Plscr3
entrez
70310
canonical
uniprot
Q9JIZ9
canonical
ensembl
ENSMUSG00000019461
resolver
ensp
ENSMUSP00000019605
resolver
ensp
ENSMUSP00000104272
resolver
ensp
ENSMUSP00000104273
resolver
ensp
ENSMUSP00000174987
resolver
ensp
ENSMUSP00000174993
resolver
enst
ENSMUST00000019605
resolver
enst
ENSMUST00000108632
resolver
enst
ENSMUST00000108633
resolver
genesymbol
Plscr3
resolver
uniprot
Q5F283
resolver
uniprot_entry
PLS3_MOUSE
resolver
uniprot_entry
Q5F283_MOUSE
resolver
amino_acid_sequence
MAGYLPPKGYAPSPPPPYPVPSGYPEPVALHPGPGQAPVPTQVPAPAPGFALFPSPGPVAPGPPAPFVPLPGVPPGLEFLVQIDQILIHQKAERVETFLGWETCNMYELRSGTGQQLGQAAEESNCCARLCCGARRPFRIRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFLPKFSILDADRQPVLRVVGPCWTCGCGTDTNFEVKTKDESRSVGRISKQWGGLLREALTDADDFGLQFPVDLDVKVKAVLLGATFLIDYMFFEKRGGAGPSAITS
uniprot
proteins
function
FUNCTION: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of the phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer membrane of the mitochondria (By similarity). Plays an important role in mitochondrial respiratory function, morphology, and apoptotic response (By similarity). Mediates the translocation of cardiolipin from the mitochondrial inner membrane to outer membrane enhancing t-Bid induced cytochrome c release and apoptosis (Probable). Enhances TNFSF10-induced apoptosis by regulating the distribution of cardiolipin in the mitochondrial membrane resulting in increased release of apoptogenic factors and consequent amplification of the activity of caspases (By similarity). Regulates cardiolipin de novo biosynthesis and its resynthesis (By similarity). {ECO:0000250|UniProtKB:Q9NRY6, ECO:0000305|PubMed:21785166}.
uniprot
proteins
mass_dalton
31803
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="C->A: Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-161, A-163, A-164 and A-166. Partial loss of palmitoylation; when associated with A-161."; /evidence="ECO:0000269|PubMed:21785166"; MUTAGEN 161; /note="C->A: Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-163, A-164 and A-166. Partial loss of palmitoylation; when associated with A-159."; /evidence="ECO:0000269|PubMed:21785166"; MUTAGEN 163; /note="C->A: Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-161, A-164 and A-166."; /evidence="ECO:0000269|PubMed:21785166"; MUTAGEN 164; /note="C->A: Complete loss of palmitoylation, mislocalization from mitochondrial membrane and reduced apoptotic function; when associated with A-159, A-161, A-163 and A-166."; /evidence="ECO:0000269|PubMed:21785166"; MUTAGEN 166; /note="C->A: Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-161, A-163 and A-164."; /evidence="ECO:0000269|PubMed:21785166
uniprot
proteins
post_translational_modification
PTM: 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:0000269|PubMed:21785166}.
uniprot
proteins
protein_family
Phospholipid scramblase family
uniprot
proteins
pubmed
10930526
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19428821
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21785166
uniprot
proteins
sequence_length
296
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:21785166}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6QBQ4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Nucleus {ECO:0000269|PubMed:21785166}. Note=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:0000269|PubMed:21785166}.
uniprot
proteins
transmembrane_region
TRANSMEM 267..283; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins