##gff-version 3 Q9NTI2 UniProtKB Chain 1 1188 . . . ID=PRO_0000046362;Note=Phospholipid-transporting ATPase IB Q9NTI2 UniProtKB Topological domain 1 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 116 119 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 141 316 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 338 364 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 365 385 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 386 887 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 888 908 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 909 910 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 911 931 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 932 959 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 960 980 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 981 997 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 998 1018 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 1019 1028 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 1029 1049 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 1050 1063 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Transmembrane 1064 1084 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NTI2 UniProtKB Topological domain 1085 1188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NTI2 UniProtKB Region 1162 1188 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NTI2 UniProtKB Active site 428 428 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 428 428 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 428 428 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 429 429 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 430 430 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 430 430 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 528 528 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 569 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 592 592 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 625 625 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 705 705 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 706 706 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 707 707 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 795 795 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 801 801 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04191 Q9NTI2 UniProtKB Binding site 821 821 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 824 824 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 825 825 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Q0 Q9NTI2 UniProtKB Binding site 825 825 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NB49 Q9NTI2 UniProtKB Site 371 371 . . . Note=Involved in the recognition of the lipid substrate on the exoplasmic side;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:C7EXK4 Q9NTI2 UniProtKB Site 376 376 . . . Note=Involved in the release of the transported lipid into the cytosolic leaflet;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:C7EXK4 Q9NTI2 UniProtKB Modified residue 45 45 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P98200 Q9NTI2 UniProtKB Alternative sequence 1 40 . . . ID=VSP_059718;Note=In isoform 1 and isoform 2. Missing Q9NTI2 UniProtKB Alternative sequence 555 568 . . . ID=VSP_059719;Note=In isoform 2. MGQEQTFGILNVLE->VSNMRVHISDHLLL Q9NTI2 UniProtKB Alternative sequence 569 1188 . . . ID=VSP_059720;Note=In isoform 2. Missing Q9NTI2 UniProtKB Natural variant 376 376 . . . ID=VAR_069928;Note=In CAMRQ4%3B abolishes ATPase activity. No effect on interaction with TMEM30A. I->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22892528,ECO:0000269|PubMed:31397519;Dbxref=dbSNP:rs546968533,PMID:22892528,PMID:31397519 Q9NTI2 UniProtKB Natural variant 429 429 . . . ID=VAR_084371;Note=In CAMRQ4%3B uncertain significance%3B abolishes ATPase activity. No effect on interaction with TMEM30A. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30012219,ECO:0000269|PubMed:31397519;Dbxref=dbSNP:rs1057522489,PMID:30012219,PMID:31397519 Q9NTI2 UniProtKB Natural variant 429 429 . . . ID=VAR_084370;Note=In CAMRQ4%3B uncertain significance%3B abolishes ATPase activity and results in protein misfolding and proteasomal degradation. No effect on interaction with TMEM30A. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27679995,ECO:0000269|PubMed:31397519;Dbxref=PMID:27679995,PMID:31397519 Q9NTI2 UniProtKB Natural variant 544 544 . . . ID=VAR_084372;Note=In CAMRQ4%3B uncertain significance%3B results in protein misfolding and proteasomal degradation. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27679995,ECO:0000269|PubMed:31397519;Dbxref=PMID:27679995,PMID:31397519 Q9NTI2 UniProtKB Natural variant 581 1188 . . . ID=VAR_084373;Note=In CAMRQ4%3B uncertain significance. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29531481;Dbxref=dbSNP:rs755133567,PMID:29531481 Q9NTI2 UniProtKB Natural variant 586 1188 . . . ID=VAR_084374;Note=In CAMRQ4%3B uncertain significance. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30012219;Dbxref=PMID:30012219 Q9NTI2 UniProtKB Natural variant 625 625 . . . ID=VAR_084375;Note=In CAMRQ4%3B uncertain significance%3B results in protein misfolding and proteasomal degradation. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27679995,ECO:0000269|PubMed:31397519;Dbxref=dbSNP:rs764911379,PMID:27679995,PMID:31397519 Q9NTI2 UniProtKB Natural variant 702 702 . . . ID=VAR_084376;Note=In CAMRQ4%3B uncertain significance%3B results in protein misfolding and proteasomal degradation. W->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30012219,ECO:0000269|PubMed:31397519;Dbxref=PMID:30012219,PMID:31397519 Q9NTI2 UniProtKB Natural variant 917 917 . . . ID=VAR_084377;Note=In CAMRQ4%3B uncertain significance. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29531481;Dbxref=dbSNP:rs1593410369,PMID:29531481 Q9NTI2 UniProtKB Natural variant 1069 1069 . . . ID=VAR_055543;Note=A->T;Dbxref=dbSNP:rs2296242 Q9NTI2 UniProtKB Mutagenesis 107 107 . . . Note=No effect on flippase activity toward phosphatidylserine. Like the wild type%2C it is unable to translocate phosphatidylcholine. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34403372;Dbxref=PMID:34403372 Q9NTI2 UniProtKB Mutagenesis 107 107 . . . Note=Reduced flippase activity toward phosphatidylserine. Like the wild type%2C it is unable to translocate phosphatidylcholine. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34403372;Dbxref=PMID:34403372 Q9NTI2 UniProtKB Mutagenesis 429 429 . . . Note=Abolishes ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31397519;Dbxref=PMID:31397519 Q9NTI2 UniProtKB Mutagenesis 429 429 . . . Note=Abolishes ATPase activity. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31397519;Dbxref=PMID:31397519 Q9NTI2 UniProtKB Mutagenesis 429 429 . . . Note=Abolishes ATPase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31397519;Dbxref=PMID:31397519 Q9NTI2 UniProtKB Sequence conflict 573 573 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305