ID A0A3B6LQ66_WHEAT Unreviewed; 860 AA.
AC A0A3B6LQ66;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 30.
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 Name=LOC123122430 {ECO:0000313|EnsemblPlants:TraesCS5B02G336100.2};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G336100.2};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS5B02G336100.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5B02G336100.2};
RA Rossello M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G336100.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
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 SMR; A0A3B6LQ66; -.
DR EnsemblPlants; TraesCS5B02G336100.2; TraesCS5B02G336100.2; TraesCS5B02G336100.
DR Gramene; TraesCS5B02G336100.2; TraesCS5B02G336100.2; TraesCS5B02G336100.
DR Gramene; TraesCS5B03G0841100.2; TraesCS5B03G0841100.2.CDS; TraesCS5B03G0841100.
DR Gramene; TraesJUL5B03G02962490.2; TraesJUL5B03G02962490.2; TraesJUL5B03G02962490.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000019116; Chromosome 5B.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 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:SF60; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
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|ARBA:ARBA00022837, 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:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..161
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 368..403
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 706..733
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 52..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 96934 MW; 7390A3EF9CFC9EDE CRC64;
MASSGGDESP SPAKPVLLHG DLDLWVVEAR LLPNMDMFSE HIRRCFASCG TASSCAPRQP
PPNSRGVGEA GSRRHHHRRI ITSDPYVTLS VAGAVVARTA VIPNSQEPRW DEQFFVPLAH
RATLLDFQVK DNDTFGAQLI GTASVPAERV VAAVDEVEEW VPIVGTSGKT YKPRTALFIR
YRFRPFAANP VYRRGIPGDP DQQGVKDSYF PLRHGGKVTL YQDAHVNEGD LPDVQLERGK
KFEHNQCWED ICHAILEAHH MIYIVGWSIY DKVKLVREPS SSRTLPEGGE LTLGELLKFK
SQEGVRVCLL VWDDKTSHDK LFIKTGGVMG THDEETRKFF KHSSVICVLS PRYASSKLSI
FKQQVVGTLF THHQKCVLVD TQASGNKRKV TAFIGGLDLC DGRYDTPQHR LFKDLDTVFE
NDFHNPTFSA GAKGPRQPWH DLHCKLDGPA AYDVLKNFEQ RWRKASKFRD RFRKVSRWKD
DALIKLERIS WILSPSPNVP NDHVSLRVSK EEDPENWHVQ VFRSIDSGSL KGFPSDCKEA
SKQNLVCRKN LIIDKSIHTA YVRAIRSAQH FIYIENQYFL GSSYEWPSYV NSGADNLIPM
ELALKIATKI RAGERFAVYI VIPMWPEGVP TSASVQEILF FQTMEMMYGV IARELKAMNI
EDAHLHDYLN FYCLGNREEP STDGSPGSDK STDKSAAGLA RKHRRFMIYV HAKGMIVDDE
YVILGSANIN QRSLAGSRDT EIAMGAYQPH HAWSSKKGHP HGQVYGYRSS LWAEHLGMVD
DHFKEPSSLD CVRLVNQIAE ENWERFASEE MQTLQGHLLR YPVKVEPDGK IVPLPDQECF
PDVGGKICGA PTSLPDSLTM
//
