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Q9LY51 (PLCD7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. 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
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 7
EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase PLC7
Short name=AtPLC10
Short name=AtPLC7
Short name=PI-PLC7
Gene names
Name:PLC7
Synonyms:PLC10
Ordered Locus Names:At3g55940
ORF Names:F27K19.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length584 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 By similarity. Ref.3

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 By similarity.

Tissue specificity

Expressed in leaves, roots, flowers and siliques. Ref.3

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LY51-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q9LY51-2)

The sequence of this isoform differs from the canonical sequence as follows:
     212-214: MVT → GNV
     215-584: Missing.
Note: No experimental confirmation available. Potentially inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 584584Phosphoinositide phospholipase C 7
PRO_0000324132

Regions

Domain26 – 10277EF-hand-like
Domain103 – 248146PI-PLC X-box
Domain323 – 439117PI-PLC Y-box
Domain442 – 549108C2
Compositional bias258 – 31255Asp-rich

Sites

Active site1181 By similarity
Active site1641 By similarity

Amino acid modifications

Modified residue2871Phosphoserine Ref.5

Natural variations

Alternative sequence212 – 2143MVT → GNV in isoform 2.
VSP_032149
Alternative sequence215 – 584370Missing in isoform 2.
VSP_032150

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 16A8C5A402A8BA05

FASTA58466,462
        10         20         30         40         50         60 
MSKQTYKVCF CFRRRYRHTV SVAPAEIKTL FDNYSDKGLM TTDLLLRFLI DVQKQDKATK 

        70         80         90        100        110        120 
EEAQDIVNAS SSLLHRNGLH LDAFFKYLFA VTNSPLSSLE VHQDMDAPLS HYFIYTGHNS 

       130        140        150        160        170        180 
YLTGNQLSSD CSELPIIEAL KKGVRVIELD IWPNSDEDGI DVLHGRTLTS PVELIKCLRA 

       190        200        210        220        230        240 
IREHAFDVSD YPVVVTLEDH LTPKLQAKVA EMVTDIFGEM LFTPPSGECL KEFPSPAFLK 

       250        260        270        280        290        300 
KRIMISTKPP KEYKAATDDD LVKKGRDLGD KEVWGREVPS FIRRDRSVDK NDSNGDDDDD 

       310        320        330        340        350        360 
DDDDDDDDDG DDKIKKNAPP EYKHLIAIEA GKPKGGITEC LKVDPDKVRR LSLSEEQLEK 

       370        380        390        400        410        420 
ASEKYAKQIV RFTQRNLLRV YPKGTRITSS NYNPLIAWSH GAQMVAFNMQ GLGRSLWVMQ 

       430        440        450        460        470        480 
GMFRGNGGCG YIKKPDLLLK SNAVFDPEAT LPVKTTLRVT IYMGEGWYYD FPHTHFDRYS 

       490        500        510        520        530        540 
PPDFYTRVGI AGVPADTVMK KTKTLEDNWI PAWDEVFEFP LTVPELALLR IEVHEYDMSE 

       550        560        570        580 
KDDFGGQICL PVWELRQGIR AVPLRNQDGV KCRSVKLLVR LEFV

« Hide

Isoform 2 [UniParc].

Checksum: 64CD6BEAD25205DB
Show »

FASTA21424,243

References

« Hide 'large scale' references
[1]"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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[4]"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.
[5]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, MASS SPECTROMETRY.
Strain: cv. La-0.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL163832 Genomic DNA. Translation: CAB87848.1.
CP002686 Genomic DNA. Translation: AEE79459.1.
IPIIPI00524623.
IPI00889355.
PIRT49206.
RefSeqNP_191153.1. NM_115452.1.
UniGeneAt.53946.

3D structure databases

HSSPHSSP built from PDB template 1DJH based on UniProtKB P10688.
ProteinModelPortalQ9LY51.
SMRQ9LY51. Positions 25-236, 352-581.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT3G55940.1-P.

Proteomic databases

PaxDbQ9LY51.
PRIDEQ9LY51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55940.1; AT3G55940.1; AT3G55940.
GeneID824760.
KEGGath:AT3G55940.

Organism-specific databases

TAIRAt3g55940.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000244119.
InParanoidQ9LY51.
KOK05857.
OMASITEGTW.
PhylomeDBQ9LY51.
ProtClustDBPLN02222.

Gene expression databases

GenevestigatorQ9LY51.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. 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]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. efhand_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. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLCD7_ARATH
AccessionPrimary (citable) accession number: Q9LY51
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents