PLDA2_ARATH
ID PLDA2_ARATH Reviewed; 810 AA.
AC Q9SSQ9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Phospholipase D alpha 2 {ECO:0000303|PubMed:11891260};
DE Short=AtPLDalpha2 {ECO:0000303|PubMed:11891260};
DE Short=PLD alpha 2 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000250|UniProtKB:Q38882};
DE AltName: Full=Choline phosphatase 2;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 2;
GN Name=PLDALPHA2 {ECO:0000303|PubMed:11891260}; Synonyms=PLD2;
GN OrderedLocusNames=At1g52570 {ECO:0000312|Araport:AT1G52570};
GN ORFNames=F6D8.21 {ECO:0000312|EMBL:AAD55607.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10198096; DOI=10.1104/pp.119.4.1371;
RA Fan L., Zheng S., Cui D., Wang X.;
RT "Subcellular distribution and tissue expression of phospholipase Dalpha,
RT Dbeta, and Dgamma in Arabidopsis.";
RL Plant Physiol. 119:1371-1378(1999).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11891260; DOI=10.1104/pp.010928;
RA Qin C., Wang X.;
RT "The Arabidopsis phospholipase D family. Characterization of a calcium-
RT independent and phosphatidylcholine-selective PLD zeta 1 with distinct
RT regulatory domains.";
RL Plant Physiol. 128:1057-1068(2002).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA). Plays an
CC important role in various cellular processes, including phytohormone
CC action and response to stress, characterized by acidification of the
CC cell. {ECO:0000250|UniProtKB:Q38882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000250|UniProtKB:Q38882};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q38882};
CC Note=Ca(2+) requirement for activity depends on pH. Active either under
CC acidic conditions with micromolar levels of calcium (PIP2-dependent) or
CC at neutral pH with millimolar levels of calcium (PIP2-independent).
CC {ECO:0000250|UniProtKB:Q38882};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096}. Membrane
CC {ECO:0000269|PubMed:10198096}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10198096}. Vacuole {ECO:0000269|PubMed:10198096}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:10198096}. Note=Found in vacuoles and also
CC associated with plasma, microsomal and mitochondrial membranes and in
CC clathrin-coated vesicles. Not found in chloroplast or nuclei.
CC Activation increases association of preexisting enzyme with membranes.
CC The distribution of this conventional PLD between membrane-associated
CC and soluble fractions varied from organ to organ and is calcium-
CC regulated.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, stems and flowers,
CC moderately in leaves, seedlings and siliques. Not detected in dry
CC seeds. {ECO:0000269|PubMed:10198096}.
CC -!- INDUCTION: Activated by abscisic acid (ABA), ethylene, heavy metal,
CC cold, salt and osmotic stresses.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. A lower affinity toward calcium
CC can be anticipated for PLD alpha due to the absence of two potential
CC calcium ligands. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; AC008016; AAD55607.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32825.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60648.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60649.1; -; Genomic_DNA.
DR PIR; D96566; D96566.
DR RefSeq; NP_001322920.1; NM_001333554.1.
DR RefSeq; NP_001322921.1; NM_001333553.1.
DR RefSeq; NP_175666.1; NM_104135.3.
DR AlphaFoldDB; Q9SSQ9; -.
DR SMR; Q9SSQ9; -.
DR BioGRID; 26914; 1.
DR STRING; 3702.AT1G52570.1; -.
DR iPTMnet; Q9SSQ9; -.
DR PaxDb; Q9SSQ9; -.
DR PRIDE; Q9SSQ9; -.
DR ProteomicsDB; 235040; -.
DR EnsemblPlants; AT1G52570.1; AT1G52570.1; AT1G52570.
DR EnsemblPlants; AT1G52570.2; AT1G52570.2; AT1G52570.
DR EnsemblPlants; AT1G52570.3; AT1G52570.3; AT1G52570.
DR GeneID; 841689; -.
DR Gramene; AT1G52570.1; AT1G52570.1; AT1G52570.
DR Gramene; AT1G52570.2; AT1G52570.2; AT1G52570.
DR Gramene; AT1G52570.3; AT1G52570.3; AT1G52570.
DR KEGG; ath:AT1G52570; -.
DR Araport; AT1G52570; -.
DR TAIR; locus:2035211; AT1G52570.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; Q9SSQ9; -.
DR OMA; NRVADKY; -.
DR OrthoDB; 128697at2759; -.
DR PhylomeDB; Q9SSQ9; -.
DR BioCyc; ARA:AT1G52570-MON; -.
DR PRO; PR:Q9SSQ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSQ9; baseline and differential.
DR Genevisible; Q9SSQ9; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Calcium; Cytoplasm; Cytoplasmic vesicle;
KW Ethylene signaling pathway; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Repeat; Vacuole.
FT CHAIN 1..810
FT /note="Phospholipase D alpha 2"
FT /id="PRO_0000218809"
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 327..365
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 656..683
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 332
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 521
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 661
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 810 AA; 91598 MW; F1FA36D8C9CFBCCA CRC64;
MEECLLHGRL HATIYEVDHL HAEGGRSGFL GSILANVEET IGVGKGETQL YATIDLEKAR
VGRTRKITKE PKNPKWFESF HIYCGHMAKH VIFTVKDANP IGATLIGRGY IPVEDILHGE
EVDRWVDILD NEKNPIAGGS KIHVKLQYFG VEKDKNWNRG IKSAKFPGVP YTFFSQRRGC
KVSLYQDAHI PGNFVPKIPL AGGKNYEPHR CWEDIFDAIT NAKHLIYITG WSVYTEISLV
RDSRRPKQGG DVTVGELLKK KASEGVKVIL LVWDDRTSVD LLKKDGLMAT HDEETENFFR
GTDVNCILCP RNPDDGGSIV QNLQISTMFT HHQKIVVVDS EMPSGGSRSR RIVSFVGGLD
LCDGRYDTPF HSLFRTLDTA HHDDFHQPNF TGAAITKGGP REPWHDIHCR LEGPIAWDVL
YNFEQRWSRQ GGKDILVKMR ELGDIIIPPS PVLFSEDHDV WNVQLFRSID GGAAAGFPDS
PEAAAEAGLV SGKDNIIDRS IQDAYIHAIR RAKDFIYIEN QYFLGSSFAW SADGIKPEEI
NALHLIPKEL SLKIVSKIKA GEKFKVYVVV PMWPEGIPES GSVQAILDWQ KRTMEMMYKD
VIKALRENGL EGEDPRDYLT FFCLGNREVK KDGEYEPSEK PEPDTDYIRA QEARRFMIYV
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPY HLSTRQPARG QIHGFRMSLW
YEHLGMLDET FLDPSSQECI QKVNRVADKY WDLYSSESLE HDLPGHLLRY PIGIASEGNI
TELPGCEFFP DTKARILGVK SDYMPPILTT
