PLDZ1_ARATH
ID PLDZ1_ARATH Reviewed; 1096 AA.
AC Q9LRZ5;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phospholipase D zeta 1 {ECO:0000303|PubMed:11891260};
DE Short=PLDzeta1 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000269|PubMed:11891260};
DE AltName: Full=Phospholipase D p1;
DE Short=AtPLDp1;
DE AltName: Full=Phospholipase D1 PHOX and PX-containing domain protein;
GN Name=PLDZETA1 {ECO:0000303|PubMed:11891260}; Synonyms=PLDP1;
GN OrderedLocusNames=At3g16785 {ECO:0000312|Araport:AT3G16785};
GN ORFNames=K20I9.1 {ECO:0000312|EMBL:BAA95772.2}, MGL6.26;
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], GENE FAMILY, NOMENCLATURE, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP FUNCTION, INDUCTION BY GL2, AND SUBCELLULAR LOCATION.
RX PubMed=12775839; DOI=10.1126/science.1083695;
RA Ohashi Y., Oka A., Rodrigues-Pousada R., Possenti M., Ruberti I.,
RA Morelli G., Aoyama T.;
RT "Modulation of phospholipid signaling by GLABRA2 in root-hair pattern
RT formation.";
RL Science 300:1427-1430(2003).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA).
CC Phosphatidylcholine-selective (PubMed:11891260). Regulates root-hair
CC morphogenesis (PubMed:12775839). Contributes to the supply of inorganic
CC phosphorus for cell metabolism and diacylglycerol moieties for
CC galactolipid synthesis in phosphorus-starved roots (PubMed:16891548).
CC Involved in root elongation during phosphate limitation
CC (PubMed:16384909). {ECO:0000269|PubMed:11891260,
CC ECO:0000269|PubMed:12775839, ECO:0000269|PubMed:16384909,
CC ECO:0000269|PubMed:16891548}.
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 -!- ACTIVITY REGULATION: Calcium-independent and PIP2-dependent.
CC {ECO:0000269|PubMed:11891260}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:11891260};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:12775839}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, flowers, siliques,
CC stems, leaves, and roots. Highest expression in roots.
CC {ECO:0000269|PubMed:16384909}.
CC -!- INDUCTION: Transcriptionally regulated by GL2 (PubMed:12775839). Up-
CC regulated by phosphate limitation (PubMed:16384909).
CC {ECO:0000269|PubMed:12775839, ECO:0000269|PubMed:16384909}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions (PubMed:16384909). No effect on root hair patterning or root
CC hair growth (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:16891548}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. PXPH-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; AF411833; AAL06337.1; -; mRNA.
DR EMBL; AB028608; BAA95772.2; -; Genomic_DNA.
DR EMBL; AB022217; BAA95772.2; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE75865.1; -; Genomic_DNA.
DR RefSeq; NP_188302.2; NM_112553.4.
DR AlphaFoldDB; Q9LRZ5; -.
DR SMR; Q9LRZ5; -.
DR STRING; 3702.AT3G16785.1; -.
DR iPTMnet; Q9LRZ5; -.
DR PaxDb; Q9LRZ5; -.
DR PRIDE; Q9LRZ5; -.
DR ProteomicsDB; 235038; -.
DR EnsemblPlants; AT3G16785.1; AT3G16785.1; AT3G16785.
DR GeneID; 820932; -.
DR Gramene; AT3G16785.1; AT3G16785.1; AT3G16785.
DR KEGG; ath:AT3G16785; -.
DR Araport; AT3G16785; -.
DR TAIR; locus:2086750; AT3G16785.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; Q9LRZ5; -.
DR OMA; CNSEHTK; -.
DR PhylomeDB; Q9LRZ5; -.
DR BioCyc; ARA:AT3G16785-MON; -.
DR BioCyc; MetaCyc:AT3G16785-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9LRZ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRZ5; baseline and differential.
DR Genevisible; Q9LRZ5; AT.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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; IBA:GO_Central.
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 Acetylation; Cytoplasmic vesicle; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1096
FT /note="Phospholipase D zeta 1"
FT /id="PRO_0000218818"
FT DOMAIN 50..204
FT /note="PX"
FT DOMAIN 234..342
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 477..504
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 892..919
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 131..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1096 AA; 124505 MW; 8B71D9D0DDEAEA45 CRC64;
MASEQLMSPA SGGGRYFQMQ PEQFPSMVSS LFSFAPAPTQ ETNRIFEELP KAVIVSVSRP
DAGDISPVLL SYTIECQYKQ FKWQLVKKAS QVFYLHFALK KRAFIEEIHE KQEQVKEWLQ
NLGIGDHPPV VQDEDADEVP LHQDESAKNR DVPSSAALPV IRPLGRQQSI SVRGKHAMQE
YLNHFLGNLD IVNSREVCRF LEVSMLSFSP EYGPKLKEDY IMVKHLPKFS KSDDDSNRCC
GCCWFCCCND NWQKVWGVLK PGFLALLEDP FDAKLLDIIV FDVLPVSNGN DGVDISLAVE
LKDHNPLRHA FKVTSGNRSI RIRAKNSAKV KDWVASINDA ALRPPEGWCH PHRFGSYAPP
RGLTDDGSQA QWFVDGGAAF AAIAAAIENA KSEIFICGWW VCPELYLRRP FDPHTSSRLD
NLLENKAKQG VQIYILIYKE VALALKINSV YSKRRLLGIH ENVRVLRYPD HFSSGVYLWS
HHEKLVIVDN QVCFIGGLDL CFGRYDTFEH KVGDNPSVTW PGKDYYNPRE SEPNTWEDAL
KDELERKKHP RMPWHDVHCA LWGPPCRDVA RHFVQRWNYA KRNKAPYEDS IPLLMPQHHM
VIPHYMGRQE ESDIESKKEE DSIRGIRRDD SFSSRSSLQD IPLLLPHEPV DQDGSSGGHK
ENGTNNRNGP FSFRKSKIEP VDGDTPMRGF VDDRNGLDLP VAKRGSNAID SEWWETQDHD
YQVGSPDETG QVGPRTSCRC QIIRSVSQWS AGTSQVEESI HSAYRSLIDK AEHFIYIENQ
FFISGLSGDD TVKNRVLEAL YKRILRAHNE KKIFRVVVVI PLLPGFQGGI DDSGAASVRA
IMHWQYRTIY RGHNSILTNL YNTIGVKAHD YISFYGLRAY GKLSEDGPVA TSQVYVHSKI
MIVDDRAALI GSANINDRSL LGSRDSEIGV LIEDTELVDS RMAGKPWKAG KFSSSLRLSL
WSEHLGLRTG EIDQIIDPVS DSTYKEIWMA TAKTNTMIYQ DVFSCVPNDL IHSRMAFRQS
LSYWKEKLGH TTIDLGIAPE KLESYHNGDI KRSDPMDRLK AIKGHLVSFP LDFMCKEDLR
PVFNESEYYA SPQVFH
