Reviewed, UniProtKB/Swiss-Prot Q56W08 (PLCD3_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphoinositide phospholipase C 3
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase PLC3
      Short name=PI-PLC3
      Short name=AtPLC3
      Short name=AtPLC1F

Gene names

Name:	PLC3
Synonyms:	ATPLC1
Ordered Locus Names:	At4g38530
ORF Names:	F20M13.90

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.5
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 and siliques, but not in flowers. Ref.5
Induction	Not induced by environmental stresses such as dehydration, salinity and low temperature. Ref.4
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.
Sequence caution	The sequence AAC48991.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC48991.1 differs from that shown. Reason: Frameshift at positions 535 and 543. The sequence CAB37509.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80517.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Membrane
Molecular function	Hydrolase Transducer
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphoinositide 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 564	564	Phosphoinositide phospholipase C 3		PRO_0000324128
Regions
	Domain	19 – 54	36	EF-hand
	Domain	106 – 250	145	PI-PLC X-box
	Domain	296 – 412	117	PI-PLC Y-box
	Domain	415 – 523	109	C2
	Compositional bias	67 – 82	16	His-rich
Sites
	Active site	121	1	By similarity
	Active site	167	1	By similarity
Experimental info
	Sequence conflict	526	1	L → R in AAC48991. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q56W08-1 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 6EA1067C8864345A	FASTA	564	64,944
	10 20 30 40 50 60 MSESFKVCFC CSRSFKEKTR QPPVSIKRLF EAYSRNGKMS FDELLRFVSE VQGERHAGLD 70 80 90 100 110 120 YVQDIFHSVK HHNVFHHHGL VHLNAFYRYL FSDTNSPLPM SGQVHHDMKA PLSHYFVYTG 130 140 150 160 170 180 HNSYLTGNQV NSRSSVEPIV QALRKGVKVI ELDLWPNPSG NAAEVRHGRT LTSHEDLQKC 190 200 210 220 230 240 LTAIKDNAFH VSDYPVIITL EDHLPPKLQA QVAKMLTKTY RGMLFRRVSE SFKHFPSPEE 250 260 270 280 290 300 LKGKILISTK PPKEYLESKT VHTTRTPTVK ETSWNRVANK ILEEYKDMES EAVGYRDLIA 310 320 330 340 350 360 IHAANCKDPS KDCLSDDPEK PIRVSMDEQW LDTMVRTRGT DLVRFTQRNL VRIYPKGTRV 370 380 390 400 410 420 DSSNYDPHVG WTHGAQMVAF NMQGHGKQLW IMQGMFRGNG GCGYVKKPRI LLDEHTLFDP 430 440 450 460 470 480 CKRFPIKTTL KVKIYTGEGW DLDFHHTHFD QYSPPDFFVK IGIAGVPRDT VSYRTETAVD 490 500 510 520 530 540 QWFPIWGNDE FLFQLSVPEL ALLWFKVQDY DNDTQNDFAG QTCLPLPELK SGVRAVRLHD 550 560 RTGKAYKNTR LLVSFALDPP YTFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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(1995) [PubMed: 7716237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-564. Strain: cv. Landsberg erecta. Tissue: Shoot.
[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: 12226484] [Abstract] Cited for: GENE FAMILY, LACK OF INDUCTION, NOMENCLATURE.
[5]	"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: IND43668249] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL035540 Genomic DNA. Translation: CAB37509.1. Sequence problems. AL161593 Genomic DNA. Translation: CAB80517.1. Sequence problems. AK222239 mRNA. Translation: BAD95426.1. U13203 mRNA. Translation: AAC48991.1. Sequence problems.
IPI	IPI00534505.
PIR	T05681.
RefSeq	NP_195565.2.
UniGene	At.2775
3D structure databases
HSSP	HSSP built from PDB template 1QAS based on UniProtKB P10688.
ModBase	Search...
Genome annotation databases
GeneID	830010.
GenomeReviews	Gene locus AT4G38530 in contig CT486007_GR.
KEGG	ath:AT4G38530.
Organism-specific databases
TAIR	At4g38530.
Phylogenomic databases
OMA	QGHESEG.
Enzyme and pathway databases
BRENDA	3.1.4.11. 302.
Gene expression databases
Genevestigator	Q56W08.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR000909. Phospholipase_C_Pinositol-sp_X. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. [Graphical view]
Gene3D	G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
ProDom	PD001202. PI_PLC_Y. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
PROSITE	PS50004. C2. 1 hit. PS50222. EF_HAND_2. False negative. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLCD3_ARATH

Accession

Primary (citable) accession number: Q56W08
Secondary accession number(s): Q38811, Q9SZN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 10, 2005
Last modified:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)