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Q9STZ3 (PLCD8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoinositide phospholipase C 8
EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase PLC8
Short name=AtPLC8
Short name=PI-PLC8
Gene names
Name:PLC8
Synonyms:PLC2
Ordered Locus Names:At3g47290
ORF Names:T21L8.40
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 length531 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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.6

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Caution

Contains substitutions of several amino acids thought to be essential for catalytic activity. Its enzyme activity is therefore unsure.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Membrane
   Molecular functionHydrolase
Transducer
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: EC

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Phosphoinositide phospholipase C 8
PRO_0000324133

Regions

Domain105 – 247143PI-PLC X-box
Domain267 – 385119PI-PLC Y-box
Domain390 – 496107C2

Experimental info

Sequence conflict821E → K in CAA59962. Ref.1
Sequence conflict3581E → D in CAA59962. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9STZ3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BA4C2C960029771F

FASTA53161,076
        10         20         30         40         50         60 
MLVTRRWESH PANSPDLILQ FFGNEFHGYG DDMPETLRRL TELLGYEKEE DGAGMNAAKK 

        70         80         90        100        110        120 
IAAELNRRKD DIPAFRRLRC LELDQLNEFL FSTKLNPPIG DQVHHDMHAP LSHYFIHTSL 

       130        140        150        160        170        180 
NSYFTGNVFG KYSILPIIEA LEQGVRVVEL DLWPDGRGSI CVRPSWNFEK PLKLQECLDS 

       190        200        210        220        230        240 
IKEHAFTKCT YPLIITFKDG LKPELQSKAT QMIQQTFNHM VYHHDPHSLE VFPSPQQLRN 

       250        260        270        280        290        300 
KILISRRPPK ELLYANDDDG KVGVRNGVEI RQHPADPNYQ SLVSFHVVEP RGMLQNVLTG 

       310        320        330        340        350        360 
KANKIQRPGW YETDIISFTQ KRFLRTRPQR KLLIYAPYKP QRAWMHGAQL IALSRKEEKE 

       370        380        390        400        410        420 
KLWLMQGMFR ANGGCGYVKK PDFLLNAGPS GVFYPTVNPV VVKILKVKIY MGDGWIVDFK 

       430        440        450        460        470        480 
KRIGRLSKPD LYVRISIAGV PHDENIMKTT VKNNEWTPTW GEEFTFPLTY PDLALISFEV 

       490        500        510        520        530 
YDYEVSTADA FCGQTCLPVS ELIEGIRAVP LYDERGKACS STMLLTRFKW S

« Hide

References

« Hide 'large scale' references
[1]Kopka J., Willmitzer L., Mueller-Roeber B.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. C24.
[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]"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.
[6]"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: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X85973 mRNA. Translation: CAA59962.1.
AL096860 Genomic DNA. Translation: CAB51201.1.
CP002686 Genomic DNA. Translation: AEE78261.1.
BT004182 mRNA. Translation: AAO42201.1.
BT005470 mRNA. Translation: AAO63890.1.
IPIIPI00542457.
PIRS54098. T12984.
RefSeqNP_190313.1. NM_114596.3.
UniGeneAt.47563.

3D structure databases

HSSPHSSP built from PDB template 1DJH based on UniProtKB P10688.
ProteinModelPortalQ9STZ3.
SMRQ9STZ3. Positions 36-527.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G47290.1; AT3G47290.1; AT3G47290.
GeneID823882.
KEGGath:AT3G47290.

Organism-specific databases

TAIRAt3g47290.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000244119.
InParanoidQ9STZ3.
PhylomeDBQ9STZ3.
ProtClustDBPLN02223.

Gene expression databases

GenevestigatorQ9STZ3.

Family and domain databases

Gene3D3.20.20.190. 1 hit.
InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR001192. Pinositol_PLipase_C.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 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 namePLCD8_ARATH
AccessionPrimary (citable) accession number: Q9STZ3
Secondary accession number(s): Q42582
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 89 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents