Reviewed, UniProtKB/Swiss-Prot O23078 (PLDB2_ARATH)

Names and origin

Protein names

Recommended name:
    Phospholipase D beta 2
      Short name=AtPLDbeta2
      Short name=PLD beta 2
    EC=3.1.4.4
Alternative name(s):
    PLDdelta1

Gene names

Name:	PLDBETA2
Ordered Locus Names:	At4g00240
ORF Names:	F5I10.13, A_IG005I10.13

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	915 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine or N-acylphosphatidylethanolamine as substrates.
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Cofactor	Calcium. Requires micromolar level (PIP2-dependent).
Enzyme regulation	Inhibited by neomycin.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Tissue specificity	Expressed in stems, and to a lower amount in leaves, flowers and siliques.
Induction	Activated by wounding, methyl jasmonate, heavy metal, osmotic and salt stresses.
Domain	C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. In PLD beta, all the calcium-coordinating acidic amino-acids are conserved.
Sequence similarities	Belongs to the phospholipase D family. C2-PLD subfamily. Contains 1 C2 domain. Contains 2 PLD phosphodiesterase domains.
Sequence caution	The sequence AAB62845.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAF02803.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80782.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylcholine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase D activity Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 915	915	Phospholipase D beta 2		PRO_0000218811
Regions
	Domain	104 – 221	118	C2
	Domain	439 – 474	36	PLD phosphodiesterase 1
	Domain	761 – 788	28	PLD phosphodiesterase 2
	Compositional bias	57 – 63	7	Poly-Pro
Sites
	Active site	444	1	Potential
	Active site	446	1	Potential
	Active site	451	1	Potential
	Active site	766	1	Potential
	Active site	768	1	Potential
	Active site	773	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	O23078-1 [UniParc]. Last modified April 3, 2002. Version 2. Checksum: 4D7B827002BB1D03	FASTA	915	102,820
	10 20 30 40 50 60 MENYGWNYPY YPYRPPRPNP PYPAPPHHHG SMSHSGPLDH HHPPMSYYAS FDYQHQPPPP 70 80 90 100 110 120 YPPVSYYASF SSHSDLSYSG RLDSSGHGFT STASPHSPGM HIVPFGKASL KVLLLHGNLD 130 140 150 160 170 180 IWVSCANNLP NLDLFHKTLG VVFGGMTNMI EGQLSKKITS DPYVSISVAG AVIGRTYVIS 190 200 210 220 230 240 NSENPVWQQH FYVPVAHHAA EVHFVVKDSD AVGSQLIGIV TIPVEQIYSG ARIEGTYSIR 250 260 270 280 290 300 DSNGKPCKPG ATLSLSIQYT SMNKLSVYHS GVGAGPYYQG VPGTYFPLRE GGSVTLYQDA 310 320 330 340 350 360 HVPEGMLPGI KLGNGMCYEH GKCWHDMFHA ICQARRLIYI TGWSVWHNVR LVRDKEDPSS 370 380 390 400 410 420 ECRLGELLRS KSQEGVRVLL LVWDDPTSQN ILGYMTDGVM GTHDEETRRF FKDSSVQVLL 430 440 450 460 470 480 CPRNAGKRHS WVKQREVGTI YTHHQKNLIV DADAGGNRRK IVAFVGGLDL CDGRYDTPQH 490 500 510 520 530 540 PLFRTLQTDH NGDYHNPTFT GNVSGCPREP WHDLHSKIDG PAAYDVLTNF EERWLKAAKP 550 560 570 580 590 600 HRINKLKTSY DDALLRIDRI PDILRVLDAP TIFRSIDSNS VKGFPKDPKY ATSKNLVCGK 610 620 630 640 650 660 NVLIDMSIHT AYVKAIRAAQ HFIYIENQYF IGSSYDWNAH KDIGANNLIP MEIALKIADK 670 680 690 700 710 720 IRAKERFAAY IVIPMWPEGV PTGAATQRIL YWQHKTMQMM YGTIYNALVE AGLEDEYSPQ 730 740 750 760 770 780 DYLNFFCLGN REMVNGNNES GTGSASNENT PQGLCRKSRR FMIYVHSKGM VVDDEYVVIG 790 800 810 820 830 840 SANINQRSME GTRDTEIAMG AYQPQHTWAR RQSGPRGQIY GYRMSLWAEH MALLDDCFVE 850 860 870 880 890 900 PESLGCVRKV RTVAEENWEQ FRSEEVSEMR GHLMKYPVEV DRKGKVRPLP GSEEFPDVGG 910 NVVGSFLAIQ ENLTI

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]	"Subcellular distribution and tissue expression of phospholipase Dalpha, Dbeta, and Dgamma in Arabidopsis." Fan L., Zheng S., Cui D., Wang X. Plant Physiol. 119:1371-1378(1999) [PubMed: 10198096] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF013293 Genomic DNA. Translation: AAB62845.1. Sequence problems. AF195115 Genomic DNA. Translation: AAF02803.1. Sequence problems. AL161471 Genomic DNA. Translation: CAB80782.1. Sequence problems.
IPI	IPI00529186.
3D structure databases
ModBase	Search...
Genome annotation databases
GenomeReviews	Gene locus AT4G00240 in contig CT486007_GR.
Organism-specific databases
TAIR	At4g00240.
Enzyme and pathway databases
BRENDA	3.1.4.4. 302.
Gene expression databases
ArrayExpress	O23078.
Genevestigator	O23078.
GermOnline	AT4G00240. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR015679. Phospholipase_D. IPR011402. PLD_pln. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00168. C2. 1 hit. PF00614. PLDc. 2 hits. [Graphical view]
PIRSF	PIRSF036470. PLD_plant. 1 hit.
SMART	SM00239. C2. 1 hit. SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS50004. C2. 1 hit. PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLDB2_ARATH

Accession

Primary (citable) accession number: O23078

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	April 3, 2002
Last modified:	October 13, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)