PLDZ2_ARATH
ID PLDZ2_ARATH Reviewed; 1046 AA.
AC Q9M9W8; A3KH17; Q7XZQ3;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phospholipase D zeta 2 {ECO:0000303|PubMed:11891260};
DE Short=PLDzeta2 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000269|PubMed:11891260};
DE AltName: Full=Phospholipase D p2;
DE Short=AtPLDp2;
DE AltName: Full=Phospholipase D2 PHOX and PX-containing domain protein;
GN Name=PLPZETA2 {ECO:0000303|PubMed:11891260}; Synonyms=PLDP2;
GN OrderedLocusNames=At3g05630 {ECO:0000312|Araport:AT3G05630};
GN ORFNames=F18C1.10 {ECO:0000312|EMBL:AAF26134.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GENE
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY
RP AUXIN, AND DISRUPTION PHENOTYPE.
RX PubMed=17259265; DOI=10.1105/tpc.106.041426;
RA Li G., Xue H.-W.;
RT "Arabidopsis PLDzeta2 regulates vesicle trafficking and is required for
RT auxin response.";
RL Plant Cell 19:281-295(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16891548; DOI=10.1104/pp.106.085647;
RA Li M., Welti R., Wang X.;
RT "Quantitative profiling of Arabidopsis polar glycerolipids in response to
RT phosphorus starvation. Roles of phospholipases D zeta1 and D zeta2 in
RT phosphatidylcholine hydrolysis and digalactosyldiacylglycerol accumulation
RT in phosphorus-starved plants.";
RL Plant Physiol. 142:750-761(2006).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY LOW
RP PHOSPHATE.
RX PubMed=16384909; DOI=10.1104/pp.105.070995;
RA Li M., Qin C., Welti R., Wang X.;
RT "Double knockouts of phospholipases Dzeta1 and Dzeta2 in Arabidopsis affect
RT root elongation during phosphate-limited growth but do not affect root hair
RT patterning.";
RL Plant Physiol. 140:761-770(2006).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LOW PHOSPHATE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16617110; DOI=10.1073/pnas.0600863103;
RA Cruz-Ramirez A., Oropeza-Aburto A., Razo-Hernandez F., Ramirez-Chavez E.,
RA Herrera-Estrella L.;
RT "Phospholipase DZ2 plays an important role in extraplastidic galactolipid
RT biosynthesis and phosphate recycling in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6765-6770(2006).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA).
CC Phosphatidylcholine-selective (PubMed:11891260). Regulates vesicle
CC trafficking and auxin responses (PubMed:17259265). Required for the
CC normal cycling of PIN-2 containing vesicles (PubMed:17259265).
CC Contributes to the supply of inorganic phosphorus for cell metabolism
CC and diacylglycerol moieties for galactolipid synthesis in phosphorus-
CC starved roots (PubMed:16891548, PubMed:16617110). Involved in root
CC elongation during phosphate limitation (PubMed:16384909).
CC {ECO:0000269|PubMed:11891260, ECO:0000269|PubMed:16384909,
CC ECO:0000269|PubMed:16617110, ECO:0000269|PubMed:16891548,
CC ECO:0000269|PubMed:17259265}.
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:0000269|PubMed:11891260};
CC -!- COFACTOR:
CC Note=Does not require Ca(2+) or any other cation for activity.
CC {ECO:0000269|PubMed:11891260};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems and
CC flowers (PubMed:17259265, PubMed:16384909). Highest expression in roots
CC (PubMed:16384909). Detected only in the meristematic regions up to 4
CC days after germination and then at later stages in all tissues
CC (PubMed:16617110). {ECO:0000269|PubMed:16384909,
CC ECO:0000269|PubMed:16617110, ECO:0000269|PubMed:17259265}.
CC -!- INDUCTION: Up-regulated by auxin (PubMed:17259265). Up-regulated by
CC phosphate limitation (PubMed:16384909, PubMed:16617110).
CC {ECO:0000269|PubMed:16384909, ECO:0000269|PubMed:16617110,
CC ECO:0000269|PubMed:17259265}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions (PubMed:16384909). Shorter roots less sensitive to exogenous
CC auxin (PubMed:17259265). Reduced gravitropism (PubMed:17259265). No
CC effect on root hair patterning or root hair growth (PubMed:16384909).
CC Defective in the hydrolysis of phospholipids, reduced capacity to
CC accumulate galactolipids and premature change in root architecture in
CC response to phosphate starvation (PubMed:16617110). Decreased
CC accumulation of phosphatidic acid in roots under phosphate-limited
CC conditions (PubMed:16384909). No effect on the concentration of
CC phospholipids and galactolipids in phosphorus-starved roots
CC (PubMed:16891548). Pldzeta1 and pldzeta2 double mutants show a smaller
CC decrease in phosphatidylcholine and a smaller increase in
CC digalactosyldiacylglycerol in phosphorus-starved roots
CC (PubMed:16891548). Pldzeta1 and pldzeta2 double mutants show reduced
CC primary root elongation and increased lateral root elongation under
CC low-phosphate conditions (PubMed:16384909).
