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Database: UniProt
Entry: A0A0D3C6V2_BRAOL
LinkDB: A0A0D3C6V2_BRAOL
Original site: A0A0D3C6V2_BRAOL 
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
//
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