ID A0A3L6TC14_PANMI Unreviewed; 825 AA.
AC A0A3L6TC14;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=C2845_PM03G34830 {ECO:0000313|EMBL:RLN35712.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN35712.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN35712.1}.
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DR EMBL; PQIB02000002; RLN35712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6TC14; -.
DR STRING; 4540.A0A3L6TC14; -.
DR Proteomes; UP000275267; Chromosome 3.
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 CDD; cd09139; PLDc_pPLD_like_1; 1.
DR CDD; cd09142; PLDc_pPLD_like_2; 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:SF137; PHOSPHOLIPASE D ALPHA 4; 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; 1.
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:UP000275267}.
FT DOMAIN 4..139
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 666..693
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 825 AA; 90873 MW; 2AF0308E9F2BFE7A CRC64;
MGSQQEEGGG AAAAADVVYL HGVLEVTVFE AEHLHNAIHG RIIEATEKVQ ETMGVHCLQH
SRLYVDVDVG AARVARTREV EFHPTSPAWN QSFRLHCAYP AAAVTFTVKN QHLIGAGVLG
AASVPAARVA SGQPVECWLS LRGGEHGHET HTPSLRVRLQ FLDVERDPSW GAGVRLPGFA
GVVPAFFPER TGCSVTLYQN AHLTDAFDPG VRLDGGRAYR PPRLWEDLYA AIRYARRFVY
VAGWSVSTEI TLVRDPGRMV PGAEGVTLGE LLKRKADEGV AVLVMPWQDN TSVSFLGNAG
LMKTHDEETR RFFEGTNVRC FLCPRNADAS LTMVQHVQTS AEFTHHQKTV TLDAATPGAG
DDGRHVVSFI GGIDLCDGRY DDENHTLFRD LDTTYLHDFM QNNYKHACLR CGGPREPWHD
VHCRLEGPAA WDVLTNFEQR WRKQAPEGMR GCLLDLSPAA LPDPAGLGDD TGSWNVQVFR
SIDDASVVGF PSDPAEAAAL GLTSGKDVTV DRSIQTAYVE AIRRARRFIY IENQYFLGGC
ASWAEDRGAG CLNLVPVEIA LKVAAKIRRG ERFAAYVVMP MCPEGLPAGD AVQAILLWNR
RTVEMMYGIV MEAIDDAGLR GQAHPCDYLN FFCLGNREAP LPGEYSPPET PEKDTDYWRA
QVNRRGPIYV HAKLMIVDDE YVIVGSANLN ERSLAGNRDS EIAQGSYQPA HLNGLCGRAR
GQVHGFRMSL WHEHFMGRHA GEDGPVFLEP ESLECVRAVR RAAERLWGVY TQDRVENLPG
HLLPFPITVS EFGEVADLPA DGCFPDTRAP VRGRKAAKLP DILTT
//
