ID A0A9J5WWK4_SOLCO Unreviewed; 1110 AA.
AC A0A9J5WWK4;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=Phospholipase D alpha 1 {ECO:0000256|ARBA:ARBA00041119};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE AltName: Full=Choline phosphatase 1 {ECO:0000256|ARBA:ARBA00042228};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1 {ECO:0000256|ARBA:ARBA00042781};
GN ORFNames=H5410_050280 {ECO:0000313|EMBL:KAG5579653.1};
OS Solanum commersonii (Commerson's wild potato) (Commerson's nightshade).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4109 {ECO:0000313|EMBL:KAG5579653.1, ECO:0000313|Proteomes:UP000824120};
RN [1] {ECO:0000313|EMBL:KAG5579653.1, ECO:0000313|Proteomes:UP000824120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ3.2 {ECO:0000313|EMBL:KAG5579653.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG5579653.1};
RA Cho K.;
RT "De no assembly of potato wild relative species, Solanum commersonii.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:KAG5579653.1}.
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DR EMBL; JACXVP010000010; KAG5579653.1; -; Genomic_DNA.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000824120; Chromosome 10.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004630; F:phospholipase D activity; IEA:TreeGrafter.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd04015; C2_plant_PLD; 1.
DR FunFam; 3.30.870.10:FF:000027; Phospholipase D; 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 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000824120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 283..417
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 626..661
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 956..983
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..191
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 124540 MW; D7B69B80E0B2034D CRC64;
MDNNNNKSSS SSTYPYNTAP PPSPSTNQAS YNNPSNNSSP YPPPGSVPYP YPPYLHYHLP
PYAAQQSGHV NYNSYPQVPP ASPSETTPSR PQQTNPPLEY SNYPPPSHIV HSPYSYHAYY
PPPPPPTISS FRPVLQQQGS FQYGSSQGPL ERQKSKGHDQ SPSLQHQNSL SSVTSSAASS
LSDANSSLAS SDHGNNGPID DHLANVHLYE NPSPATAAPA APASCHSGPR HHVANNYNAQ
GTIYGHPNAS FSKGEASSVV QSEPCHRPTH SRTSSGEQQN NWGMQVMPFM ASKNVLLLHG
NLDIWVFEAR NLPNLDVFHK TIGDMFNKMG NNGQLGNMTS DPYVTIILAG AVIGRTYVIN
NNENPVWMQH FNVPVAHYAS DVQFLVKDND MVGSQLIGTV AVPVEHIYGG GKVEGFFPIL
NNGKPCKAGA VLRISVQYYP MDQLSFYHHG VGAGPEYYGV PGTYFPLRMG GSVTLYQDAH
VPDGCLPNLK LDYGMMQYEH GKCWRDIFDA ICQARRLIYI TGWSVWHKVR LVRDDASVED
SCLGELLKSK SQEGVRVLLL VWDDPTSRSI LGYKTFKFEK NMQDGLMATH DEETRRFFKH
SSVQVLLCPR VAGKRHSWAK QREVGVIYTH HQKTVIVDAD AGNNRRKIIS FIGGLDLCDG
RYDTPEHPIF RTLQTVHSDD YHNPTYAGST TGCPREPWHD LHCKIDGPAA YDILKNFEER
WLKASKPQGI RKLKKTYDDS LLRIERMPEI LSIAETSSTS STDPDNWHVQ IFRSIDSNSV
KGFPKDPKEA TMKNLVCGKN VLIDMSIHTA YVKAIRAAQH FVYIENQYFI GSSYNWSQYN
DVGANNLIPM EIALKICEKI RAHQRFAAYI VIPMWPEGNP TGAATQRILF WQHKTIQMMY
ETIYKTLVEV GLEDAFSPQD YLNFFCLGNR EVDVEETENS GAANTPQALC RKYRRFMIYV
HSKGMIVDDE YVILGSANIN QRSLEGTRDT EIAMGAYQPH HTWARNQSSP SGQIYRYRMS
LWAEHLGVVD DYFIRPESLE CVRRVRSMGE ANWRQFSADE VTEMRGHLLK YPVEVDRRGK
VKNLPGFEEF PDVGGDIIGS FLAIQENLTI
//
