ID   A0A3L6SIL0_PANMI        Unreviewed;      1101 AA.
AC   A0A3L6SIL0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 26.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=C2845_PM07G08110 {ECO:0000313|EMBL:RLN22449.1};
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:RLN22449.1, 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   -!- 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:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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:RLN22449.1}.
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   EMBL; PQIB02000004; RLN22449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6SIL0; -.
DR   STRING; 4540.A0A3L6SIL0; -.
DR   OrthoDB; 14911at2759; -.
DR   Proteomes; UP000275267; Chromosome 7.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   FunFam; 3.30.870.10:FF:000011; Phospholipase; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          449..476
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          884..911
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1101 AA;  125481 MW;  583FDC2EBD47B6A7 CRC64;
     MTGAEEEEEL GGHRYFRMPP EPPEPEGLAA AASSASFRLP ESARVFDELP RARIVAVSRP
     DAGDITPMLL SYTIEVHYKQ FRWLLYKKAS QVLYLHFALK RRAFLEEFHE KQEQVKEWLQ
     NLGIGEHMPV VHDDDEADDV HVPSQHDEHS IKNRNVPSSA VLPVIRPALG RQQSVSDRAK
     VAMQEYLNHF LGNLDIVNSR EVCKFLEVSL LSFLPEYGPK LKEDYVTVWA VLKPGFLALL
     QDPFDPKLLD IVIFDVSPCT DRNGEGQTTL ANEIKEHNPL HFGFEVSSGG RAIKLRTRSS
     AKVKDWVTAI NVARRPPEGW CHPHRFGSFA PPRGLTEDGS VVQWFIDGRA AFDAIASSIE
     EAKSEIFITD WWLCPELYLR RPFHFHGSSR LDILLESRAK QGVQIYILLY KEVSLALKIN
     SMYSKRRLLN IHENVKVLRY PDHFSTGIYL WSHHEKIVIV DNQVCYIGGL DLCFGRYDSP
     EHKVADFPPS TWPGKDYYNP REYEPNSWED TMKDELDRTK YPRMPWHDVQ CALYGPACRD
     VARHFVQRWN YAKRNKAPNE QAIPLLMPHH HMVIPHYMGT SKETNGETES KQNHSMDIKI
     DRLNSMKTPA SCQDIPLLLP HEPDHHAFPN GDFGLNGMNI NNGLSDHANK TNRNHPLPNR
     KAKVDLSLQD LQMKGFVDNV GSPEVSVSKR YDTSKPDMQN IDKEWWETQE RGDQVASVLD
     VGEVGPRAAC RCQVDRSVGP WSAGTTQIEG SIHNAYFSLI EKAEHFVYIE NQFFISGLSG
     DDTIKNRVLE ALYRRILRAE KEKKRFRVII VIPLLPGFQG GIDDGGAASV RAIMHWQYRT
     ICRGPNSILK NLYDVVGSKG HDYISFYGLR AHGRLGDGGP LVTNQIYVHS KLMIIDDRIA
     LIGSANINDR SLLGSRDSEI GMIIEDKEVV SSIMDGRPWE AGKFSLSLRL SLWAEHLGLL
     PGEVRCIMDP VDDSAYKNIW MATAKVNTMI YQQVFSCVPN DHIHSRRKVV LTGRSTSCRN
     QFRQNFAHRK EKIGHTTIDL GVALEKPETK QDRDLADADP MEQLQAVRGH IVSFPLEFMC
     QEDLRPFFSE SEYYTSPQVF H
//