O23179 · PLP1_ARATH
- ProteinPatatin-like protein 1
- GenePLP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids414 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
pH Dependence
Optimum pH is 7.0.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 66 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 215 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acylglycerol lipase activity | |
Molecular Function | phospholipase activity | |
Biological Process | defense response | |
Biological Process | lateral root formation | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePatatin-like protein 1
- EC number
- Short namesAtPLP1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO23179
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreased number of lateral roots.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 27 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000425813 | 1-414 | Patatin-like protein 1 | |||
Sequence: MENKSPSKKNKPPSCGSLVTILSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAMTAVSKQIVKNNPDMGKLKPLGFDRFLVISIGTGSTKREEKYSAKKAAKWGIISWLYDDGSTPILDITMESSRDMIHYHSSVVFKALQSEDKYLRIDDDTLEGDVSTMDLATKSNLENLQKIGEKMLTNRVMQMNIDTGVYEPVAENITNDEQLKRYAKILSDERKLRRLRSDTMIKDSSNESQEIK | ||||||
Modified residue | 399 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-399 by CPK3. Phosphorylation enhances PLP1 activity towards phosphatidylcholine.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed specifically in roots and root hairs.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-228 | PNPLA | ||||
Sequence: LSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAM | ||||||
Motif | 26-31 | GXGXXG | ||||
Sequence: GGGVRG | ||||||
Motif | 64-68 | GXSXG | ||||
Sequence: GTSTG | ||||||
Motif | 215-217 | DGA/G | ||||
Sequence: DGA |
Domain
The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence similarities
Belongs to the patatin family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O23179-1
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
- Length414
- Mass (Da)45,824
- Last updated1999-05-01 v2
- Checksum078E35777043AF43
O23179-2
- Name2
- Differences from canonical
- 384-414: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8MR01 | A8MR01_ARATH | PLP1 | 372 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 359 | in Ref. 5; AAM64566 | ||||
Sequence: M → V | ||||||
Alternative sequence | VSP_053856 | 384-414 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z99707 EMBL· GenBank· DDBJ | CAB16787.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161590 EMBL· GenBank· DDBJ | CAB80373.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE86744.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE86745.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE86746.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT029750 EMBL· GenBank· DDBJ | ABM06020.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087005 EMBL· GenBank· DDBJ | AAM64566.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ002596 EMBL· GenBank· DDBJ | CAA05628.1 EMBL· GenBank· DDBJ | mRNA |