussion for a published description of this protein (Thomson and Finkelstein 2015). APOL1 risk variants induce opening of the mitochondrial permeability transition pore (Carney 2019). Cation channel conductance and pH gating of the innate immunity factor APOL1 is governed by pore lining residues in the C-terminal domain (Schaub et al. 2020). Two residues in the C-terminal domain (CTD), tyrosine-351 and glutamate-355 influence pH gating properties, and a single residue, aspartate-348, determines both cation selectivity and pH gating. Thus, the predicted transmembrane region closest to the APOL1 C-terminus is the pore-lining segment of this channel-forming protein (Schaub et al. 2020).

Accession Number:O14791
Protein Name:Apolipoprotein L1
Length:398
Molecular Weight:43974.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Secreted1
Substrate

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FASTA formatted sequence
1:	MEGAALLRVS VLCIWMSALF LGVGVRAEEA GARVQQNVPS GTDTGDPQSK PLGDWAAGTM 
61:	DPESSIFIED AIKYFKEKVS TQNLLLLLTD NEAWNGFVAA AELPRNEADE LRKALDNLAR 
121:	QMIMKDKNWH DKGQQYRNWF LKEFPRLKSE LEDNIRRLRA LADGVQKVHK GTTIANVVSG 
181:	SLSISSGILT LVGMGLAPFT EGGSLVLLEP GMELGITAAL TGITSSTMDY GKKWWTQAQA 
241:	HDLVIKSLDK LKEVREFLGE NISNFLSLAG NTYQLTRGIG KDIRALRRAR ANLQSVPHAS 
301:	ASRPRVTEPI SAESGEQVER VNEPSILEMS RGVKLTDVAP VSFFLVLDVV YLVYESKHLH 
361:	EGAKSETAEE LKKVAQELEE KLNILNNNYK ILQADQEL