ID A0A0D3C6V2_BRAOL Unreviewed; 1064 AA.
AC A0A0D3C6V2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=106294909 {ECO:0000313|EnsemblPlants:Bo5g001220.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g001220.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g001220.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo5g001220.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013586067.1; XM_013730613.1.
DR RefSeq; XP_013586068.1; XM_013730614.1.
DR AlphaFoldDB; A0A0D3C6V2; -.
DR STRING; 109376.A0A0D3C6V2; -.
DR EnsemblPlants; Bo5g001220.1; Bo5g001220.1; Bo5g001220.
DR GeneID; 106294909; -.
DR Gramene; Bo5g001220.1; Bo5g001220.1; Bo5g001220.
DR KEGG; boe:106294909; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_1_1; -.
DR OMA; HGVWGSS; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000032141; Chromosome C5.
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:UP000032141}.
FT DOMAIN 240..374
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 576..611
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 910..937
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 21..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 119374 MW; DB5DD0D5278AE308 CRC64;
MENYGPRYPY PYPQYPYQPS YQYPPAPYRP PGPGSEQYQH PPPPPYYPYP PPPPYAPPPY
ASPPPLHQHA SGSHSGPLDY PPRSSSPEYH RHSFDYQPSP YPSPYPPHPQ GTYAPPPPPP
PHYPYQEPPR YAPPETKPQD PPPPPPSKTQ AFPEYRRQDC LTSVPNDNVS NSAPSYDELL
GGLRISDKPQ LSSYPSNSWL SRPADLYGYP NSSFPSNSHL PILDRVDSSS SGYASSESPH
GVDMRMTLFG KGSLKVLLLH GNFDIWIYHA KNLPNMDMFH KTLGDVFGGQ LNRKITSDPY
VSVSVAGAVI GRTYVMSNSE NPVWMQHFYV PVAHHAAEVH FVVKDSDVVG SQLIGLVTIP
VEQIYSGAKI EGTFPILSSN GKPCKPGANL SLSIQYTPME KLSVYHHGVG AGPDYQGVPG
TYFPLRKGGT VTLYQDAHVP EGMLPGIRLD NGMSYQHGKC WHDMFDAIRQ ARRLIYITGW
SVWHKVRLVR DKVGPASACT LGELLRSKSQ EGVRVLLLVW DDPTSRSILG YKTDGVMATH
DEETRRFFKH SSVQVLLCPR NAGKRHSWVK QREVGTIYTH HQKNVIVDAD AGANRRKIVA
FVGGLDLCDG RYDTPQHPLF RTLQTIHKDD FHNPTFTGNL SGCPREPWHD LHSKIDGPAA
YDVLTNFEER WLKAAKPSGI KKFKTSYDDA LLRIDRIPDI VGVSDTPTIS ENDPEAWHVQ
IFRSIDSNSV KGFPKDPKDA TYKNLVCGKN VLIDMSIHTA YVKAIRAAQH FIYIENQYFI
GSSYNWNAHK DIGANNLIPM EIALKIAEKI RANERFAAYI VIPMWPEGVP TGAATQRILY
WQHKTMQMMY ETIYKALVET GLEGAFSPQD YLNFFCLGNR EMVDGIDNSG TGSPSNANTP
QALSRKSRRF MIYVHSKGMV VDDEYVVIGS ANINQRSMEG TRDTEIAMGA YQPQHTWARK
HSGPRGQIYG YRMSLWAEHM ATLDDCFTQP ESIECVRKVR TMGERNWEQF AAEEVSDMRG
HLLKYPVEVD RKGKVRPLPG SEAFPDVGGN IVGSFIAIQE NLTI
//