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Phospholipase D gamma 1 (AtPLDgamma1) (PLD gamma 1) (EC 3.1.4.4) (Choline phosphatase) (Lecithinase D) (Lipophosphodiesterase II)

 PLDG1_ARATH             Reviewed;         858 AA.
Q9T053; O48544;
03-APR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 135.
RecName: Full=Phospholipase D gamma 1 {ECO:0000303|PubMed:9353280};
Short=AtPLDgamma1 {ECO:0000303|PubMed:9353280};
Short=PLD gamma 1 {ECO:0000303|PubMed:9353280};
EC=3.1.4.4 {ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280};
AltName: Full=Choline phosphatase;
AltName: Full=Lecithinase D;
AltName: Full=Lipophosphodiesterase II;
Name=PLDGAMMA1 {ECO:0000303|PubMed:9353280};
OrderedLocusNames=At4g11850 {ECO:0000312|Araport:AT4G11850};
ORFNames=T26M18.60 {ECO:0000312|EMBL:CAB44323.1};
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], CATALYTIC ACTIVITY, 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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., 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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[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;
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).
[5]
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).
[6]
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).
[7]
SUBCELLULAR LOCATION.
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).
[8]
INDUCTION BY WOUNDING.
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).
[9]
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).
[10]
INDUCTION BY WOUNDING, TISSUE SPECIFICITY, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17098468; DOI=10.1016/j.bbalip.2006.09.017;
Qin C., Li M., Qin W., Bahn S.C., Wang C., Wang X.;
"Expression and characterization of Arabidopsis phospholipase
Dgamma2.";
Biochim. Biophys. Acta 1761:1450-1458(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[13]
FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
PubMed=22163277; DOI=10.1371/journal.pone.0028086;
Zhao J., Wang C., Bedair M., Welti R., Sumner L.W., Baxter I.,
Wang X.;
"Suppression of phospholipase Dgammas confers increased aluminum
resistance in Arabidopsis thaliana.";
PLoS ONE 6:E28086-E28086(2011).
-!- 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, vesicular trafficking, secretion,
cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis,
membrane deterioration and senescence (PubMed:10441386). Can use
phosphatidylserine (PS) and phosphatidylethanolamine (PE) as
substrates only in the presence of PIP2. Can use
phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-
acylphosphatidylethanolamine (NAPE) as substrates in the presence
of PE and PIP2 (PubMed:9578608, PubMed:17098468). Involved in
membrane lipid modulation under aluminum (Al) stress and
negatively modulate plant tolerance to Al (PubMed:22163277).
{ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:17098468,
ECO:0000269|PubMed:22163277, ECO:0000269|PubMed:9578608}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate. {ECO:0000269|PubMed:10441386,
ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:17098468,
ECO:0000269|PubMed:9353280};
Note=Ca(2+). Requires micromolar level (PIP2-dependent).
{ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280};
-!- ENZYME REGULATION: Inhibited by neomycin. Up-regulated by PIP2
binding. {ECO:0000269|PubMed:9353280}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5 to 8.5. {ECO:0000269|PubMed:10441386,
ECO:0000269|PubMed:17098468};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096}.
Membrane {ECO:0000269|PubMed:10198096}; Peripheral membrane
protein {ECO:0000269|PubMed:10198096}. Note=Found mainly
associated with intracellular membranes but also with
mitochondrial membranes, nuclei and clathrin-coated vesicles. Not
found in chloroplast.
-!- TISSUE SPECIFICITY: Highly expressed in roots and flowers,
moderately in stems, leaves and seedlings and low in siliques. Not
detected in seeds. {ECO:0000269|PubMed:10198096,
ECO:0000269|PubMed:17098468}.
-!- INDUCTION: Activated by wounding, heavy metal, methyl salicylate,
osmotic and salt stresses (PubMed:11090221, PubMed:17098468). Up-
regulated by aluminum stress (PubMed:22163277).
{ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:17098468,
ECO:0000269|PubMed:22163277}.
-!- 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.
{ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Increased tolerance to aluminum.
{ECO:0000269|PubMed:22163277}.
-!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB87672.1; Type=Frameshift; Positions=60, 79, 260, 300, 465, 758; Evidence={ECO:0000305};
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EMBL; AF027408; AAB87672.1; ALT_FRAME; mRNA.
EMBL; AL078606; CAB44323.1; -; Genomic_DNA.
EMBL; AL161532; CAB78228.1; -; Genomic_DNA.
EMBL; CP002687; AEE83058.1; -; Genomic_DNA.
EMBL; AY099569; AAM20421.1; -; mRNA.
EMBL; BT002140; AAN72151.1; -; mRNA.
PIR; T09344; T09344.
RefSeq; NP_192922.1; NM_117255.3.
UniGene; At.20523; -.
ProteinModelPortal; Q9T053; -.
SMR; Q9T053; -.
BioGrid; 12089; 2.
IntAct; Q9T053; 1.
STRING; 3702.AT4G11850.1; -.
iPTMnet; Q9T053; -.
PaxDb; Q9T053; -.
PRIDE; Q9T053; -.
EnsemblPlants; AT4G11850.1; AT4G11850.1; AT4G11850.
GeneID; 826791; -.
Gramene; AT4G11850.1; AT4G11850.1; AT4G11850.
KEGG; ath:AT4G11850; -.
Araport; AT4G11850; -.
TAIR; locus:2137045; AT4G11850.
eggNOG; KOG1329; Eukaryota.
eggNOG; COG1502; LUCA.
HOGENOM; HOG000240112; -.
InParanoid; Q9T053; -.
KO; K01115; -.
OMA; GPTTGCP; -.
OrthoDB; EOG093601WQ; -.
PhylomeDB; Q9T053; -.
BioCyc; ARA:AT4G11850-MONOMER; -.
BioCyc; MetaCyc:AT4G11850-MONOMER; -.
BRENDA; 3.1.4.4; 399.
PRO; PR:Q9T053; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q9T053; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0004630; F:phospholipase D activity; IDA:TAIR.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006643; P:membrane lipid metabolic process; IMP:TAIR.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
GO; GO:0006979; P:response to oxidative stress; 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; PS50004; C2; 1.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Calcium; Complete proteome; Cytoplasm; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 858 Phospholipase D gamma 1.
/FTId=PRO_0000218812.
DOMAIN 29 147 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 364 399 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 704 731 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 369 369 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 371 371 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 376 376 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 709 709 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 711 711 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 716 716 {ECO:0000255|PROSITE-ProRule:PRU00153}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
CONFLICT 114 115 MQ -> IE (in Ref. 1; AAB87672).
{ECO:0000305}.
CONFLICT 370 370 Q -> E (in Ref. 1; AAB87672).
{ECO:0000305}.
CONFLICT 377 377 A -> S (in Ref. 1; AAB87672).
{ECO:0000305}.
CONFLICT 634 635 MQ -> IE (in Ref. 1; AAB87672).
{ECO:0000305}.
SEQUENCE 858 AA; 95588 MW; 334AF9DB9E3A7A73 CRC64;
MAYHPAYTET MSMGGGSSHG GGQQYVPFAT SSGSLRVELL HGNLDIWVKE AKHLPNMDGF
HNRLGGMLSG LGRKKVEGEK SSKITSDPYV TVSISGAVIG RTFVISNSEN PVWMQHFDVP
VAHSAAEVHF VVKDSDIIGS QIMGAVGIPT EQLCSGNRIE GLFPILNSSG KPCKQGAVLG
LSIQYTPMER MRLYQMGVGS GNECVGVPGT YFPLRKGGRV TLYQDAHVDD GTLPSVHLDG
GIQYRHGKCW EDMADAIRQA RRLIYITGWS VFHPVRLVRR TNDPTEGTLG ELLKVKSQEG
VRVLVLVWDD PTSRSLLGFK TQGVMNTSDE ETRRFFKHSS VQVLLCPRSG GKGHSFIKKS
EVGTIYTHHQ KTVIVDAEAA QNRRKIVAFV GGLDLCNGRF DTPKHPLFRT LKTLHKDDFH
NPNFVTTADD GPREPWHDLH SKIDGPAAYD VLANFEERWM KASKPRGIGK LKSSSDDSLL
RIDRIPDIVG LSEASSANDN DPESWHVQVF RSIDSSSVKG FPKDPKEATG RNLLCGKNIL
IDMSIHAAYV KAIRSAQHFI YIENQYFLGS SFNWDSNKDL GANNLIPMEI ALKIANKIRA
REKFAAYIVI PMWPEGAPTS NPIQRILYWQ HKTMQMMYQT IYKALVEVGL DSQFEPQDFL
NFFCLGTREV PVGTVSVYNS PRKPPQPNAN ANAAQVQALK SRRFMIYVHS KGMVVDDEFV
LIGSANINQR SLEGTRDTEI AMGGYQPHYS WAMKGSRPHG QIFGYRMSLW AEHLGFLEQG
FEEPENMECV RRVRQLSELN WRQYAAEEVT EMSGHLLKYP VQVDRTGKVS SLPGCETFPD
LGGKIIGSFL ALQENLTI


