Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00282
Entry Name
UniProt Accession
Theoretical PI
6.08
Molecular Weight
66122.31
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phosphoinositide phospholipase C 2
Protein Synonyms/Alias
3.1.4.11; Phosphoinositide phospholipase PLC2; AtPLC2; PI-PLC2;
Gene Name
PLC2
Gene Synonyms/Alias
At3g08510; T8G24.4;
Created Date
18-MAR-2008
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
9
Canonical
SKQTYKVCFCFRRRF
[1]
S-Palmitoylation
11
Canonical
QTYKVCFCFRRRFRY
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Domain: 26 102 EF-hand-like.
Domain: 103 248 PI-PLC X-box.
Domain: 317 433 PI-PLC Y-box.
Domain: 439 546 C2.
Active site: 118 118
Active site: 164 164
Protein Length
581 AA.
Protein Sequence
(Canonical)
MSKQTYKVCF CFRRRFRYTA SEAPREIKTI FEKYSENGVM TVDHLHRFLI DVQKQDKATR  60
EDAQSIINSA SSLLHRNGLH LDAFFKYLFG DNNPPLALHK VHHDMDAPIS HYFIFTGHNS  120
YLTGNQLSSD CSEVPIIDAL KKGVRVIELD IWPNSNKDDI DVLHGMTLTT PVGLIKCLKA  180
IRAHAFDVSD YPVVVTLEDH LTPDLQSKVA EMVTEIFGEI LFTPPVGESL KEFPSPNSLK  240
RRIIISTKPP KEYKEGKDVE VVQKGKDLGD EEVWGREVPS FIQRNKSEAK DDLDGNDDDD  300
DDDDEDKSKI NAPPQYKHLI AIHAGKPKGG ITECLKVDPD KVRRLSLSEE QLEKAAEKYA  360
KQIVRFTQHN LLRIYPKGTR VTSSNYNPLV GWSHGAQMVA FNMQGYGRSL WLMQGMFRAN  420
GGCGYIKKPD LLLKSGSDSD IFDPKATLPV KTTLRVTVYM GEGWYFDFRH THFDQYSPPD  480
FYTRVGIAGV PGDTVMKKTK TLEDNWIPAW DEVFEFPLTV PELALLRLEV HEYDMSEKDD  540
FGGQTCLPVW ELSEGIRAFP LHSRKGEKYK SVKLLVKVEF V                      581
FASTA
(Canonical)
>LipidDB-3702-00282|Q39033
MSKQTYKVCFCFRRRFRYTASEAPREIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATR
EDAQSIINSASSLLHRNGLHLDAFFKYLFGDNNPPLALHKVHHDMDAPISHYFIFTGHNS
YLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSNKDDIDVLHGMTLTTPVGLIKCLKA
IRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVGESLKEFPSPNSLK
RRIIISTKPPKEYKEGKDVEVVQKGKDLGDEEVWGREVPSFIQRNKSEAKDDLDGNDDDD
DDDDEDKSKINAPPQYKHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEEQLEKAAEKYA
KQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRAN
GGCGYIKKPDLLLKSGSDSDIFDPKATLPVKTTLRVTVYMGEGWYFDFRHTHFDQYSPPD
FYTRVGIAGVPGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDD
FGGQTCLPVWELSEGIRAFPLHSRKGEKYKSVKLLVKVEFV
Gene Ontology
GO:0005886; C:plasma membrane; IDA:TAIR
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC
GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW
GO:0035556; P:intracellular signal transduction; IEA:InterPro
GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW
Interpro
InterPro; IPR000008; C2_dom
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR001192; PI-PLC_fam
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl
InterPro; IPR015359; PLipase_C_EF-hand-like
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y
Pfam
Pfam; PF00168; C2;
Pfam; PF09279; EF-hand_like;
Pfam; PF00388; PI-PLC-X;
Pfam; PF00387; PI-PLC-Y;
SMART
SMART; SM00239; C2;
SMART; SM00148; PLCXc;
SMART; SM00149; PLCYc;
PROSITE
PROSITE; PS50004; C2;
PROSITE; PS50007; PIPLC_X_DOMAIN;
PROSITE; PS50008; PIPLC_Y_DOMAIN;
PRINTS
PRINTS; PR00390; PHPHLIPASEC;