Q39033 · PLCD2_ARATH
- ProteinPhosphoinositide phospholipase C 2
- GenePLC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids581 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. At physiological calcium concentration, the preferred substrate is phosphatidylinositol 4,5-bisphosphate versus phosphatidylinositol.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H+
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 118 | |||||
Sequence: H | ||||||
Active site | 164 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | phosphatidylinositol phospholipase C activity | |
Molecular Function | phospholipase C activity | |
Biological Process | defense response to bacterium | |
Biological Process | embryo sac development | |
Biological Process | floral organ development | |
Biological Process | intracellular signal transduction | |
Biological Process | lipid catabolic process | |
Biological Process | microsporogenesis | |
Biological Process | positive regulation of auxin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoinositide phospholipase C 2
- EC number
- 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 accessionQ39033
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000324127 | 1-581 | Phosphoinositide phospholipase C 2 | |||
Sequence: MSKQTYKVCFCFRRRFRYTASEAPREIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATREDAQSIINSASSLLHRNGLHLDAFFKYLFGDNNPPLALHKVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSNKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVGESLKEFPSPNSLKRRIIISTKPPKEYKEGKDVEVVQKGKDLGDEEVWGREVPSFIQRNKSEAKDDLDGNDDDDDDDDEDKSKINAPPQYKHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFDPKATLPVKTTLRVTVYMGEGWYFDFRHTHFDQYSPPDFYTRVGIAGVPGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSEGIRAFPLHSRKGEKYKSVKLLVKVEFV |
Post-translational modification
Phosphorylation level varies significantly during early response to bacterial elicitor.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, shoots, leaves and flowers.
Induction
Not induced by environmental stresses such as dehydration, salinity and low temperature.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-102 | EF-hand-like | ||||
Sequence: EIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATREDAQSIINSASSLLHRNGLHLDAFFKYLFGDNNPPLALHKVH | ||||||
Domain | 103-248 | PI-PLC X-box | ||||
Sequence: HDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSNKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVGESLKEFPSPNSLKRRIIISTK | ||||||
Region | 279-314 | Disordered | ||||
Sequence: PSFIQRNKSEAKDDLDGNDDDDDDDDEDKSKINAPP | ||||||
Domain | 317-433 | PI-PLC Y-box | ||||
Sequence: KHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLL | ||||||
Domain | 434-563 | C2 | ||||
Sequence: KSGSDSDIFDPKATLPVKTTLRVTVYMGEGWYFDFRHTHFDQYSPPDFYTRVGIAGVPGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSEGIRAFPLHS |
Domain
Amino acids 23-36 of the EF-hand-like domain are necessary catalysis but not for binding to lipid vesicles.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q39033-1
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
- Length581
- Mass (Da)66,122
- Last updated1996-11-01 v1
- ChecksumE337EB95EC16FC0B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4IX90 | F4IX90_ARATH | PLC2 | 552 |
Sequence caution
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D50804 EMBL· GenBank· DDBJ | BAA09432.1 EMBL· GenBank· DDBJ | mRNA | ||
AC074395 EMBL· GenBank· DDBJ | AAG50827.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74640.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74641.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF360206 EMBL· GenBank· DDBJ | AAK25916.1 EMBL· GenBank· DDBJ | mRNA | ||
AY040054 EMBL· GenBank· DDBJ | AAK64112.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084465 EMBL· GenBank· DDBJ | AAM61037.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK221660 EMBL· GenBank· DDBJ | BAD95335.1 EMBL· GenBank· DDBJ | mRNA |