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EIAAB32069 Homo sapiens,Human,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase magnesium-dependent 1 gamma
EIAAB29628 cPLA2-gamma,Cytosolic phospholipase A2 gamma,Homo sapiens,Human,Phospholipase A2 group IVC,PLA2G4C
EIAAB31574 Calcium-independent phospholipase A2-gamma,Group VIB calcium-independent phospholipase A2,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,iPLA2-gamma,Oryctolagus cuniculus
18-785-210380 PLC-gamma2 (Phospho-Tyr753) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-2; Phospholipase C-gamma-2; PLC-IV Polyclonal 0.05 mg
18-785-210378 PLC-gamma1 (Phospho-Tyr783) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-1; Phospholipase C-gamma-1; PLC-II; PLC-148 Polyclonal 0.1 mg
18-785-210378 PLC-gamma1 (Phospho-Tyr783) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-1; Phospholipase C-gamma-1; PLC-II; PLC-148 Polyclonal 0.05 mg
18-785-210380 PLC-gamma2 (Phospho-Tyr753) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-2; Phospholipase C-gamma-2; PLC-IV Polyclonal 0.1 mg
EIAAB31575 BM-043,Calcium-independent phospholipase A2-gamma,Homo sapiens,Human,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,IPLA22,iPLA2-2,IPLA2G,iPLA2-gamma,Patatin-like phospho
PP-PPM1G-050 PPM1G, Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phos 50


 

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