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. Author manuscript; available in PMC: 2020 Jun 17.
Published in final edited form as: FEBS J. 2019 Dec 2;287(10):2000–2022. doi: 10.1111/febs.15133

Table 1.

The effect of APOL1 polymorphism on domain structures (related to α helices)

Domain Secondary Structure APOL1G0 APOL1G1 APOL1G2
Amino terminal signal peptide α helices Ala4-Leu6
Leu7-Val11
Met16-Phe20
Ala30-Ala32
Asn37-Ala56		 Glu2-Ser17
Gly31-Gln35
Asn37-Asp43
Asp46- Gly58		 Gly3-Met16
Val23-Asn37
Ser40- Thr44
Pore forming domain α helices Ser64-Ile68
Glu69-Lys76
Asn83-Ala99
Glu107-Gln134
Trp139-Leu141
Ser149-Val168
Asn176-Leu196
Gly202-Thr227
Lys232-Ala240		 Glu63-Lys76
Asn83-Ala101
Arg105-Met124
Lys127-Gln134
Phe140-Asp163
Val178-Leu196
Leu205-Thr227
Lys232-Gln239		 Glu63-Lys76
Thr81-Ala99
Asp109-Met124
Lys132-Gln135
Phe140-Ala162 Val165-Val168 Val178-Leu196
Gly203-Asp229
Membrane addressing domain α helices Lys232-Ala240
His241-Leu243
Val244-Glu260
Ser267-Ile283
Pro297-Ser300
Ser302-Thr307		 Asp242-Gly259
Leu266-Asp282		 Trp234-Glu260
Asn264-Arg284
C-terminal region α helices Ser314-Arg331
Val338-His360
Ser365-Ile391
Ser302-Thr307		 Pro304-Val321
Pro324-Asp337
Pro340-His360
Ser365-Leu392		 Glu308-Met329
Val338-Lys357
Glu369-Ile389