PLSCR3
entrez
57048
canonical
uniprot
Q9NRY6
canonical
ensembl
ENSG00000187838
resolver
ensembl
ENSG00000284009
resolver
ensp
ENSP00000316021
resolver
ensp
ENSP00000459019
resolver
ensp
ENSP00000459419
resolver
ensp
ENSP00000483743
resolver
ensp
ENSP00000491350
resolver
ensp
ENSP00000491393
resolver
ensp
ENSP00000492026
resolver
ensp
ENSP00000492083
resolver
ensp
ENSP00000569159
resolver
ensp
ENSP00000569167
resolver
ensp
ENSP00000607965
resolver
ensp
ENSP00000607966
resolver
ensp
ENSP00000625959
resolver
ensp
ENSP00000625960
resolver
enst
ENST00000324822
resolver
enst
ENST00000574401
resolver
enst
ENST00000576201
resolver
enst
ENST00000619711
resolver
enst
ENST00000639780
resolver
enst
ENST00000639874
resolver
enst
ENST00000640053
resolver
enst
ENST00000640375
resolver
enst
ENST00000899108
resolver
enst
ENST00000937906
resolver
enst
ENST00000937907
resolver
enst
ENST00000955900
resolver
enst
ENST00000955901
resolver
genesymbol
PLSCR3
resolver
hgnc
HGNC:16495
resolver
uniprot
A8K252
resolver
uniprot
Q567U0
resolver
uniprot
Q8NBW6
resolver
uniprot
Q96F13
resolver
uniprot_entry
PLS3_HUMAN
resolver
uniprot_sec
A8K252
resolver
uniprot_sec
Q567U0
resolver
uniprot_sec
Q8NBW6
resolver
uniprot_sec
Q96F13
resolver
activity_regulation
ACTIVITY REGULATION: Activated by Pb(2+) and Hg(2+) ions. {ECO:0000269|PubMed:31769662}.
uniprot
proteins
amino_acid_sequence
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVALGSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAAEESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQWGGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
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 (PubMed:14573790, PubMed:17226776, PubMed:18358005, PubMed:29337693, PubMed:31769662). Plays an important role in mitochondrial respiratory function, morphology, and apoptotic response (PubMed:12649167, PubMed:14573790, PubMed:17226776, PubMed:18358005). Mediates the translocation of cardiolipin from the mitochondrial inner membrane to outer membrane enhancing t-Bid induced cytochrome c release and apoptosis (PubMed:14573790, PubMed:17226776, PubMed:18358005). 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 (PubMed:18491232). Regulates cardiolipin de novo biosynthesis and its resynthesis (PubMed:16939411). {ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:14573790, ECO:0000269|PubMed:16939411, ECO:0000269|PubMed:17226776, ECO:0000269|PubMed:18358005, ECO:0000269|PubMed:18491232, ECO:0000269|PubMed:29337693, ECO:0000269|PubMed:31769662}.
uniprot
proteins
mass_dalton
31648
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="T->A: Fails to enhance apoptosis mediated by PRKCD activators."; /evidence="ECO:0000269|PubMed:17226776"; MUTAGEN 21; /note="T->D: Promotes apoptosis, more potent in lipid flippase activity."; /evidence="ECO:0000269|PubMed:17226776"; MUTAGEN 49; /note="F->A: Reduces interaction with PDCD6. Abolishes interaction with PDCD6; when associated with A-52."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 49; /note="F->W: No effect on the interaction with PDCD6."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 49; /note="F->Y,L: Reduces interaction with PDCD6."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 52; /note="F->A: Abolishes interaction with PDCD6; when associated with A-49."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 258; /note="F->V: Reduced phospholipid scramblase activity. Reduced calcium and magnesium-binding. Diminished apoptotic responsiveness. Defective mitochondrial structure and oxidative function. Reduced binding affinity for Pb(2+) and Hg(2+) ions. Increased cardiolipin biosynthesis from glycerol and decreased cardiolipin resynthesis from linoleic acid."; /evidence="ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:14573790, ECO:0000269|PubMed:16939411, ECO:0000269|PubMed:18358005, ECO:0000269|PubMed:18491232, ECO:0000269|PubMed:29337693, ECO:0000269|PubMed:31769662
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-21 by PKC/PRKCD upon apoptotic stimuli enhances phospholipid scramblase activity. {ECO:0000269|PubMed:17226776, ECO:0000305|PubMed:12649167}.; 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:0000250|UniProtKB:Q9JIZ9}.
uniprot
proteins
protein_family
Phospholipid scramblase family
uniprot
proteins
pubmed
10930526
uniprot
proteins
pubmed
12649167
uniprot
proteins
pubmed
14573790
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16939411
uniprot
proteins
pubmed
17226776
uniprot
proteins
pubmed
18256029
uniprot
proteins
pubmed
18358005
uniprot
proteins
pubmed
18491232
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
29337693
uniprot
proteins
pubmed
31769662
uniprot
proteins
sequence_length
295
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:14573790, ECO:0000269|PubMed:17226776, ECO:0000269|PubMed:18491232}; 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:0000250|UniProtKB:Q9JIZ9}. 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:0000250|UniProtKB:Q9JIZ9}.
uniprot
proteins
transmembrane_region
TRANSMEM 266..282; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins