Plscr1
entrez
22038
canonical
uniprot
Q9JJ00
canonical
ensembl
ENSMUSG00000032369
resolver
ensp
ENSMUSP00000091318
resolver
ensp
ENSMUSP00000139479
resolver
enst
ENSMUST00000093801
resolver
enst
ENSMUST00000186364
resolver
genesymbol
Plscr1
resolver
genesymbol_syn
Tra1b
resolver
genesymbol_syn
Tras1
resolver
uniprot
O54730
resolver
uniprot
O54731
resolver
uniprot
Q9D1F8
resolver
uniprot_entry
PLS1_MOUSE
resolver
uniprot_sec
O54730
resolver
uniprot_sec
O54731
resolver
uniprot_sec
Q9D1F8
resolver
amino_acid_sequence
MENHSKQTEAPHPGTYMPAGYPPPYPPAAFQGPSDHAAYPIPQAGYQGPPGPYPGPQPGYPVPPGGYAGGGPSGFPVQNQPAYNHPGGPGGTPWMPAPPPPLNCPPGLEYLAQIDQLLVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTRNCCGASRPFTLRILDNLGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVTQTWHPCLPKFTLQNEKKQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNEEQRSGAWQ
uniprot
proteins
disease_involvement
DISEASE: Note=Participates in a chromosomal translocation that produces MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude mice.
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
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 (PubMed:32110987). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (PubMed:32110987). 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 (PubMed:26745724). May contribute to cytokine-regulated cell proliferation and differentiation (PubMed:12010804). {ECO:0000250|UniProtKB:O15162, ECO:0000269|PubMed:12010804, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:32110987}.
uniprot
proteins
mass_dalton
35914
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-170 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (By similarity). Phosphorylated by OXSR1 in the presence of RELT (By similarity). {ECO:0000250|UniProtKB:O15162}.; PTM: Palmitoylation is required for its phospholipid scramblase activity (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:O15162}.
uniprot
proteins
protein_family
Phospholipid scramblase family
uniprot
proteins
pubmed
10930526
uniprot
proteins
pubmed
12010804
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26745724
uniprot
proteins
pubmed
32110987
uniprot
proteins
pubmed
35595813
uniprot
proteins
pubmed
9108418
uniprot
proteins
sequence_length
328
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 298..314; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins