ID A0A0E0MS01_ORYRU Unreviewed; 871 AA.
AC A0A0E0MS01;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI01G04930.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI01G04930.1}
RP IDENTIFICATION.
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 AlphaFoldDB; A0A0E0MS01; -.
DR STRING; 4529.A0A0E0MS01; -.
DR EnsemblPlants; ORUFI01G04930.1; ORUFI01G04930.1; ORUFI01G04930.
DR Gramene; ORUFI01G04930.1; ORUFI01G04930.1; ORUFI01G04930.
DR eggNOG; KOG1329; Eukaryota.
DR OMA; PNWGRGI; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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 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:SF115; PHOSPHOLIPASE D ALPHA 2; 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:UP000008022}.
FT DOMAIN 45..189
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 389..427
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 717..744
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 871 AA; 98301 MW; 22243B3B3B1589A4 CRC64;
MTASEVASLT LSLFSRNFII SLDPICSPSS STLPISALAI AILLSLPGED ASLRRSPPAM
AQMLLHGTLH ATIFEAASLS NPHRASGSAP KFIRKFVEGI EDTVGVGKGA TKVYSTIDLE
KARVGRTRMI TNEPINPRWY ESFHIYCAHM ASNVIFTVKI DNPIGATNIG RAYLPVQELL
NGEEIDRWLD ICDNNREPVG ESKIHVKLQY FDVSKDRNWA RGVRSTKYPG VPYTFFSQRQ
GCKVTLYQDA HVPDNFIPKI PLADGKNYEP HRCWEDIFDA ISNAQHLIYI TGWSVYTEIT
LVRDSNRPKP GGDVTLGELL KKKASEGVRV LMLVWDDRTS VGLLKRDGLM ATHDEETENY
FHGSDVNCVL CPRNPDDSGS IVQDLSISTM FTHHQKIVVV DHELPNQGSQ QRRIVSFVGG
LDLCDGRYDT QYHSLFRTLD STHHDDFHQP NFATASIKKG GPREPWHDIH SRLEGPIAWD
VLYNFEQRWR KQGGKDLLLQ LRDLSDTIIP PSPVMFPEDR ETWNVQLFRS IDGGAAFGFP
DTPEEAAKAG LVSGKDQIID RSIQDAYIHA IRRAKNFIYI ENQYFLGSSY AWKPEGIKPE
DIGALHLIPK ELALKVVSKI EAGERFTVYV VVPMWPEGVP ESGSVQAILD WQRRTMEMMY
TDITEALQAK GIEANPKDYL TFFCLGNREV KQAGEYQPEE QPEADTDYSR AQEARRFMIY
VHTKMMIVDD EYIIIGSANI NQRSMDGARD SEIAMGGYQP YHLATRQPAR GQIHGFRMAL
WYEHLGMLDD VFQRPESLEC VQKVNRIAEK YWDMYSSDDL QQDLPGHLLS YPIGVASDGV
VTELPGMEYF PDTRARVLGA KSDYMPPILT S
//