Protein: Phospholipid scramblase 1 (PL scramblase 1) (Ca(2+)-dependent phospholipid scramblase 1) (Erythrocyte phospholipid scramblase) (Mg(2+)-dependent nuclease) (EC 3.1.-.-) (MmTRA1b) (O15162)
Organism: Homo sapiens (Human)
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement 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. 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. Negatively regulates FcR-mediated phagocytosis in differentiated macrophages. May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. Acts as an attachment receptor for HCV.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:37438530}; Single-pass type II membrane protein {ECO:0000269|PubMed:26745724}. Cell membrane {ECO:0000269|PubMed:12564925}; Lipid-anchor {ECO:0000305|PubMed:12564925}; Cytoplasmic side. Nucleus {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:16091359, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:35595813}. Cytoplasm {ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:29352288, ECO:0000269|PubMed:35595813}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:26745724}. Note=Localizes to the perinuclear region in the presence of RELT (PubMed:22052202). 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 (PubMed:12564925). {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202}.
Interaction partners:
- Interferon-induced protein with tetratricopeptide repeats 3
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced protein 44-like
- 2'-5'-oligoadenylate synthase 1
- Beta-secretase 1
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon-induced protein 44
- Protein mono-ADP-ribosyltransferase PARP9
- Interferon-induced helicase C domain-containing protein 1
Sequence:
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW