ID  P58195;
PN  Phospholipid scramblase 1;
GN  Plscr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}. Cell membrane {ECO:0000250|UniProtKB:O15162}; Lipid-anchor {ECO:0000250|UniProtKB:O15162}; Cytoplasmic side. Nucleus {ECO:0000250|UniProtKB:O15162}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:O15162}.
DR  UNIPROT: P58195;
DR  Pfam: PF03803;
DE  Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific distribution of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (By similarity). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (By similarity). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (By similarity). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:O15162, ECO:0000250|UniProtKB:Q9JJ00}.
DE  Reference Proteome: Yes;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005887;
GO  GO:0045121;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0042609;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0019899;
GO  GO:0005154;
GO  GO:0032791;
GO  GO:0000287;
GO  GO:0045340;
GO  GO:0004518;
GO  GO:0017128;
GO  GO:0017124;
GO  GO:0001618;
GO  GO:0008270;
GO  GO:0006953;
GO  GO:0006915;
GO  GO:0071345;
GO  GO:0071222;
GO  GO:0051607;
GO  GO:0006955;
GO  GO:0097193;
GO  GO:0030099;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0045071;
GO  GO:0006659;
GO  GO:0070782;
GO  GO:0015914;
GO  GO:0017121;
GO  GO:0043065;
GO  GO:1905820;
GO  GO:2000373;
GO  GO:0010628;
GO  GO:0045089;
GO  GO:1902231;
GO  GO:0045944;
GO  GO:0060368;
GO  GO:0033003;
GO  GO:0035455;
GO  GO:0035456;
GO  GO:0010288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDP
SQ  SGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAV
SQ  EDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEK
SQ  RQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFM
SQ  FFERTGNEEQRSGVW
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