##gff-version 3 Q00169 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2HJ54 Q00169 UniProtKB Chain 2 270 . . . ID=PRO_0000191639;Note=Phosphatidylinositol transfer protein alpha isoform Q00169 UniProtKB Region 250 270 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q00169 UniProtKB Binding site 58 58 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Binding site 60 60 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Binding site 85 85 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Binding site 89 89 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Binding site 96 96 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Binding site 194 194 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Modified residue 215 215 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q00169 UniProtKB Mutagenesis 58 58 . . . Note=Reduced phosphatidylinositol and phosphatidylcholine transfer activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 58 58 . . . Note=Complete loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 58 58 . . . Note=Reduced phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 60 60 . . . Note=Complete loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 85 85 . . . Note=Reduced phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 85 85 . . . Note=Reduced phosphatidylinositol and phosphatidylcholine transfer activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 89 89 . . . Note=Significant loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. N->F%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 94 94 . . . Note=No effect on phosphatidylinositol transfer activity. Resistant to inhibition by N-ethylmaleimide. C->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18636990;Dbxref=PMID:18636990 Q00169 UniProtKB Mutagenesis 102 102 . . . Note=Reduced phosphatidylinositol and phosphatidylcholine transfer activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14962392;Dbxref=PMID:14962392 Q00169 UniProtKB Mutagenesis 187 187 . . . Note=No effect on phosphatidylinositol transfer activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18636990;Dbxref=PMID:18636990 Q00169 UniProtKB Mutagenesis 202 203 . . . Note=Significant loss of phosphatidylinositol and phosphatidylcholine transfer activity. WW->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14962392,ECO:0000269|PubMed:18636990;Dbxref=PMID:14962392,PMID:18636990 Q00169 UniProtKB Sequence conflict 45 45 . . . Note=N->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q00169 UniProtKB Beta strand 3 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 15 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 38 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 54 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 70 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 81 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 93 99 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 106 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Turn 123 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 130 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 137 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 177 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Beta strand 190 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 206 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 232 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5 Q00169 UniProtKB Helix 240 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UW5