PLAAT3
entrez
11145
canonical
uniprot
P53816
canonical
ensembl
ENSG00000176485
resolver
ensp
ENSP00000320337
resolver
ensp
ENSP00000389124
resolver
ensp
ENSP00000543704
resolver
ensp
ENSP00000543707
resolver
ensp
ENSP00000581602
resolver
ensp
ENSP00000581603
resolver
ensp
ENSP00000581606
resolver
enst
ENST00000323646
resolver
enst
ENST00000415826
resolver
enst
ENST00000873645
resolver
enst
ENST00000873648
resolver
enst
ENST00000911543
resolver
enst
ENST00000911544
resolver
enst
ENST00000911547
resolver
genesymbol
PLAAT3
resolver
genesymbol_syn
HRASLS3
resolver
genesymbol_syn
HREV107
resolver
genesymbol_syn
PLA2G16
resolver
hgnc
HGNC:17825
resolver
uniprot
B2R7Q4
resolver
uniprot
B7XAK5
resolver
uniprot
Q3SYI3
resolver
uniprot
Q9HDD1
resolver
uniprot_entry
PLAT3_HUMAN
resolver
uniprot_sec
B2R7Q4
resolver
uniprot_sec
B7XAK5
resolver
uniprot_sec
Q3SYI3
resolver
uniprot_sec
Q9HDD1
resolver
amino_acid_sequence
MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ
uniprot
proteins
disease_involvement
DISEASE: Lipodystrophy, familial partial, 9 (FPLD9) [MIM:620683]: An autosomal recessive form of partial lipodystrophy, a disorder characterized by abnormal subcutaneous fat distribution. FPLD9 patients are lean and show muscular hypertrophy, insulin-resistant diabetes with hyperinsulinemia, hypertriglyceridemia with low high-density lipoprotein (HDL) cholesterol, liver steatosis, and polycystic ovary syndrome with hirsutism. Some patients have more generalized lipoatrophy, whereas others have abnormal fat accumulation in the face and neck regions and show cushingoid or acromegalic facial features. Most patients also have neurologic features, including demyelinating polyneuropathy, developmental delay and intellectual disability. {ECO:0000269|PubMed:37919452}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). 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, PubMed:19615464, PubMed:22605381, PubMed:22825852). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). 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). {ECO:0000250|UniProtKB:Q8R3U1, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616, ECO:0000303|PubMed:26503625}.; FUNCTION: (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
uniprot
proteins
mass_dalton
17937
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="H->A: No effect on PPP2R1A-binding."; /evidence="ECO:0000269|PubMed:17374643"; MUTAGEN 39..57; /note="PSEVAGAGAASVMSALTDK->DILLALTDDMGRTQKVVSNKRLILGVIVKV: Induces a major structural rearrangement accompanied by domain-swapping dimerization and changes in substrate-specificity."; /evidence="ECO:0000269|PubMed:25383759"; MUTAGEN 113; /note="C->S: No effect on PPP2R1A-binding. Impaired ability to act as a host factor for picornaviruses."; /evidence="ECO:0000269|PubMed:17374643, ECO:0000269|PubMed:28077878
uniprot
proteins
protein_family
H-rev107 family
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
11526504
uniprot
proteins
pubmed
11973642
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17374643
uniprot
proteins
pubmed
19047760
uniprot
proteins
pubmed
19136964
uniprot
proteins
pubmed
19615464
uniprot
proteins
pubmed
20837014
uniprot
proteins
pubmed
22605381
uniprot
proteins
pubmed
22825852
uniprot
proteins
pubmed
22923616
uniprot
proteins
pubmed
25383759
uniprot
proteins
pubmed
26503625
uniprot
proteins
pubmed
28077878
uniprot
proteins
pubmed
37919452
uniprot
proteins
pubmed
9771974
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:17374643}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. 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 134..154; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins