Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoinositide phospholipase C 2

Gene

PLC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei118 – 1181PROSITE-ProRule annotation
Active sitei164 – 1641PROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  2. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciARA:GQT-1492-MONOMER.
ARA:GQT-328-MONOMER.
MetaCyc:MONOMER-1621.
BRENDAi3.1.4.11. 399.
ReactomeiREACT_278077. Role of phospholipids in phagocytosis.
REACT_278842. Role of second messengers in netrin-1 signaling.
REACT_279237. VEGFR2 mediated cell proliferation.
REACT_284166. Generation of second messenger molecules.
REACT_286162. PLC beta mediated events.
REACT_306790. GPVI-mediated activation cascade.
REACT_318389. Signaling by FGFR1 fusion mutants.
REACT_328347. DAG and IP3 signaling.
REACT_350143. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PLC2
Ordered Locus Names:At3g08510
ORF Names:T8G24.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G08510.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Phosphoinositide phospholipase C 2PRO_0000324127Add
BLAST

Post-translational modificationi

Phosphorylation level varies significantly during early response to bacterial elicitor.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ39033.
PRIDEiQ39033.

Expressioni

Tissue specificityi

Expressed in roots, shoots, leaves and flowers.2 Publications

Inductioni

Not induced by environmental stresses such as dehydration, salinity and low temperature.

Gene expression databases

ExpressionAtlasiQ39033. baseline and differential.
GenevestigatoriQ39033.

Interactioni

Protein-protein interaction databases

IntActiQ39033. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ39033.
SMRiQ39033. Positions 26-579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10277EF-hand-likeAdd
BLAST
Domaini103 – 248146PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini317 – 433117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini439 – 546108C2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi291 – 30616Asp-richAdd
BLAST

Domaini

Amino acids 23-36 of the EF-hand-like domain are necessary catalysis but not for binding to lipid vesicles.

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand-like domain.Curated
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000244119.
InParanoidiQ39033.
KOiK05857.
OMAiKTEHWIL.
PhylomeDBiQ39033.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: Q39033-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSKQTYKVCF CFRRRFRYTA SEAPREIKTI FEKYSENGVM TVDHLHRFLI
60 70 80 90 100
DVQKQDKATR EDAQSIINSA SSLLHRNGLH LDAFFKYLFG DNNPPLALHK
110 120 130 140 150
VHHDMDAPIS HYFIFTGHNS YLTGNQLSSD CSEVPIIDAL KKGVRVIELD
160 170 180 190 200
IWPNSNKDDI DVLHGMTLTT PVGLIKCLKA IRAHAFDVSD YPVVVTLEDH
210 220 230 240 250
LTPDLQSKVA EMVTEIFGEI LFTPPVGESL KEFPSPNSLK RRIIISTKPP
260 270 280 290 300
KEYKEGKDVE VVQKGKDLGD EEVWGREVPS FIQRNKSEAK DDLDGNDDDD
310 320 330 340 350
DDDDEDKSKI NAPPQYKHLI AIHAGKPKGG ITECLKVDPD KVRRLSLSEE
360 370 380 390 400
QLEKAAEKYA KQIVRFTQHN LLRIYPKGTR VTSSNYNPLV GWSHGAQMVA
410 420 430 440 450
FNMQGYGRSL WLMQGMFRAN GGCGYIKKPD LLLKSGSDSD IFDPKATLPV
460 470 480 490 500
KTTLRVTVYM GEGWYFDFRH THFDQYSPPD FYTRVGIAGV PGDTVMKKTK
510 520 530 540 550
TLEDNWIPAW DEVFEFPLTV PELALLRLEV HEYDMSEKDD FGGQTCLPVW
560 570 580
ELSEGIRAFP LHSRKGEKYK SVKLLVKVEF V
Length:581
Mass (Da):66,122
Last modified:November 1, 1996 - v1
Checksum:iE337EB95EC16FC0B
GO

Sequence cautioni

The sequence AAM61037.1 differs from that shown. Reason: Erroneous termination at position 335. Translated as Leu.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS71170.
RefSeqiNP_001030660.1. NM_001035583.1. [Q39033-1]
NP_187464.1. NM_111686.5. [Q39033-1]
UniGeneiAt.20554.

Genome annotation databases

EnsemblPlantsiAT3G08510.1; AT3G08510.1; AT3G08510. [Q39033-1]
AT3G08510.2; AT3G08510.2; AT3G08510. [Q39033-1]
GeneIDi819999.
KEGGiath:AT3G08510.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS71170.
RefSeqiNP_001030660.1. NM_001035583.1. [Q39033-1]
NP_187464.1. NM_111686.5. [Q39033-1]
UniGeneiAt.20554.

3D structure databases

ProteinModelPortaliQ39033.
SMRiQ39033. Positions 26-579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ39033. 1 interaction.

Proteomic databases

PaxDbiQ39033.
PRIDEiQ39033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G08510.1; AT3G08510.1; AT3G08510. [Q39033-1]
AT3G08510.2; AT3G08510.2; AT3G08510. [Q39033-1]
GeneIDi819999.
KEGGiath:AT3G08510.

Organism-specific databases

TAIRiAT3G08510.

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000244119.
InParanoidiQ39033.
KOiK05857.
OMAiKTEHWIL.
PhylomeDBiQ39033.

Enzyme and pathway databases

BioCyciARA:GQT-1492-MONOMER.
ARA:GQT-328-MONOMER.
MetaCyc:MONOMER-1621.
BRENDAi3.1.4.11. 399.
ReactomeiREACT_278077. Role of phospholipids in phagocytosis.
REACT_278842. Role of second messengers in netrin-1 signaling.
REACT_279237. VEGFR2 mediated cell proliferation.
REACT_284166. Generation of second messenger molecules.
REACT_286162. PLC beta mediated events.
REACT_306790. GPVI-mediated activation cascade.
REACT_318389. Signaling by FGFR1 fusion mutants.
REACT_328347. DAG and IP3 signaling.
REACT_350143. Synthesis of IP3 and IP4 in the cytosol.

Gene expression databases

ExpressionAtlasiQ39033. baseline and differential.
GenevestigatoriQ39033.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [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 (FEB-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 (FEB-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(2000) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Mol. Cell. Proteomics 2:1234-1243(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. La-0.
  10. "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(2003)
    [AGRICOLA] [Europe PMC]
    Cited for: FUNCTION, LACK OF INDUCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLCD2_ARATH
AccessioniPrimary (citable) accession number: Q39033
Secondary accession number(s): Q56XL3, Q8LG47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.