Plscr1
entrez
117540
canonical
uniprot
P58195
canonical
ensembl
ENSRNOG00000008048
resolver
ensp
ENSRNOP00000010689
resolver
ensp
ENSRNOP00000053569
resolver
ensp
ENSRNOP00000074296
resolver
genesymbol
Plscr1
resolver
uniprot
Q5U351
resolver
uniprot_entry
PLS1_RAT
resolver
uniprot_entry
Q5U351_RAT
resolver
amino_acid_sequence
MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDPSGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEKRQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNEEQRSGVW
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 (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}.
uniprot
proteins
mass_dalton
36711
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues (PubMed:11259432). Phosphorylated by OXSR1 in the presence of RELT (By similarity). Phosphorylation at Thr-178 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (By similarity). {ECO:0000250|UniProtKB:O15162, ECO:0000269|PubMed:11259432}.; 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
11259432
uniprot
proteins
sequence_length
335
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 306..322; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins