ID A0A4S8JN58_MUSBA Unreviewed; 854 AA.
AC A0A4S8JN58;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
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=C4D60_Mb01t18030 {ECO:0000313|EMBL:THU63648.1};
OS Musa balbisiana (Banana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=52838 {ECO:0000313|EMBL:THU63648.1, ECO:0000313|Proteomes:UP000317650};
RN [1] {ECO:0000313|EMBL:THU63648.1, ECO:0000313|Proteomes:UP000317650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC TISSUE=Leaves {ECO:0000313|EMBL:THU63648.1};
RA Yao X.;
RT "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT function divergence in polyploid bananas.";
RL Nat. Plants 0:0-0(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:THU63648.1}.
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DR EMBL; PYDT01000004; THU63648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S8JN58; -.
DR STRING; 52838.A0A4S8JN58; -.
DR Proteomes; UP000317650; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd04015; C2_plant_PLD; 1.
DR FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 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:SF60; PHOSPHOLIPASE D; 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; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, 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:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000317650};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..151
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 352..387
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 700..727
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96496 MW; FEB4BF66FF094096 CRC64;
MGPHSAGAAA DEAILLHGDL HLSVLAARRL PNMDMLSEYL RRCFAPCSPV LPSSDSDPTP
DHGRRGHRKK IATADPYVTA LLAGATVART RVIHNSQNPI WNERFKIPVA HSAAALVLHV
KDNDVFGSQL IGTVSIPVAR VASGEVIDEW FPVIAPSGRT PKPDTALRVS LQYTPVEESV
EHRHGIAGDP DKRGVSDAYF PVRKGCLVTL YQDAHVRDGE LPEIRLEEGA IFEHNKCWED
ICHAILEAHH LIYITGWSIY HKVKLVREPT RPLPTAGQLT LGELLKYKSQ EGVRVCMLVW
DDKTSHHNFF IKTEGVMQTH DEETRKFFKH SSVICVLAPR YASSKLSFVV GTLFTHHQKC
VLVDTQASGN NRKITAFIGG LDLCDGRYDT PEHRLFHELD SVFLNDFHNP TFAGDPQLET
KGPRQPWHDL HCRIEGPAAY DVLENFEQRW RKATKWREFG LRFKKKVSHW HDDALIKLER
ISWIISPSPT VPNDDPSLWV ASEEDAGPWH VQIFRSIDSG SVKGFPKNPQ ETLRKNLVCQ
KNLIIDKSIH TAYVRAIRSA QHFIYIESQY FLGSSYAWPF YKNSGADNLI PMELALKIAS
KIKAKERFAV YVVIPMWPEG VPTTSSVQEI LFWQGQTIQM MYEIIAKELK AVNFEDSHPQ
DYLNFYCLGN REELSKDELQ SNGHSSERSP VVLAQRSRRF MIYVHAKGMI VDDEYIIMGS
SNINQRSLAG SRDTEIAMGA YQPHQTWAEK ERHPHGQIYG YRMSLWAEQL GSVDDRFEQP
NSLECVRLVN KIADDNWCRY TAKEVSSLTG HLLKYPIKVE ADGKVGALPD QQCFPDVGGK
ILGAPTSLPD TLTM
//
