Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9SSQ9 (PLDA2_ARATH)

Last modified November 3, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase D alpha 2
      Short name=PLD alpha 2
      Short name=AtPLDalpha2
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 2
    Phosphatidylcholine-hydrolyzing phospholipase D 2
Gene names
Name: PLDALPHA2
Synonyms: PLD2
Ordered Locus Names: At1g52570
ORF Names: F6D8.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 and response to stress, characterized by acidification of the cell.

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Cofactor

Calcium. Calcium requirement for activity depends on pH. Active either under acidic conditions with micromolar levels of calcium (PIP2-dependent) or at neutral pH with millimolar levels of calcium (PIP2-independent).

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Vacuole. Cytoplasmic vesicleclathrin-coated vesicle. Note: Found in vacuoles and also associated with plasma, microsomal and mitochondrial membranes and in clathrin-coated vesicles. Not found in chloroplast or nuclei. Activation increases association of preexisting enzyme with membranes. The distribution of this conventional PLD between membrane-associated and soluble fractions varied from organ to organ and is calcium-regulated. Ref.2

Tissue specificity

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

Induction

Activated by abscisic acid (ABA), ethylene, heavy metal, cold, salt and osmotic stresses.

Domain

C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. A lower affinity toward calcium can be anticipated for PLD alpha due to the absence of two potential calcium ligands.

Sequence similarities

Belongs to the phospholipase D family. C2-PLD subfamily.

Contains 1 C2 domain.

Contains 2 PLD phosphodiesterase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Phospholipase D alpha 2
PRO_0000218809

Regions

Domain1 – 110110C2
Domain327 – 36539PLD phosphodiesterase 1
Domain656 – 68328PLD phosphodiesterase 2

Sites

Active site3321 Potential
Active site3341 Potential
Active site3391 Potential
Active site6611 Potential
Active site6631 Potential
Active site6681 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SSQ9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F1FA36D8C9CFBCCA

FASTA81091,598
        10         20         30         40         50         60 
MEECLLHGRL HATIYEVDHL HAEGGRSGFL GSILANVEET IGVGKGETQL YATIDLEKAR 

        70         80         90        100        110        120 
VGRTRKITKE PKNPKWFESF HIYCGHMAKH VIFTVKDANP IGATLIGRGY IPVEDILHGE 

       130        140        150        160        170        180 
EVDRWVDILD NEKNPIAGGS KIHVKLQYFG VEKDKNWNRG IKSAKFPGVP YTFFSQRRGC 

       190        200        210        220        230        240 
KVSLYQDAHI PGNFVPKIPL AGGKNYEPHR CWEDIFDAIT NAKHLIYITG WSVYTEISLV 

       250        260        270        280        290        300 
RDSRRPKQGG DVTVGELLKK KASEGVKVIL LVWDDRTSVD LLKKDGLMAT HDEETENFFR 

       310        320        330        340        350        360 
GTDVNCILCP RNPDDGGSIV QNLQISTMFT HHQKIVVVDS EMPSGGSRSR RIVSFVGGLD 

       370        380        390        400        410        420 
LCDGRYDTPF HSLFRTLDTA HHDDFHQPNF TGAAITKGGP REPWHDIHCR LEGPIAWDVL 

       430        440        450        460        470        480 
YNFEQRWSRQ GGKDILVKMR ELGDIIIPPS PVLFSEDHDV WNVQLFRSID GGAAAGFPDS 

       490        500        510        520        530        540 
PEAAAEAGLV SGKDNIIDRS IQDAYIHAIR RAKDFIYIEN QYFLGSSFAW SADGIKPEEI 

       550        560        570        580        590        600 
NALHLIPKEL SLKIVSKIKA GEKFKVYVVV PMWPEGIPES GSVQAILDWQ KRTMEMMYKD 

       610        620        630        640        650        660 
VIKALRENGL EGEDPRDYLT FFCLGNREVK KDGEYEPSEK PEPDTDYIRA QEARRFMIYV 

       670        680        690        700        710        720 
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPY HLSTRQPARG QIHGFRMSLW 

       730        740        750        760        770        780 
YEHLGMLDET FLDPSSQECI QKVNRVADKY WDLYSSESLE HDLPGHLLRY PIGIASEGNI 

       790        800        810 
TELPGCEFFP DTKARILGVK SDYMPPILTT 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [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

AC008016 Genomic DNA. Translation: AAD55607.1.
IPIIPI00542684.
PIRD96566.
RefSeqNP_175666.1.
UniGeneAt.52162

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9SSQ9.

Genome annotation databases

GeneID841689.
GenomeReviewsGene locus AT1G52570 in contig CT485782_GR.
KEGGath:AT1G52570.
NMPDRfig|3702.1.peg.4742.

Organism-specific databases

TAIRAt1g52570.

Phylogenomic databases

OMADAITNAK.

Enzyme and pathway databases

BRENDA3.1.4.4. 302.

Gene expression databases

ArrayExpressQ9SSQ9.
GenevestigatorQ9SSQ9.
GermOnlineAT1G52570. Arabidopsis thaliana.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR015679. Phospholipase_D.
IPR011402. PLD_pln.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00168. C2. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
PIRSFPIRSF036470. PLD_plant. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
PROSITEPS50004. C2. False negative.
PS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLDA2_ARATH
AccessionPrimary (citable) accession number: Q9SSQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents