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Phospholipase D alpha 1 (AtPLDalpha1) (PLD alpha 1) (EC 3.1.4.4) (Choline phosphatase 1) (PLDalpha) (Phosphatidylcholine-hydrolyzing phospholipase D 1)

 PLDA1_ARATH             Reviewed;         810 AA.
Q38882; Q0WV84; Q944M4; Q9LW06;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
25-OCT-2017, entry version 150.
RecName: Full=Phospholipase D alpha 1 {ECO:0000303|PubMed:11891260};
Short=AtPLDalpha1 {ECO:0000303|PubMed:11891260};
Short=PLD alpha 1 {ECO:0000303|PubMed:11891260};
EC=3.1.4.4 {ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:9353280};
AltName: Full=Choline phosphatase 1;
AltName: Full=PLDalpha {ECO:0000303|PubMed:11891260};
AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
Name=PLDALPHA1 {ECO:0000303|PubMed:11891260}; Synonyms=PLD1;
OrderedLocusNames=At3g15730 {ECO:0000312|Araport:AT3G15730};
ORFNames=MSJ11.13 {ECO:0000312|EMBL:BAB02304.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Dyer J.H., Zheng L., Wang X.;
"Cloning and nucleotide sequence of a cDNA encoding phospholipase D
from Arabidopsis.";
(er) Plant Gene Register PGR95-096(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-810.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.,
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
CATALYTIC ACTIVITY, COFACTOR, AND ENZYME REGULATION.
PubMed=9353280; DOI=10.1074/jbc.272.45.28267;
Qin W., Pappan K., Wang X.;
"Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma
and regulation of plant PLDgamma, -beta, and -alpha by
polyphosphoinositides and calcium.";
J. Biol. Chem. 272:28267-28273(1997).
[7]
FUNCTION, AND INDUCTION BY ABSCISIC ACID AND ETHYLENE.
PubMed=9437863; DOI=10.1105/tpc.9.12.2183;
Fan L., Zheng S., Wang X.;
"Antisense suppression of phospholipase D alpha retards abscisic
acid- and ethylene-promoted senescence of postharvest Arabidopsis
leaves.";
Plant Cell 9:2183-2196(1997).
[8]
SUBSTRATE SPECIFICITY.
PubMed=9578608; DOI=10.1006/abbi.1998.0640;
Pappan K., Austin-Brown S., Chapman K.D., Wang X.;
"Substrate selectivities and lipid modulation of plant phospholipase D
alpha, -beta, and -gamma.";
Arch. Biochem. Biophys. 353:131-140(1998).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10441386; DOI=10.1006/abbi.1999.1325;
Pappan K., Wang X.;
"Plant phospholipase Dalpha is an acidic phospholipase active at near-
physiological Ca(2+) concentrations.";
Arch. Biochem. Biophys. 368:347-353(1999).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10198096; DOI=10.1104/pp.119.4.1371;
Fan L., Zheng S., Cui D., Wang X.;
"Subcellular distribution and tissue expression of phospholipase
Dalpha, Dbeta, and Dgamma in Arabidopsis.";
Plant Physiol. 119:1371-1378(1999).
[11]
DOMAIN, AND 3D-STRUCTURE MODELING.
PubMed=10777500; DOI=10.1074/jbc.M001945200;
Zheng L., Krishnamoorthi R., Zolkiewski M., Wang X.;
"Distinct Ca2+ binding properties of novel C2 domains of plant
phospholipase dalpha and beta.";
J. Biol. Chem. 275:19700-19706(2000).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11090221; DOI=10.1105/tpc.12.11.2237;
Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.;
"Involvement of phospholipase D in wound-induced accumulation of
jasmonic acid in arabidopsis.";
Plant Cell 12:2237-2246(2000).
[13]
FUNCTION.
PubMed=11239826; DOI=10.1016/S1388-1981(01)00091-9;
Zien C.A., Wang C., Wang X., Welti R.;
"In vivo substrates and the contribution of the common phospholipase
D, PLDalpha, to wound-induced metabolism of lipids in Arabidopsis.";
Biochim. Biophys. Acta 1530:236-248(2001).
[14]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=11706190; DOI=10.1104/pp.127.3.1102;
Wang C., Wang X.;
"A novel phospholipase d of Arabidopsis that is activated by oleic
acid and associated with the plasma membrane.";
Plant Physiol. 127:1102-1112(2001).
[15]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11891260; DOI=10.1104/pp.010928;
Qin C., Wang X.;
"The Arabidopsis phospholipase D family. Characterization of a
calcium-independent and phosphatidylcholine-selective PLD zeta 1 with
distinct regulatory domains.";
Plant Physiol. 128:1057-1068(2002).
[16]
FUNCTION, INTERACTION WITH GPA1, AND MUTAGENESIS OF GLU-563; LYS-564
AND PHE-565.
PubMed=14594812; DOI=10.1074/jbc.M309529200;
Zhao J., Wang X.;
"Arabidopsis phospholipase Dalpha1 interacts with the heterotrimeric
G-protein alpha-subunit through a motif analogous to the DRY motif in
G-protein-coupled receptors.";
J. Biol. Chem. 279:1794-1800(2004).
[17]
FUNCTION.
PubMed=16949955; DOI=10.1016/j.jplph.2005.08.006;
Rajashekar C.B., Zhou H.E., Zhang Y., Li W., Wang X.;
"Suppression of phospholipase Dalpha1 induces freezing tolerance in
Arabidopsis: response of cold-responsive genes and osmolyte
accumulation.";
J. Plant Physiol. 163:916-926(2006).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GPA1.
PubMed=16614222; DOI=10.1126/science.1123769;
Mishra G., Zhang W., Deng F., Zhao J., Wang X.;
"A bifurcating pathway directs abscisic acid effects on stomatal
closure and opening in Arabidopsis.";
Science 312:264-266(2006).
[19]
FUNCTION.
PubMed=17261695; DOI=10.1093/jxb/erl262;
Mane S.P., Vasquez-Robinet C., Sioson A.A., Heath L.S., Grene R.;
"Early PLDalpha-mediated events in response to progressive drought
stress in Arabidopsis: a transcriptome analysis.";
J. Exp. Bot. 58:241-252(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17565616; DOI=10.1111/j.1365-313X.2007.03103.x;
Devaiah S.P., Pan X., Hong Y., Roth M., Welti R., Wang X.;
"Enhancing seed quality and viability by suppressing phospholipase D
in Arabidopsis.";
Plant J. 50:950-957(2007).
[22]
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=19017627; DOI=10.1093/pcp/pcn173;
Bargmann B.O., Laxalt A.M., ter Riet B., van Schooten B., Merquiol E.,
Testerink C., Haring M.A., Bartels D., Munnik T.;
"Multiple PLDs required for high salinity and water deficit tolerance
in plants.";
Plant Cell Physiol. 50:78-89(2009).
[23]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23150630; DOI=10.1105/tpc.112.104182;
Zhang Q., Lin F., Mao T., Nie J., Yan M., Yuan M., Zhang W.;
"Phosphatidic acid regulates microtubule organization by interacting
with MAP65-1 in response to salt stress in Arabidopsis.";
Plant Cell 24:4555-4576(2012).
[24]
FUNCTION, INDUCTION BY ABSCISIC ACID, AND DISRUPTION PHENOTYPE.
PubMed=22392280; DOI=10.1104/pp.112.195578;
Uraji M., Katagiri T., Okuma E., Ye W., Hossain M.A., Masuda C.,
Miura A., Nakamura Y., Mori I.C., Shinozaki K., Murata Y.;
"Cooperative function of PLDdelta and PLDalpha1 in abscisic acid-
induced stomatal closure in Arabidopsis.";
Plant Physiol. 159:450-460(2012).
[25]
INTERACTION WITH GPA1.
PubMed=23913032; DOI=10.1007/978-1-62703-532-3_3;
Zhao J., Wang X.;
"Biochemical analysis of the interaction between phospholipase Dalpha1
and GTP-binding protein alpha-subunit from Arabidopsis thaliana.";
Methods Mol. Biol. 1043:21-35(2013).
-!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
phosphodiesteric bond to generate phosphatidic acids (PA). Plays
an important role in various cellular processes, including
phytohormone action and response to stress, characterized by
acidification of the cell (PubMed:9437863). Involved in wound
induction of jasmonic acid (PubMed:11090221). May be involved in
membrane lipid remodeling (PubMed:11239826). Probably involved in
freezing tolerance by modulating the cold-responsive genes and
accumulation of osmolytes (PubMed:16949955). Can use
phosphatidylcholine (PC), phosphatidylethanolamine (PE) and
phosphatidylglycerol (PG) as substrates, both in presence or in
absence of PIP2 (PubMed:9578608). Its main substrate is
phosphatidylcholine (PubMed:11239826). Stimulates the intrinsic
GTPase activity of GPA1 upon binding (PubMed:14594812). Mediates
the abscisic acid effects on stomata through interaction with GPA1
and the production of phosphatidic acid that bind to ABI1
(PubMed:17261695, PubMed:17565616). Involved in seed aging and
deterioration (PubMed:17565616). Involved in microtubule
stabilization and salt tolerance (PubMed:23150630). Involved in
abscisic acid-induced stomatal closure (PubMed:22392280).
{ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:11090221,
ECO:0000269|PubMed:11239826, ECO:0000269|PubMed:14594812,
ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:16949955,
ECO:0000269|PubMed:17261695, ECO:0000269|PubMed:17565616,
ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:23150630,
ECO:0000269|PubMed:9437863, ECO:0000269|PubMed:9578608}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate. {ECO:0000269|PubMed:10441386,
ECO:0000269|PubMed:9353280}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:9353280};
Note=Ca(2+) 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). {ECO:0000269|PubMed:9353280};
-!- ENZYME REGULATION: Not inhibited by neomycin.
{ECO:0000269|PubMed:9353280}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 4.5 to 5.0 in the presence of micromolar levels of
Ca(2+) and PIP2. Optimum pH is 5.5 to 6.5 in the presence of
millimolar levels of Ca(2+). {ECO:0000269|PubMed:10441386};
-!- SUBUNIT: Interacts with GPA1 (PubMed:14594812, PubMed:16614222,
PubMed:23913032). This binding inhibits PLDALPHA1 activity and is
relieved by GTP (PubMed:14594812). {ECO:0000269|PubMed:14594812,
ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:23913032}.
-!- INTERACTION:
P18064:GPA1; NbExp=3; IntAct=EBI-962294, EBI-443890;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096,
ECO:0000269|PubMed:11706190}. Cell membrane
{ECO:0000269|PubMed:10198096, ECO:0000269|PubMed:11706190};
Peripheral membrane protein {ECO:0000269|PubMed:10198096}.
Mitochondrion membrane {ECO:0000269|PubMed:11706190}. Microsome
membrane {ECO:0000269|PubMed:11706190}. Vacuole
{ECO:0000269|PubMed:10198096}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000269|PubMed:10198096}. Note=Not found in
chloroplast or nuclei. The distribution of this conventional PLD
between membrane-associated and soluble fractions varied from
organ to organ and is calcium-regulated. Activation or wounding
increases association of preexisting enzyme with membranes.
{ECO:0000269|PubMed:11090221}.
-!- TISSUE SPECIFICITY: Highly expressed in roots, stems and flowers,
moderately in leaves, seedlings and siliques. Not detected in
seeds. {ECO:0000269|PubMed:10198096}.
-!- INDUCTION: Up-regulated by abscisic acid and ethylene
(PubMed:9437863). Up-regulated by salt, dehydration and osmotic
stresses (PubMed:19017627). Not regulated by abscisic acid
(PubMed:22392280). {ECO:0000269|PubMed:19017627,
ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:9437863}.
-!- DOMAIN: C2 domain is a calcium-binding fold, and the binding
induces conformational changes, promoting the protein association
with membranes. These conformational changes occure at millimolar
Ca(2+) concentrations. Binds also PIP2. A lower affinity toward
calcium can be anticipated for PLD alpha due to the absence of two
potential calcium ligands. {ECO:0000269|PubMed:10777500}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but improved resistance of the seeds to deterioration
during storage (PubMed:17565616). Insensitivity to abscisic acid
for both promotion of stomatal closure and inhibition of stomatal
opening (PubMed:16614222). Hypersensitivity to hyperosmotic stress
(PubMed:19017627). Increased NaCl-induced disorganization of
microtubules (PubMed:23150630). No effect on abscisic acid-induced
stomatal closure (PubMed:22392280). Pldalpha1 and plddelta double
mutants have a suppressed abscisic acid-induced stomatal closure
(PubMed:22392280). {ECO:0000269|PubMed:16614222,
ECO:0000269|PubMed:17565616, ECO:0000269|PubMed:19017627,
ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:23150630}.
-!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC49274.1; Type=Frameshift; Positions=81, 95, 369, 381, 458, 491; Evidence={ECO:0000305};
Sequence=AAL16110.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U36381; AAC49274.1; ALT_FRAME; mRNA.
EMBL; AB017071; BAB02304.1; -; Genomic_DNA.
EMBL; CP002686; AEE75720.1; -; Genomic_DNA.
EMBL; AK226887; BAE98964.1; -; mRNA.
EMBL; AF428278; AAL16110.1; ALT_INIT; mRNA.
RefSeq; NP_188194.1; NM_112443.3.
UniGene; At.23882; -.
ProteinModelPortal; Q38882; -.
SMR; Q38882; -.
BioGrid; 6150; 9.
IntAct; Q38882; 5.
STRING; 3702.AT3G15730.1; -.
iPTMnet; Q38882; -.
PaxDb; Q38882; -.
PRIDE; Q38882; -.
DNASU; 820816; -.
EnsemblPlants; AT3G15730.1; AT3G15730.1; AT3G15730.
GeneID; 820816; -.
Gramene; AT3G15730.1; AT3G15730.1; AT3G15730.
KEGG; ath:AT3G15730; -.
Araport; AT3G15730; -.
TAIR; locus:2093227; AT3G15730.
eggNOG; KOG1329; Eukaryota.
eggNOG; COG1502; LUCA.
HOGENOM; HOG000240112; -.
InParanoid; Q38882; -.
KO; K01115; -.
OMA; YPDDHET; -.
OrthoDB; EOG093601XZ; -.
PhylomeDB; Q38882; -.
BioCyc; ARA:AT3G15730-MONOMER; -.
BioCyc; MetaCyc:AT3G15730-MONOMER; -.
BRENDA; 3.1.4.4; 399.
PRO; PR:Q38882; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q38882; baseline and differential.
Genevisible; Q38882; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005096; F:GTPase activator activity; IDA:TAIR.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:TAIR.
GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
GO; GO:0004630; F:phospholipase D activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
GO; GO:0010358; P:leaf shaping; IMP:TAIR.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009845; P:seed germination; IMP:TAIR.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
InterPro; IPR024632; PLipase_D_C.
InterPro; IPR015679; PLipase_D_fam.
InterPro; IPR011402; PLipase_D_pln.
PANTHER; PTHR18896; PTHR18896; 1.
Pfam; PF00168; C2; 1.
Pfam; PF12357; PLD_C; 1.
Pfam; PF00614; PLDc; 2.
PIRSF; PIRSF036470; PLD_plant; 1.
SMART; SM00239; C2; 1.
SMART; SM00155; PLDc; 2.
SUPFAM; SSF49562; SSF49562; 1.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Abscisic acid signaling pathway; Calcium; Cell membrane;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; Ethylene signaling pathway; Hydrolase;
Lipid degradation; Lipid metabolism; Membrane; Microsome;
Mitochondrion; Reference proteome; Repeat; Vacuole.
CHAIN 1 810 Phospholipase D alpha 1.
/FTId=PRO_0000218808.
DOMAIN 1 110 C2.
DOMAIN 327 366 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 656 683 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 332 332 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 334 334 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 339 339 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 661 661 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 663 663 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 668 668 {ECO:0000255|PROSITE-ProRule:PRU00153}.
MUTAGEN 563 563 E->A: Decreased GPA1 binding.
{ECO:0000269|PubMed:14594812}.
MUTAGEN 564 564 K->A: Loss of GPA1 binding.
{ECO:0000269|PubMed:14594812}.
MUTAGEN 565 565 F->A: Decreased GPA1 binding.
{ECO:0000269|PubMed:14594812}.
CONFLICT 3 4 QH -> HD (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 26 26 R -> M (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 49 49 Q -> R (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 99 99 N -> I (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 121 121 Missing (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 218 218 A -> T (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 301 302 GS -> ER (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 435 435 D -> E (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 560 561 EK -> DQ (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 607 612 RAQGLE -> KGLEGP (in Ref. 1; AAC49274).
{ECO:0000305}.
CONFLICT 735 739 SSLEC -> KLSES (in Ref. 1; AAC49274).
{ECO:0000305}.
SEQUENCE 810 AA; 91848 MW; 87A8692E43BD73CE CRC64;
MAQHLLHGTL HATIYEVDAL HGGGVRQGFL GKILANVEET IGVGKGETQL YATIDLQKAR
VGRTRKIKNE PKNPKWYESF HIYCAHLASD IIFTVKDDNP IGATLIGRAY IPVDQVINGE
EVDQWVEILD NDRNPIQGGS KIHVKLQYFH VEEDRNWNMG IKSAKFPGVP YTFFSQRQGC
KVSLYQDAHI PDNFVPRIPL AGGKNYEPQR CWEDIFDAIS NAKHLIYITG WSVYAEIALV
RDSRRPKPGG DVTIGELLKK KASEGVRVLL LVWDDRTSVD VLKKDGLMAT HDEETENFFR
GSDVHCILCP RNPDDGGSIV QSLQISTMFT HHQKIVVVDS EMPSRGGSEM RRIVSFVGGI
DLCDGRYDTP FHSLFRTLDT VHHDDFHQPN FTGAAITKGG PREPWHDIHS RLEGPIAWDV
MYNFEQRWSK QGGKDILVKL RDLSDIIITP SPVMFQEDHD VWNVQLFRSI DGGAAAGFPE
SPEAAAEAGL VSGKDNIIDR SIQDAYIHAI RRAKDFIYVE NQYFLGSSFA WAADGITPED
INALHLIPKE LSLKIVSKIE KGEKFRVYVV VPMWPEGLPE SGSVQAILDW QRRTMEMMYK
DVIQALRAQG LEEDPRNYLT FFCLGNREVK KDGEYEPAEK PDPDTDYMRA QEARRFMIYV
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPH HLSHRQPARG QIHGFRMSLW
YEHLGMLDET FLDPSSLECI EKVNRISDKY WDFYSSESLE HDLPGHLLRY PIGVASEGDI
TELPGFEFFP DTKARILGTK SDYLPPILTT


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