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Protein

Phosphoinositide phospholipase C 8

Gene

PLC8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

Cofactori

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:AT3G47290-MONOMER.
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 8 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase PLC8
Short name:
AtPLC8
Short name:
PI-PLC8
Gene namesi
Name:PLC8
Synonyms:PLC2
Ordered Locus Names:At3g47290
ORF Names:T21L8.40
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G47290.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Phosphoinositide phospholipase C 8PRO_0000324133Add
BLAST

Expressioni

Tissue specificityi

Expressed in leaves, roots, flowers and siliques.1 Publication

Gene expression databases

GenevestigatoriQ9STZ3.

Interactioni

Protein-protein interaction databases

BioGridi9202. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9STZ3.
SMRiQ9STZ3. Positions 36-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 247143PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini267 – 385119PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini390 – 496107C2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000244119.
InParanoidiQ9STZ3.
PhylomeDBiQ9STZ3.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.20.20.190. 1 hit.
InterProiIPR000008. C2_dom.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. C2. 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.

Q9STZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVTRRWESH PANSPDLILQ FFGNEFHGYG DDMPETLRRL TELLGYEKEE
60 70 80 90 100
DGAGMNAAKK IAAELNRRKD DIPAFRRLRC LELDQLNEFL FSTKLNPPIG
110 120 130 140 150
DQVHHDMHAP LSHYFIHTSL NSYFTGNVFG KYSILPIIEA LEQGVRVVEL
160 170 180 190 200
DLWPDGRGSI CVRPSWNFEK PLKLQECLDS IKEHAFTKCT YPLIITFKDG
210 220 230 240 250
LKPELQSKAT QMIQQTFNHM VYHHDPHSLE VFPSPQQLRN KILISRRPPK
260 270 280 290 300
ELLYANDDDG KVGVRNGVEI RQHPADPNYQ SLVSFHVVEP RGMLQNVLTG
310 320 330 340 350
KANKIQRPGW YETDIISFTQ KRFLRTRPQR KLLIYAPYKP QRAWMHGAQL
360 370 380 390 400
IALSRKEEKE KLWLMQGMFR ANGGCGYVKK PDFLLNAGPS GVFYPTVNPV
410 420 430 440 450
VVKILKVKIY MGDGWIVDFK KRIGRLSKPD LYVRISIAGV PHDENIMKTT
460 470 480 490 500
VKNNEWTPTW GEEFTFPLTY PDLALISFEV YDYEVSTADA FCGQTCLPVS
510 520 530
ELIEGIRAVP LYDERGKACS STMLLTRFKW S
Length:531
Mass (Da):61,076
Last modified:May 1, 2000 - v1
Checksum:iBA4C2C960029771F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821E → K in CAA59962 (Ref. 1) Curated
Sequence conflicti358 – 3581E → D in CAA59962 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT12984. S54098.
RefSeqiNP_190313.1. NM_114596.3.
UniGeneiAt.47563.

Genome annotation databases

EnsemblPlantsiAT3G47290.1; AT3G47290.1; AT3G47290.
GeneIDi823882.
KEGGiath:AT3G47290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT12984. S54098.
RefSeqiNP_190313.1. NM_114596.3.
UniGeneiAt.47563.

3D structure databases

ProteinModelPortaliQ9STZ3.
SMRiQ9STZ3. Positions 36-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9202. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G47290.1; AT3G47290.1; AT3G47290.
GeneIDi823882.
KEGGiath:AT3G47290.

Organism-specific databases

TAIRiAT3G47290.

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000244119.
InParanoidiQ9STZ3.
PhylomeDBiQ9STZ3.

Enzyme and pathway databases

BioCyciARA:AT3G47290-MONOMER.
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

GenevestigatoriQ9STZ3.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.20.20.190. 1 hit.
InterProiIPR000008. C2_dom.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. C2. 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. Kopka J., Willmitzer L., Mueller-Roeber B.
    Submitted (FEB-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.
    , 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. "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.
  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(2003)
    [AGRICOLA] [Europe PMC]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLCD8_ARATH
AccessioniPrimary (citable) accession number: Q9STZ3
Secondary accession number(s): Q42582
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

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

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.