Plaat3
entrez
24913
canonical
uniprot
P53817
canonical
ensembl
ENSRNOG00000021206
resolver
ensp
ENSRNOP00000038045
resolver
ensp
ENSRNOP00000105263
resolver
enst
ENSRNOT00000163362
resolver
genesymbol
Plaat3
resolver
genesymbol_syn
H-rev107
resolver
genesymbol_syn
Hrasls3
resolver
genesymbol_syn
Hrev107
resolver
genesymbol_syn
Pla2g16
resolver
genesymbol_syn
Rlp-3
resolver
uniprot
A0ABK0LKD1
resolver
uniprot
B7X6T2
resolver
uniprot_entry
A0ABK0LKD1_RAT
resolver
uniprot_entry
PLAT3_RAT
resolver
uniprot_sec
B7X6T2
resolver
amino_acid_sequence
MPIPEPKPGDLIEIFRPMYSHWAIYVGDGYVIHLAPPSEIPGAGAASIMSALTDKAIVKKELLRDVAGKDKYQVNNKHDKEYTPLPLNKIIQRAEELVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKVATVTGVGLAALGLIGVMLSRNKKQKQ
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). Shows phospholipase A1 (PLA1) and A2 (PLA2), ccatalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760). 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:17158102, 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. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). Plays a role in phospholipid metabolism and adipogenesis. {ECO:0000250|UniProtKB:P53816, ECO:0000250|UniProtKB:Q8R3U1, ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:19047760}.
uniprot
proteins
mass_dalton
17749
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="H->L: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:19047760"; MUTAGEN 111; /note="C->S: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:19047760
uniprot
proteins
protein_family
H-rev107 family
uniprot
proteins
pubmed
17158102
uniprot
proteins
pubmed
18614531
uniprot
proteins
pubmed
19047760
uniprot
proteins
pubmed
8290259
uniprot
proteins
sequence_length
160
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8290259}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:8290259}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8290259}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; 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:0000250|UniProtKB:Q8R3U1}.
uniprot
proteins
transmembrane_region
TRANSMEM 132..152; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins