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   27-MAR-2024, entry version 162.
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;
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.Q9SSQ9; -.
DR   iPTMnet; Q9SSQ9; -.
DR   PaxDb; 3702-AT1G52570-1; -.
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; AT1G52570; PLDALPHA2.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_004684_0_0_1; -.
DR   InParanoid; Q9SSQ9; -.
DR   OMA; GERFKVY; -.
DR   OrthoDB; 3014064at2759; -.
DR   PhylomeDB; Q9SSQ9; -.
DR   BioCyc; ARA:AT1G52570-MONOMER; -.
DR   PRO; PR:Q9SSQ9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SSQ9; baseline and differential.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
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; IEA:UniProtKB-EC.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   CDD; cd04015; C2_plant_PLD; 1.
DR   CDD; cd09199; PLDc_pPLDalpha_2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
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; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF115; PHOSPHOLIPASE D ALPHA 2; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   PIRSF; PIRSF036470; PLD_plant; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50035; PLD; 2.
DR   Genevisible; Q9SSQ9; AT.
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
//