ID D7L3X0_ARALL Unreviewed; 1057 AA.
AC D7L3X0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=ARALYDRAFT_477854 {ECO:0000313|EMBL:EFH58688.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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:0000256|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; GL348715; EFH58688.1; -; Genomic_DNA.
DR RefSeq; XP_002882429.1; XM_002882383.1.
DR AlphaFoldDB; D7L3X0; -.
DR STRING; 81972.D7L3X0; -.
DR EnsemblPlants; fgenesh2_kg.3__555__AT3G05630.1; fgenesh2_kg.3__555__AT3G05630.1; fgenesh2_kg.3__555__AT3G05630.1.
DR Gramene; fgenesh2_kg.3__555__AT3G05630.1; fgenesh2_kg.3__555__AT3G05630.1; fgenesh2_kg.3__555__AT3G05630.1.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblPlants.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEA:EnsemblPlants.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:EnsemblPlants.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:EnsemblPlants.
DR GO; GO:0009733; P:response to auxin; IEA:EnsemblPlants.
DR GO; GO:0048364; P:root development; IEA:EnsemblPlants.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR CDD; cd06895; PX_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF133; PHOSPHOLIPASE D ZETA 2; 1.
DR Pfam; PF00169; PH; 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 SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 216..344
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 473..500
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 858..885
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 654..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 120618 MW; 8E3D19F32D8BBBFA CRC64;
MSTDKLLLPN GVKSDGVMRR TRPDAAAAAA ASYSLGGGSQ IFDELPKAAI VSVSRPDTTD
FSPLLLSYTL ELQYKQFKWT LQKKASQVLY LHFALKKRLI IEDLHDKQEQ VREWLHSLGI
FDMQGSVVQD DEEPDDGALP LHYTEDSIKN RNVPSRAAFP IIRPTIGRSE TVVDRGRTAM
QGYLSLFLGN LDIVNSKEVC KFLEVSRLSF AREYGSKMKE GFVTVKHLRE VPGSDSVRCC
LPSHCFGFFG TSWTKVWAVL KPGFLALLED PFSGKLLDIM VFDTLGLQST KESSEQLRLA
EQVKEQNPLR FGFKITSGDR TVTLRTTSSR KVKEWVKAVD EAGCYSPHRF GSFAPPRGLT
SDGSQAQWFV DGHTAFEAIA FAIQNATSEI FMTGWWLCPE LYLKRPFEDH PSLRLDALLE
TKAKQGVKIY ILLYKEVQIA LKINSMYSKK RLQNIHKNVK VLRYPDHLSS GIYLWSHHDK
IVIVDYQVCF IGGLDLCFGR YDTAEHKIGD FPPYIWPGKD YYNPRESEPN SWEETMKDEL
DRRKYPRMPW HEVHCALWGP PCRDVARHFV QRWNHSKRNK APNEQTIPLL MPHHHMVLPH
YLGTREIDII AAAKPEEDPD KPVVLARQDS FSSASPPQDI PLLLPQETDA DFTSRGDLKF
DSGSRQDLDR SGSQVEFPGE TSEESDRDEA VNDWWWQIGK QSDCRCQIIR SVSQWSAGTS
QSEDSIHRAY CSLIQNAEHF IYIENQFFIS GLEKDDTILN RVLETLYRRI LKAHEQNKCF
RVVIVIPLLP GFQGGIDDFG AATVRALMHW QYRTISRERT SILDNLNALL GPKTQEYISF
YGLRSYGRLF EDGPIATSQI YVHSKLMIVD DRIAVIGSSN INDRSLLGSR DSEIGVVIED
KEFVESSMNG VKWMAGKFSY SLRCSLWSEH LGLHPGEMQK IEDPIKDATY KDLWMATAKK
NTDIYDQVFS CIPNEHIRSR AALRHNMSIC KDKLGHTTID LGIAPERLDS CGSDSWEMLK
ETRGHLVCFP LQFMCDQEDL RPVFNESEFY TAPQVFH
//
