ID D7M0A9_ARALL Unreviewed; 861 AA.
AC D7M0A9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=ARALYDRAFT_489999 {ECO:0000313|EMBL:EFH50986.1};
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 -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL348718; EFH50986.1; -; Genomic_DNA.
DR RefSeq; XP_002874727.1; XM_002874681.1.
DR AlphaFoldDB; D7M0A9; -.
DR STRING; 81972.D7M0A9; -.
DR EnsemblPlants; fgenesh2_kg.6__3133__AT4G11840.1; fgenesh2_kg.6__3133__AT4G11840.1; fgenesh2_kg.6__3133__AT4G11840.1.
DR GeneID; 9310794; -.
DR Gramene; fgenesh2_kg.6__3133__AT4G11840.1; fgenesh2_kg.6__3133__AT4G11840.1; fgenesh2_kg.6__3133__AT4G11840.1.
DR KEGG; aly:9310794; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
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 InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF130; PHOSPHOLIPASE D GAMMA 1-RELATED; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF036470; PLD_plant; 1.
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 Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 27..166
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 367..402
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 707..734
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 861 AA; 96045 MW; 0F67C334BDD50369 CRC64;
MAYHPVYTET MSMGGGSSHG GGQQYVPFAT SSGSLRVELL HGNLDIWVKE AKHLPNMDGF
HHRLGGMLSG LGRRNSIKVD GEKSSKITSD PYVTVSISGA VIGRTFVISN SENPVWMQHF
DVPVAHSAAE VHFVVKDSDI IGSQIMGAVG IPTEQLCSGN RIEGLFPILN SSGKPCKAGA
VLSLSIQYIP MERMRLYQMG VGFGNDCVGV PGTYFPLRKG GRVTLYQDAH VDDGTLPSVY
LDGGIQYQHG KCWEDMADAI RQARRLIYIT GWSVFHPVRL VRRSNDPTEG TLGDLLKVKS
QEGVRVLVLV WDDPTSRSLL GFKTQGVMNT SDEETRRFFK HSSVQVLLCP RSGGKGHSFI
KKSEVGTIYT HHQKTVILDA EAAQNRRKIV AFVGGLDLCN GRFDTPKHPL FRTLKTLHKD
DFHNPNFVTT ADDGPREPWH DLHSKIDGPA AYDVLANFEE RWMKASKPRG IGKLKSSDDD
SLLRIDRIPD IMGLSEASSA NDNDPESWHV QVFRSIDSSS VKGFPKDPKE ATGRNLLCGK
NILIDMSIHA AYVKAIRSAQ HFIYIENQYF LGSSFNWDSN KDLGANNLIP IEIALKIANK
IRAREKFAAY IVIPMWPEGA PTSNPIQRIL YWQHKTMQMM YQTIYKALVE VGLDGQFEPQ
DFLNFFCLGT REVPDGTVSV YNSPRKPPQT NANANAAQVQ ALKSRRFMIY VHSKGMVVDD
EFVLIGSANI NQRSLEGTRD TEIAMGGYQP HHSWAMKGSR PRGQIFGYRM SLWAEHLGFL
EQGFEEPENM ECVRRVRQLS ELNWRQYAAE EVTEMPGHLL KYPVQVDRTG KVSSLPGCET
FPDLGGKIIG SFLVLQENLT I
//
