ID M0ZIV2_SOLTU Unreviewed; 811 AA.
AC M0ZIV2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=102597936 {ECO:0000313|EnsemblPlants:PGSC0003DMT400001650};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400001650, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400001650}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400001650};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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}.
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DR RefSeq; XP_006364210.1; XM_006364148.2.
DR AlphaFoldDB; M0ZIV2; -.
DR STRING; 4113.M0ZIV2; -.
DR PaxDb; 4113-PGSC0003DMT400001650; -.
DR EnsemblPlants; PGSC0003DMT400001650; PGSC0003DMT400001650; PGSC0003DMG400000614.
DR GeneID; 102597936; -.
DR Gramene; PGSC0003DMT400001650; PGSC0003DMT400001650; PGSC0003DMG400000614.
DR KEGG; sot:102597936; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; M0ZIV2; -.
DR OMA; ISRDRNW; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
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:SF135; PHOSPHOLIPASE D; 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:UP000011115}.
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 326..364
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 654..681
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 811 AA; 92745 MW; 9C7CDDCF8CCF2AC8 CRC64;
MAPILLHGTL HVTIHEVDRL HGKHGRNFFS KIKDSVEETV GMGKGASRIY ATVDLEKARV
GRTRVIENEP NNPRWYESFH IYCAHMAKNV IFTVKDNNSI GATLIGRAYL PVNDLLEGEE
VDEWIEILDE DENPIEAGSK IHVTLQYFEI SRDRNWGRGI GSSKYPGVPY TFFPQRTGCR
VSLYQDAHIP DKFIPKIPLS GGKYYEPHRC WEDIFDAITN AKHMIYITGW SVYTEITLLR
DSRREKPGGD DSVGELLKKK AKEGVKVLML VWDDRTSVRL LKKDGLMATH DEETEEYFKD
TDVHCVLCPR DPDDGGSIVK DLQTSAMFTH HQKIVIVDTD MPNGESETRR LMSFVGGLDL
CDGRYDTPFH SLFRTLDTAH HDDFHQPNFA EASIDKGGPR EPWHDIHSRV EGPIAWDVLY
NFEQRWRKQG GKDILVDLRE LDNVIIPPSS VMYPDDTESW NVQLFRSIDG GAAFGFPDTP
EESVKAGLVS GKNNIVDRSI QDAYITAIRR AKNFIYIENQ YFLGSCYDWE CDDVKVEEVG
ALHLIPKELT LKIVSKIEAG ERFTVYVLVP MWPEGLPDSA SVQAILDWQR RTMEMMYKHI
FQAIRDQGLD DHPRNYLTFF CIGNREVKKS GEYEPSDKPE SDTDYERAQE ARRFMIYVHS
KMMIVDDEYI IVGSANINQR SMDGARDSEI AIGAYQPHNL TTSRQPARGQ VHGFRMALWY
EHMGMLDDTF QHPESEDCVR KVNEIADKYW DLYTSERLET DLPGHLLRYP IGLTNDGEIT
DLPGNGNEYF PDTKAKVVGT KSDLLPPILT T
//