CC {ECO:0000269|PubMed:16384909, ECO:0000269|PubMed:16617110,
CC ECO:0000269|PubMed:16891548, ECO:0000269|PubMed:17259265}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. PXPH-PLD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26134.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY305003; AAP68834.1; -; mRNA.
DR EMBL; AM182458; CAJ58441.1; -; mRNA.
DR EMBL; AC011620; AAF26134.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74269.1; -; Genomic_DNA.
DR RefSeq; NP_187214.2; NM_111436.6.
DR AlphaFoldDB; Q9M9W8; -.
DR SMR; Q9M9W8; -.
DR STRING; 3702.AT3G05630.1; -.
DR PaxDb; Q9M9W8; -.
DR PRIDE; Q9M9W8; -.
DR ProteomicsDB; 235039; -.
DR EnsemblPlants; AT3G05630.1; AT3G05630.1; AT3G05630.
DR GeneID; 819730; -.
DR Gramene; AT3G05630.1; AT3G05630.1; AT3G05630.
DR KEGG; ath:AT3G05630; -.
DR Araport; AT3G05630; -.
DR TAIR; locus:2078037; AT3G05630.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; Q9M9W8; -.
DR OMA; VRHPHRE; -.
DR OrthoDB; 755722at2759; -.
DR PhylomeDB; Q9M9W8; -.
DR BioCyc; ARA:AT3G05630-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9M9W8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9W8; baseline and differential.
DR Genevisible; Q9M9W8; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IDA:TAIR.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:TAIR.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IMP:TAIR.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IDA:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0048364; P:root development; IGI:TAIR.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome; Repeat.
FT CHAIN 1..1046
FT /note="Phospholipase D zeta 2"
FT /id="PRO_0000218819"
FT DOMAIN 45..205
FT /note="PX"
FT DOMAIN 215..343
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 472..499
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 847..874
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 653..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 854
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 859
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 1046 AA; 118810 MW; DEF5E388891E5D23 CRC64;
MSTDKLLLPN GVKSDGVIRM TRADAAAAAA SSSLGGGSQI FDELPKAAIV SVSRPDTTDF
SPLLLSYTLE LQYKQFKWTL QKKASQVLYL HFALKKRLII EELHDKQEQV REWLHSLGIF
DMQGSVVQDD EEPDDGALPL HYTEDSIKNR NVPSRAALPI IRPTIGRSET VVDRGRTAMQ
GYLSLFLGNL DIVNSKEVCK FLEVSRLSFA REYGSKMKEG YVTVKHLRDV PGSDGVRCCL
PTHCLGFFGT SWTKVWAVLK PGFLALLEDP FSGKLLDIMV FDTLGLQGTK ESSEQPRLAE
QVKEHNPLRF GFKVTSGDRT VRLRTTSSRK VKEWVKAVDE AGCYSPHRFG SFAPPRGLTS
DGSQAQWFVD GHTAFEAIAF AIQNATSEIF MTGWWLCPEL YLKRPFEDHP SLRLDALLET
KAKQGVKIYI LLYKEVQIAL KINSLYSKKR LQNIHKNVKV LRYPDHLSSG IYLWSHHEKI
VIVDYQVCFI GGLDLCFGRY DTAEHKIGDC PPYIWPGKDY YNPRESEPNS WEETMKDELD
RRKYPRMPWH DVHCALWGPP CRDVARHFVQ RWNHSKRNKA PNEQTIPLLM PHHHMVLPHY
LGTREIDIIA AAKPEEDPDK PVVLARHDSF SSASPPQEIP LLLPQETDAD FAGRGDLKLD
SGARQDPGET SEESDLDEAV NDWWWQIGKQ SDCRCQIIRS VSQWSAGTSQ PEDSIHRAYC
SLIQNAEHFI YIENQFFISG LEKEDTILNR VLEALYRRIL KAHEENKCFR VVIVIPLLPG
FQGGIDDFGA ATVRALMHWQ YRTISREGTS ILDNLNALLG PKTQDYISFY GLRSYGRLFE
DGPIATSQIY VHSKLMIVDD RIAVIGSSNI NDRSLLGSRD SEIGVVIEDK EFVESSMNGM
KWMAGKFSYS LRCSLWSEHL GLHAGEIQKI EDPIKDATYK DLWMATAKKN TDIYNQVFSC
IPNEHIRSRA ALRHNMALCK DKLGHTTIDL GIAPERLESC GSDSWEILKE TRGNLVCFPL
QFMCDQEDLR PGFNESEFYT APQVFH
