Plaat3
entrez
225845
canonical
uniprot
Q8R3U1
canonical
ensembl
ENSMUSG00000060675
resolver
ensp
ENSMUSP00000025925
resolver
ensp
ENSMUSP00000115151
resolver
genesymbol
Plaat3
resolver
genesymbol_syn
H-rev107
resolver
genesymbol_syn
Hrasls3
resolver
genesymbol_syn
Hrev107
resolver
genesymbol_syn
Pla2g16
resolver
uniprot
B7X6T3
resolver
uniprot
Q3V3C3
resolver
uniprot
Q8BWF7
resolver
uniprot_entry
PLAT3_MOUSE
resolver
uniprot_sec
B7X6T3
resolver
uniprot_sec
Q3V3C3
resolver
uniprot_sec
Q8BWF7
resolver
amino_acid_sequence
MLAPIPEPKPGDLIEIFRPMYRHWAIYVGDGYVIHLAPPSEIAGAGAASIMSALTDKAIVKKELLCHVAGKDKYQVNNKHDEEYTPLPLSKIIQRAERLVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
3.1.1.32
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19047760, PubMed:37919452). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:18614531, PubMed:19047760, PubMed:19136964, PubMed:22134920). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity,catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19047760). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light (PubMed:33854238). Organelle membrane degradation is probably catalyzed by the phospholipase activity (PubMed:33854238). {ECO:0000250|UniProtKB:P53816, ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920, ECO:0000269|PubMed:33854238, ECO:0000269|PubMed:37919452}.; FUNCTION: (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
uniprot
proteins
mass_dalton
17872
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="H->A,Q: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:22134920"; MUTAGEN 112; /note="N->A,Q: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18614531"; MUTAGEN 113; /note="C->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18614531"; MUTAGEN 113; /note="C->S: Loss of phospholipase activity and loss of organelle membrane rupture."; /evidence="ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:33854238"; MUTAGEN 129; /note="Q->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18614531
uniprot
proteins
protein_family
H-rev107 family
uniprot
proteins
pubmed
12055182
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18614531
uniprot
proteins
pubmed
19047760
uniprot
proteins
pubmed
19136964
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22134920
uniprot
proteins
pubmed
28077878
uniprot
proteins
pubmed
33854238
uniprot
proteins
pubmed
37919452
uniprot
proteins
sequence_length
162
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:33854238}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18614531}. Peroxisome membrane {ECO:0000269|PubMed:22134920}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:33854238}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.
uniprot
proteins
transmembrane_region
TRANSMEM 134..154; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins