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Q9T053 (PLDG1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. 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:
Phospholipase D gamma 1
Short name=AtPLDgamma1
Short name=PLD gamma 1
EC=3.1.4.4
Alternative name(s):
Choline phosphatase
Lecithinase D
Lipophosphodiesterase II
Gene names
Name:PLDGAMMA1
Ordered Locus Names:At4g11850
ORF Names:T26M18.60
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 but prefers ethanolamine-containing lipids 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. Membrane; Peripheral membrane protein. Note: Found mainly associated with intracellular membranes but also with mitochondrial membranes, nuclei and clathrin-coated vesicles. Not found in chloroplast. Ref.5

Tissue specificity

Highly expressed in roots and flowers, moderately in stems, leaves and seedlings and low in siliques. Not detected in seeds.

Induction

Activated by wounding, heavy metal, methyl salicylate, osmotic and salt stresses.

Domain

C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. In PLD gamma, 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.

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.

Sequence caution

The sequence AAB87672.1 differs from that shown. Reason: Frameshift at positions 60, 79, 260, 300, 465 and 758.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 858858Phospholipase D gamma 1
PRO_0000218812

Regions

Domain29 – 147119C2
Domain364 – 39936PLD phosphodiesterase 1
Domain704 – 73128PLD phosphodiesterase 2

Sites

Active site3691 Potential
Active site3711 Potential
Active site3761 Potential
Active site7091 Potential
Active site7111 Potential
Active site7161 Potential

Amino acid modifications

Modified residue6801Phosphoserine Ref.6 Ref.7

Experimental info

Sequence conflict114 – 1152MQ → IE in AAB87672. Ref.1
Sequence conflict3701Q → E in AAB87672. Ref.1
Sequence conflict3771A → S in AAB87672. Ref.1
Sequence conflict634 – 6352MQ → IE in AAB87672. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9T053 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 334AF9DB9E3A7A73

FASTA85895,588
        10         20         30         40         50         60 
MAYHPAYTET MSMGGGSSHG GGQQYVPFAT SSGSLRVELL HGNLDIWVKE AKHLPNMDGF 

        70         80         90        100        110        120 
HNRLGGMLSG LGRKKVEGEK SSKITSDPYV TVSISGAVIG RTFVISNSEN PVWMQHFDVP 

       130        140        150        160        170        180 
VAHSAAEVHF VVKDSDIIGS QIMGAVGIPT EQLCSGNRIE GLFPILNSSG KPCKQGAVLG 

       190        200        210        220        230        240 
LSIQYTPMER MRLYQMGVGS GNECVGVPGT YFPLRKGGRV TLYQDAHVDD GTLPSVHLDG 

       250        260        270        280        290        300 
GIQYRHGKCW EDMADAIRQA RRLIYITGWS VFHPVRLVRR TNDPTEGTLG ELLKVKSQEG 

       310        320        330        340        350        360 
VRVLVLVWDD PTSRSLLGFK TQGVMNTSDE ETRRFFKHSS VQVLLCPRSG GKGHSFIKKS 

       370        380        390        400        410        420 
EVGTIYTHHQ KTVIVDAEAA QNRRKIVAFV GGLDLCNGRF DTPKHPLFRT LKTLHKDDFH 

       430        440        450        460        470        480 
NPNFVTTADD GPREPWHDLH SKIDGPAAYD VLANFEERWM KASKPRGIGK LKSSSDDSLL 

       490        500        510        520        530        540 
RIDRIPDIVG LSEASSANDN DPESWHVQVF RSIDSSSVKG FPKDPKEATG RNLLCGKNIL 

       550        560        570        580        590        600 
IDMSIHAAYV KAIRSAQHFI YIENQYFLGS SFNWDSNKDL GANNLIPMEI ALKIANKIRA 

       610        620        630        640        650        660 
REKFAAYIVI PMWPEGAPTS NPIQRILYWQ HKTMQMMYQT IYKALVEVGL DSQFEPQDFL 

       670        680        690        700        710        720 
NFFCLGTREV PVGTVSVYNS PRKPPQPNAN ANAAQVQALK SRRFMIYVHS KGMVVDDEFV 

       730        740        750        760        770        780 
LIGSANINQR SLEGTRDTEI AMGGYQPHYS WAMKGSRPHG QIFGYRMSLW AEHLGFLEQG 

       790        800        810        820        830        840 
FEEPENMECV RRVRQLSELN WRQYAAEEVT EMSGHLLKYP VQVDRTGKVS SLPGCETFPD 

       850 
LGGKIIGSFL ALQENLTI

« Hide

References

« Hide 'large scale' references
[1]"Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma and regulation of plant PLDgamma, -beta, and -alpha by polyphosphoinositides and calcium."
Qin W., Pappan K., Wang X.
J. Biol. Chem. 272:28267-28273(1997) [PubMed: 9353280] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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.
[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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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.
[6]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, MASS SPECTROMETRY.
Strain: cv. Columbia.
[7]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF027408 mRNA. Translation: AAB87672.1. Frameshift.
AL078606 Genomic DNA. Translation: CAB44323.1.
AL161532 Genomic DNA. Translation: CAB78228.1.
CP002687 Genomic DNA. Translation: AEE83058.1.
AY099569 mRNA. Translation: AAM20421.1.
BT002140 mRNA. Translation: AAN72151.1.
IPIIPI00517388.
PIRT09344.
RefSeqNP_192922.1. NM_117255.2.
UniGeneAt.20523.

3D structure databases

ProteinModelPortalQ9T053.
SMRQ9T053. Positions 34-167.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9T053. 1 interaction.
STRINGQ9T053.

Proteomic databases

PRIDEQ9T053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G11850.1; AT4G11850.1; AT4G11850.
GeneID826791.
GenomeReviewsGene locus AT4G11850 in contig CT486007_GR.
KEGGath:AT4G11850.
NMPDRfig|3702.1.peg.18856.

Organism-specific databases

TAIRAt4g11850.

Phylogenomic databases

eggNOGKOG1329.
GeneTreeEPGT00070000028492.
HOGENOMHBG748198.
InParanoidQ9T053.
OMAQYVPFAT.
PhylomeDBQ9T053.
ProtClustDBCLSN2685536.

Enzyme and pathway databases

BRENDA3.1.4.4. 399.

Gene expression databases

ArrayExpressQ9T053.
GenevestigatorQ9T053.
GermOnlineAT4G11850. Arabidopsis thaliana.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR015679. PLipase_D.
IPR001736. PLipase_D/transphosphatidylase.
IPR024632. PLipase_D_C.
IPR011402. PLipase_D_pln.
[Graphical view]
KOK01115.
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00168. C2. 1 hit.
PF12357. PLD_C. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
PIRSFPIRSF036470. PLD_plant. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLDG1_ARATH
AccessionPrimary (citable) accession number: Q9T053
Secondary accession number(s): O48544
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 93 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