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Protein

Phosphoinositide phospholipase C 3

Gene

PLC3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

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 sitei121 – 1211PROSITE-ProRule annotation
Active sitei167 – 1671PROSITE-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:AT4G38530-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 3 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase PLC3
Short name:
AtPLC1F
Short name:
AtPLC3
Short name:
PI-PLC3
Gene namesi
Name:PLC3
Synonyms:ATPLC1
Ordered Locus Names:At4g38530
ORF Names:F20M13.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G38530.

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 – 564564Phosphoinositide phospholipase C 3PRO_0000324128Add
BLAST

Proteomic databases

PRIDEiQ56W08.

Expressioni

Tissue specificityi

Expressed in leaves, roots and siliques, but not in flowers.1 Publication

Inductioni

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

Gene expression databases

GenevestigatoriQ56W08.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G38530.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ56W08.
SMRiQ56W08. Positions 26-557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436EF-handAdd
BLAST
Domaini106 – 250145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini296 – 412117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini415 – 523109C2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi67 – 8216His-richAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand 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.
InParanoidiQ56W08.
KOiK05857.
OMAiIAIHAAN.
PhylomeDBiQ56W08.

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.

Q56W08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESFKVCFC CSRSFKEKTR QPPVSIKRLF EAYSRNGKMS FDELLRFVSE
60 70 80 90 100
VQGERHAGLD YVQDIFHSVK HHNVFHHHGL VHLNAFYRYL FSDTNSPLPM
110 120 130 140 150
SGQVHHDMKA PLSHYFVYTG HNSYLTGNQV NSRSSVEPIV QALRKGVKVI
160 170 180 190 200
ELDLWPNPSG NAAEVRHGRT LTSHEDLQKC LTAIKDNAFH VSDYPVIITL
210 220 230 240 250
EDHLPPKLQA QVAKMLTKTY RGMLFRRVSE SFKHFPSPEE LKGKILISTK
260 270 280 290 300
PPKEYLESKT VHTTRTPTVK ETSWNRVANK ILEEYKDMES EAVGYRDLIA
310 320 330 340 350
IHAANCKDPS KDCLSDDPEK PIRVSMDEQW LDTMVRTRGT DLVRFTQRNL
360 370 380 390 400
VRIYPKGTRV DSSNYDPHVG WTHGAQMVAF NMQGHGKQLW IMQGMFRGNG
410 420 430 440 450
GCGYVKKPRI LLDEHTLFDP CKRFPIKTTL KVKIYTGEGW DLDFHHTHFD
460 470 480 490 500
QYSPPDFFVK IGIAGVPRDT VSYRTETAVD QWFPIWGNDE FLFQLSVPEL
510 520 530 540 550
ALLWFKVQDY DNDTQNDFAG QTCLPLPELK SGVRAVRLHD RTGKAYKNTR
560
LLVSFALDPP YTFR
Length:564
Mass (Da):64,944
Last modified:May 9, 2005 - v1
Checksum:i6EA1067C8864345A
GO

Sequence cautioni

The sequence AAC48991.1 differs from that shown. Reason: Frameshift at positions 535 and 543. Curated
The sequence AAC48991.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB37509.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB80517.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261L → R in AAC48991 (PubMed:7716237).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035540 Genomic DNA. Translation: CAB37509.1. Sequence problems.
AL161593 Genomic DNA. Translation: CAB80517.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86943.1.
AK222239 mRNA. Translation: BAD95426.1.
U13203 mRNA. Translation: AAC48991.1. Sequence problems.
PIRiT05681.
RefSeqiNP_195565.2. NM_120014.4.
UniGeneiAt.2775.

Genome annotation databases

EnsemblPlantsiAT4G38530.1; AT4G38530.1; AT4G38530.
GeneIDi830010.
KEGGiath:AT4G38530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035540 Genomic DNA. Translation: CAB37509.1. Sequence problems.
AL161593 Genomic DNA. Translation: CAB80517.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86943.1.
AK222239 mRNA. Translation: BAD95426.1.
U13203 mRNA. Translation: AAC48991.1. Sequence problems.
PIRiT05681.
RefSeqiNP_195565.2. NM_120014.4.
UniGeneiAt.2775.

3D structure databases

ProteinModelPortaliQ56W08.
SMRiQ56W08. Positions 26-557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G38530.1-P.

Proteomic databases

PRIDEiQ56W08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G38530.1; AT4G38530.1; AT4G38530.
GeneIDi830010.
KEGGiath:AT4G38530.

Organism-specific databases

TAIRiAT4G38530.

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000244119.
InParanoidiQ56W08.
KOiK05857.
OMAiIAIHAAN.
PhylomeDBiQ56W08.

Enzyme and pathway databases

BioCyciARA:AT4G38530-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

GenevestigatoriQ56W08.

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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "An Arabidopsis cDNA related to animal phosphoinositide-specific phospholipase C genes."
    Yamamoto Y.T., Conkling M.A., Sussex I.M., Irish V.F.
    Plant Physiol. 107:1029-1030(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-564.
    Strain: cv. Landsberg erecta.
    Tissue: Shoot.
  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, LACK OF INDUCTION, 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: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLCD3_ARATH
AccessioniPrimary (citable) accession number: Q56W08
Secondary accession number(s): Q38811, Q9SZN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 17, 2008
Last sequence update: May 9, 2005
Last modified: March 31, 2015
This is version 88 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.