PLSCR1
entrez
5359
canonical
uniprot
O15162
canonical
ensembl
ENSG00000188313
resolver
ensp
ENSP00000345494
resolver
ensp
ENSP00000411675
resolver
ensp
ENSP00000417792
resolver
ensp
ENSP00000418103
resolver
ensp
ENSP00000577700
resolver
ensp
ENSP00000577701
resolver
ensp
ENSP00000577702
resolver
ensp
ENSP00000577704
resolver
enst
ENST00000448787
resolver
enst
ENST00000487389
resolver
genesymbol
PLSCR1
resolver
hgnc
HGNC:9092
resolver
uniprot
B2R8H8
resolver
uniprot
B4DTE8
resolver
uniprot
C9J7K9
resolver
uniprot_entry
C9J7K9_HUMAN
resolver
uniprot_entry
PLS1_HUMAN
resolver
uniprot_sec
B2R8H8
resolver
uniprot_sec
B4DTE8
resolver
activity_regulation
ACTIVITY REGULATION: Activated by Pb(2+) and Hg(2+) ions (PubMed:23659204, PubMed:29748552). Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (PubMed:10770950). {ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:29748552}.
uniprot
proteins
amino_acid_sequence
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
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 (PubMed:10770950, PubMed:18629440, PubMed:23590222, PubMed:23659204, PubMed:24343571, PubMed:24648509, PubMed:29748552, PubMed:32110987, PubMed:8663431, PubMed:9218461, PubMed:9485382, PubMed:9572851). 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 (PubMed:17567603, PubMed:27206388). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed:26745724). 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 (PubMed:15308695). Inhibits the functions of viral transactivators, including human T-cell leukemia virus (HTLV)-1 protein Tax, human immunodeficiency virus (HIV)-1 Tat, human hepatitis B virus (HBV) HBx, Epstein-Barr virus (EBV) BZLF1 and human cytomegalovirus IE1 and IE2 proteins through direct interactions (PubMed:22789739, PubMed:23501106, PubMed:25365352, PubMed:31434743, PubMed:35138119). Also mediates the inhibition of influenza virus infection by preventing nuclear import of the viral nucleoprotein/NP (PubMed:29352288, PubMed:35595813). Plays a crucial role as a defense factor against SARS-CoV-2 independently of its scramblase activity by directly targeting nascent viral vesicles to prevent virus-membrane fusion and the release of viral RNA into the host-cell cytosol (PubMed:37438530). {ECO:0000250|UniProtKB:Q9JJ00, ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:15308695, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18629440, ECO:0000269|PubMed:21806988, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:23501106, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:25365352, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:27206388, ECO:0000269|PubMed:29748552, ECO:0000269|PubMed:31434743, ECO:0000269|PubMed:32110987, ECO:0000269|PubMed:35138119, ECO:0000269|PubMed:37438530, ECO:0000269|PubMed:8663431, ECO:0000269|PubMed:9218461, ECO:0000269|PubMed:9485382, ECO:0000269|PubMed:9572851}.; FUNCTION: (Microbial infection) Acts as an attachment receptor for HCV. {ECO:0000269|PubMed:21806988}.
uniprot
proteins
mass_dalton
35049
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="H->A: 60% reduction in nuclease activity; when associated with A-53; A-111; A-211 and A-262."; /evidence="ECO:0000269|PubMed:27206388"; MUTAGEN 53; /note="H->A: 60% reduction in nuclease activity; when associated with A-12; A-111; A-211 and A-262."; /evidence="ECO:0000269|PubMed:27206388"; MUTAGEN 69; /note="Y->F: Decrease in phosphorylation."; /evidence="ECO:0000269|PubMed:11390389"; MUTAGEN 74; /note="Y->F: Decrease in phosphorylation."; /evidence="ECO:0000269|PubMed:11390389"; MUTAGEN 111; /note="H->A: 60% reduction in nuclease activity; when associated with A-12; A-53; A-211 and A-262."; /evidence="ECO:0000269|PubMed:27206388"; MUTAGEN 161; /note="T->A: No induction by PKC/PRKCD."; /evidence="ECO:0000269|PubMed:10770950"; MUTAGEN 184..189; /note="CCCPCC->AAAPAA: No palmitoylation; constitutively localizes in the nucleus. Loss of protection against SARS-CoV-2-containing vesicles."; /evidence="ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:15611084, ECO:0000269|PubMed:37438530"; MUTAGEN 211; /note="H->A: 60% reduction in nuclease activity; when associated with A-12; A-53; A-111 and A-262."; /evidence="ECO:0000269|PubMed:27206388"; MUTAGEN 262; /note="H->A: 60% reduction in nuclease activity; when associated with A-12; A-53; A-111 and A-211."; /evidence="ECO:0000269|PubMed:27206388"; MUTAGEN 273; /note="D->A: Reduces the Ca(2+)-dependent phospholipid scrambling."; /evidence="ECO:0000269|PubMed:9485382"; MUTAGEN 275; /note="D->A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling. No effect on its nuclease activity."; /evidence="ECO:0000269|PubMed:27206388, ECO:0000269|PubMed:9485382"; MUTAGEN 277; /note="F->A: Reduces the Ca(2+)-dependent phospholipid scrambling."; /evidence="ECO:0000269|PubMed:9485382"; MUTAGEN 279; /note="I->A: Reduces the Ca(2+)-dependent phospholipid scrambling."; /evidence="ECO:0000269|PubMed:9485382"; MUTAGEN 281; /note="F->A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling."; /evidence="ECO:0000269|PubMed:37438530, ECO:0000269|PubMed:9485382"; MUTAGEN 284; /note="D->A: Reduces the Ca(2+)-dependent phospholipid scrambling."; /evidence="ECO:0000269|PubMed:9485382
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (PubMed:10770950). Phosphorylated by OXSR1 in the presence of RELT. {ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:22052202}.; PTM: Palmitoylation is required for its phospholipid scramblase activity (PubMed:9572851). 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:9572851}.
uniprot
proteins
protein_family
Phospholipid scramblase family
uniprot
proteins
pubmed
10770950
uniprot
proteins
pubmed
10930526
uniprot
proteins
pubmed
11390389
uniprot
proteins
pubmed
12564925
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15308695
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15611084
uniprot
proteins
pubmed
16091359
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17567603
uniprot
proteins
pubmed
18629440
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21806988
uniprot
proteins
pubmed
22052202
uniprot
proteins
pubmed
22789739
uniprot
proteins
pubmed
23501106
uniprot
proteins
pubmed
23590222
uniprot
proteins
pubmed
23659204
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24343571
uniprot
proteins
pubmed
24648509
uniprot
proteins
pubmed
25365352
uniprot
proteins
pubmed
26745724
uniprot
proteins
pubmed
27206388
uniprot
proteins
pubmed
29352288
uniprot
proteins
pubmed
29748552
uniprot
proteins
pubmed
31434743
uniprot
proteins
pubmed
32110987
uniprot
proteins
pubmed
35138119
uniprot
proteins
pubmed
35595813
uniprot
proteins
pubmed
37438530
uniprot
proteins
pubmed
8663431
uniprot
proteins
pubmed
9218461
uniprot
proteins
pubmed
9485382
uniprot
proteins
pubmed
9572851
uniprot
proteins
pubmed
9712717
uniprot
proteins
sequence_length
318
uniprot
proteins
subcellular_location
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 289..305; /note="Helical"; /evidence="ECO:0000269|PubMed:23590222
uniprot
proteins