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Q39033 (PLCD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Protein existenceEvidence 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.10

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.10

Induction

Not induced by environmental stresses such as dehydration, salinity and low temperature. Ref.1 Ref.10

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 581581Phosphoinositide phospholipase C 2
PRO_0000324127

Regions

Domain26 – 10277EF-hand-like
Domain103 – 248146PI-PLC X-box
Domain317 – 433117PI-PLC Y-box
Domain439 – 546108C2
Compositional bias291 – 30616Asp-rich

Sites

Active site1181 By similarity
Active site1641 By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E337EB95EC16FC0B

FASTA58166,122
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"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(2003) [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(2004) [AGRICOLA] [Europe PMC]
Cited for: FUNCTION, LACK OF INDUCTION, TISSUE SPECIFICITY.
+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.
PIRS71170.
RefSeqNP_001030660.1. NM_001035583.1. [Q39033-1]
NP_187464.1. NM_111686.5. [Q39033-1]
UniGeneAt.20554.

3D structure databases

ProteinModelPortalQ39033.
SMRQ39033. Positions 26-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ39033. 1 interaction.

Proteomic databases

PaxDbQ39033.
PRIDEQ39033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G08510.1; AT3G08510.1; AT3G08510. [Q39033-1]
AT3G08510.2; AT3G08510.2; AT3G08510. [Q39033-1]
GeneID819999.
KEGGath:AT3G08510.

Organism-specific databases

TAIRAT3G08510.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000244119.
InParanoidQ39033.
KOK05857.
OMADRCFSII.
PhylomeDBQ39033.

Enzyme and pathway databases

BioCycARA:GQT-1492-MONOMER.
ARA:GQT-328-MONOMER.
MetaCyc:MONOMER-1621.
BRENDA3.1.4.11. 399.

Gene expression databases

ArrayExpressQ39033.
GenevestigatorQ39033.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. 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]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLCD2_ARATH
AccessionPrimary (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: June 11, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names