Q9QZU4 · PLAT1_MOUSE
- ProteinPhospholipase A and acyltransferase 1
- GenePlaat1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids167 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity).
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:21880860).
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) (By similarity).
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:21880860).
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) (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H+ + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamineThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholineThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 30 | |||||
Sequence: H | ||||||
Active site | 119 | Acyl-thioester intermediate | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A and acyltransferase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QZU4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-138 | Cytoplasmic | ||||
Sequence: MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANR | ||||||
Transmembrane | 139-159 | Helical | ||||
Sequence: AIGTIGLVAAGIDIFTFLGLF | ||||||
Topological domain | 160-167 | Lumenal | ||||
Sequence: PKRQRTKY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000152482 | 1-167 | Phospholipase A and acyltransferase 1 | |||
Sequence: MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-135 | LRAT | ||||
Sequence: LIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQ |
Sequence similarities
Belongs to the H-rev107 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9QZU4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsPLAAT-1S
- Length167
- Mass (Da)18,810
- Last updated2000-05-01 v1
- Checksum619C43691DCC86C8
Q9QZU4-2
- Name2
- SynonymsPLAAT-1L
- Differences from canonical
- 1-1: M → MPEACLEDLGGGEGAGLGRAPKTRGRRQGPQDAVWQARARNPRRDQRWRGARTLALTQRREAVVALAVALASGRCGWSHPGSASGTAASPWRTREARHCLQGTKTTQLEQM
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J130 | A0A0R4J130_MOUSE | Plaat1 | 167 | ||
E0CYE9 | E0CYE9_MOUSE | Plaat1 | 50 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_060191 | 1 | in isoform 2 | |||
Sequence: M → MPEACLEDLGGGEGAGLGRAPKTRGRRQGPQDAVWQARARNPRRDQRWRGARTLALTQRREAVVALAVALASGRCGWSHPGSASGTAASPWRTREARHCLQGTKTTQLEQM | ||||||
Sequence conflict | 105 | in Ref. 1; BAB23348 | ||||
Sequence: P → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF163095 EMBL· GenBank· DDBJ | AAF13304.1 EMBL· GenBank· DDBJ | mRNA | ||
AB510982 EMBL· GenBank· DDBJ | BAI63211.1 EMBL· GenBank· DDBJ | mRNA | ||
AK004528 EMBL· GenBank· DDBJ | BAB23348.1 EMBL· GenBank· DDBJ | mRNA | ||
AK039471 EMBL· GenBank· DDBJ | BAC30361.1 EMBL· GenBank· DDBJ | mRNA | ||
AC154448 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466521 EMBL· GenBank· DDBJ | EDK97707.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466521 EMBL· GenBank· DDBJ | EDK97708.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC048482 EMBL· GenBank· DDBJ | AAH48482.1 EMBL· GenBank· DDBJ | mRNA |