Q39033 (PLCD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoinositide phospholipase C 2
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase PLC2
Short name=AtPLC2
Short name=PI-PLC2

Gene names

Name:	PLC2
Ordered Locus Names:	At3g08510
ORF Names:	T8G24.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7 Ref.9
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Subcellular location	Cell membrane; Peripheral membrane protein Ref.7.
Tissue specificity	Expressed in roots, shoots, leaves and flowers. Ref.1 Ref.9
Induction	Not induced by environmental stresses such as dehydration, salinity and low temperature. Ref.1 Ref.9
Domain	Amino acids 23-36 of the EF-hand-like domain are necessary catalysis but not for binding to lipid vesicles.
Post-translational modification	Phosphorylation level varies significantly during early response to bacterial elicitor.
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand-like domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.
Sequence caution	The sequence AAM61037.1 differs from that shown. Reason: Erroneous termination at position 335. Translated as Leu.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from direct assay PubMed 14506206PubMed 17317660PubMed 17644812PubMed 22923678. Source: TAIR
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 581	581	Phosphoinositide phospholipase C 2		PRO_0000324127
Regions
	Domain	26 – 102	77	EF-hand-like
	Domain	103 – 248	146	PI-PLC X-box
	Domain	317 – 433	117	PI-PLC Y-box
	Domain	439 – 546	108	C2
	Compositional bias	291 – 306	16	Asp-rich
Sites
	Active site	118	1	By similarity
	Active site	164	1	By similarity
Amino acid modifications
	Modified residue	280	1	Phosphoserine Ref.10 Ref.11 Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E337EB95EC16FC0B	FASTA	581	66,122
	10 20 30 40 50 60 MSKQTYKVCF CFRRRFRYTA SEAPREIKTI FEKYSENGVM TVDHLHRFLI DVQKQDKATR 70 80 90 100 110 120 EDAQSIINSA SSLLHRNGLH LDAFFKYLFG DNNPPLALHK VHHDMDAPIS HYFIFTGHNS 130 140 150 160 170 180 YLTGNQLSSD CSEVPIIDAL KKGVRVIELD IWPNSNKDDI DVLHGMTLTT PVGLIKCLKA 190 200 210 220 230 240 IRAHAFDVSD YPVVVTLEDH LTPDLQSKVA EMVTEIFGEI LFTPPVGESL KEFPSPNSLK 250 260 270 280 290 300 RRIIISTKPP KEYKEGKDVE VVQKGKDLGD EEVWGREVPS FIQRNKSEAK DDLDGNDDDD 310 320 330 340 350 360 DDDDEDKSKI NAPPQYKHLI AIHAGKPKGG ITECLKVDPD KVRRLSLSEE QLEKAAEKYA 370 380 390 400 410 420 KQIVRFTQHN LLRIYPKGTR VTSSNYNPLV GWSHGAQMVA FNMQGYGRSL WLMQGMFRAN 430 440 450 460 470 480 GGCGYIKKPD LLLKSGSDSD IFDPKATLPV KTTLRVTVYM GEGWYFDFRH THFDQYSPPD 490 500 510 520 530 540 FYTRVGIAGV PGDTVMKKTK TLEDNWIPAW DEVFEFPLTV PELALLRLEV HEYDMSEKDD 550 560 570 580 FGGQTCLPVW ELSEGIRAFP LHSRKGEKYK SVKLLVKVEF V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AtPLC2, a gene encoding phosphoinositide-specific phospholipase C, is constitutively expressed in vegetative and floral tissues in Arabidopsis thaliana." Hirayama T., Mitsukawa N., Shibata D., Shinozaki K. Plant Mol. Biol. 34:175-180(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, LACK OF INDUCTION.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-581.
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-581. Strain: cv. Columbia.
[7]	"N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana." Otterhag L., Sommarin M., Pical C. FEBS Lett. 497:165-170(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C." Mueller-Roeber B., Pical C. Plant Physiol. 130:22-46(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"Gene-specific expression and calcium activation of Arabidopsis thaliana phospholipase C isoforms." Hunt L., Otterhag L., Lee J.C., Lasheen T., Hunt J., Seki M., Shinozaki K., Sommarin M., Gilmour D.J., Pical C., Gray J.E. New Phytol. 162:643-654(2004) [AGRICOLA] [Europe PMC] Cited for: FUNCTION, LACK OF INDUCTION, TISSUE SPECIFICITY.
[10]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, MASS SPECTROMETRY.
[11]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, MASS SPECTROMETRY. Tissue: Seedling.
[12]	"Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses." Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C. Plant J. 51:931-940(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50804 mRNA. Translation: BAA09432.1. AC074395 Genomic DNA. Translation: AAG50827.1. CP002686 Genomic DNA. Translation: AEE74640.1. CP002686 Genomic DNA. Translation: AEE74641.1. AF360206 mRNA. Translation: AAK25916.1. AY040054 mRNA. Translation: AAK64112.1. AY084465 mRNA. Translation: AAM61037.1. Sequence problems. AK221660 mRNA. Translation: BAD95335.1.
IPI	IPI00536168.
PIR	S71170.
RefSeq	NP_001030660.1. NM_001035583.1. NP_187464.1. NM_111686.5.
UniGene	At.20554.
3D structure databases
HSSP	HSSP built from PDB template 1DJH based on UniProtKB P10688.
ProteinModelPortal	Q39033.
SMR	Q39033. Positions 26-579.
ModBase	Search...
Proteomic databases
PaxDb	Q39033.
PRIDE	Q39033.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G08510.1; AT3G08510.1; AT3G08510. AT3G08510.2; AT3G08510.2; AT3G08510.
GeneID	819999.
KEGG	ath:AT3G08510.
Organism-specific databases
TAIR	At3g08510.
Phylogenomic databases
eggNOG	NOG149692.
HOGENOM	HOG000244119.
InParanoid	Q39033.
KO	K05857.
OMA	APISHYF.
PhylomeDB	Q39033.
ProtClustDB	PLN02222.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-1621.
BRENDA	3.1.4.11. 399.
Gene expression databases
ArrayExpress	Q39033.
Genevestigator	Q39033.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 3.20.20.190. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR015359. PLipase_C_EF-hand-like. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR001711. PLipase_C_Pinositol-sp_Y. [Graphical view]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLCD2_ARATH

Accession

Primary (citable) accession number: Q39033
Secondary accession number(s): Q56XL3, Q8LG47

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program