ID D7LI11_ARALL Unreviewed; 1087 AA.
AC D7LI11;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=ARALYDRAFT_903548 {ECO:0000313|EMBL:EFH58076.1};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683}.
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DR EMBL; GL348716; EFH58076.1; -; Genomic_DNA.
DR RefSeq; XP_002881817.1; XM_002881771.1.
DR AlphaFoldDB; D7LI11; -.
DR STRING; 81972.D7LI11; -.
DR EnsemblPlants; scaffold_403049.1; scaffold_403049.1; scaffold_403049.1.
DR GeneID; 9317883; -.
DR Gramene; scaffold_403049.1; scaffold_403049.1; scaffold_403049.1.
DR KEGG; aly:9317883; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_1_1; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04015; C2_plant_PLD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF65; PHOSPHOLIPASE D BETA 1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 256..397
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 599..634
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 933..960
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 21..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 121536 MW; 8A948BD23934A3E7 CRC64;
MDNHGPRYPY PYGQYPYPYP YPAPYRPPSS EPYPPPPTNQ YNAPYYPYPP PPYATPPPQP
PYASPPPHQH TSGSHSGPLD YSHNPQPSSH AAPPEYHRHS FDYQPSPYPY SGHQPQANFG
AYGPPPHYSS YQEPAQYPPP ETKPQEPPPQ TQGYPEYRRQ DCLSSGGTGH DNVSNSGSSY
PPVDELLGGL HISTNQPGPS VPQLSSLPSN SWQSRPGDLY GYPNSSFPSN SHLPHLGRVD
SSSSYTPSYA STESPHSADM QMTLFGKGSL KVLLLHGNLD IWIYHAKNLP NMDMFHKTLG
DMFGRLPGKI EGQLSSKITS DPYVSVSVAG AVIGRTYVMS NSENPVWMQH FYVPVAHHAA
EVHFVVKDSD VVGSQLIGLV TIPVEQIYSG AKIEGTYPIL NSNGKPCKPG ANLSLSIQYT
PMEKLSVYHH GVGAGPDYQG VPGTYFPLRK GGTVRLYQDA HVPEGMLPGI RLDNGMSYEH
GKCWHDMFDA IRQARRLIYI TGWSVWHKVR LVRDKLGPAS ECTLGELLRS KSQEGVRVLL
LIWDDPTSRS ILGYKTDGVM ATHDEETRRF FKHSSVQVLL CPRNAGKRHS WVKQREVGTI
YTHHQKNVIV DADAGGNRRK IVAFVGGLDL CDGRYDTPQH PLFRTLQTVH KDDFHNPTFT
GNLSGCPREP WHDLHSKIDG PAAYDVLTNF EERWLKAAKP SGIKKFKTSY DDALLRIDRI
PDILGVSDTP TVSENDPEAW HVQIFRSIDS NSVKGFPKDP KDATCKNLVC GKNVLIDMSI
HTAYVKAIRA AQHFIYIENQ YFIGSSYNWN AHKDIGANNL IPMEIALKIA EKIRANERFA
AYIVIPMWPE GVPTGAATQR ILYWQHKTMQ MMYETIYKAL VETGLEGAFS PQDYLNFFCL
GNREMVDGID NSGTGSPSNA NTPQALSRKS RRFMVYVHSK GMVVDDEYVL IGSANINQRS
MEGTRDTEIA MGAYQPQHTW ARKHSGPRGQ IYGYRMSLWA EHMATLDDCF TQPESIECVR
KVRTMGERNW KQFAAEEVSD MRGHLLKYPV EVDRKGKVRP LPGSETFPDV GGNIVGSFIA
IQENLTI
//
