ID A0A0E0P3P8_ORYRU Unreviewed; 847 AA.
AC A0A0E0P3P8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:ORUFI03G42170.1, 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:ORUFI03G42170.1}
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}.
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 AlphaFoldDB; A0A0E0P3P8; -.
DR STRING; 4529.A0A0E0P3P8; -.
DR EnsemblPlants; ORUFI03G42170.1; ORUFI03G42170.1; ORUFI03G42170.
DR Gramene; ORUFI03G42170.1; ORUFI03G42170.1; ORUFI03G42170.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR OMA; NARVCHE; -.
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:SF199; 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|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 1..155
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 355..390
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 691..718
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 847 AA; 94803 MW; 58F940DF6E3CE2F0 CRC64;
MGKSSADLSA SSESAVLLHG DLDIWITEAK CLPNMDIMSE RMRRFFTGYG ACGSSCGGTG
DNARRAGGGV RPKKIITSDP YVSVCLAGAT VAQTRVIPNS ENPRWEERFR VEVAHAVSRL
EFHVKDNDVF GAQLIGVASL PVDRILSGAP AEGWFPIDGH CSSNPMRPPP ELRLSVQYRP
IDDNPLYRGG AGAVPNAYFP LRRGGGVTLY QDAHVADGGL PAIQIAGGRA YEHGRCWEDI
CHSIVEAHHL VYMVGWSIYH PVKLVREPTR ALPGETPSTL GELLKKRARE GVRIVILLWD
DKTSHDKFLL KTDGVMHTHD EETKKFFRHS GVHCVLVPRY ASTKLSIFKQ QVVGTLFTHH
QKCVLVDTQA TGNNRKITAF IGGLDLCDGR YDTPEHRLFK DLDTAFNKDF HNPTFPVNSY
GPRQPWHDLH CKIEGPAAFD ILTNFEQRWR KATKWKVNLK KVASWHHDTL IKINRMSWIV
TPAADEANAH VCEEKDPENW HVQVFRSIDS GSVKGFPKIV QEAESQNLVC AKNLKIDKSI
HSAYVKAIRS AQHFIYIENQ YFIGSSFLWS SHKSAGADNL IPVELALKIA SKIKANEQFA
VYIVLPMWPE GIPTAAPMQQ ILFWQSQTMS MMYKIIADAL QMQGLVEAHP QDYLNFYCLG
KREVAAGDSM SQTSLCNDNS TLRSAQKLRR FMIYVHSKGM VVDDEYVIIG SANINQRSME
GCRDTEIAMG AYQPHYKWSA DHGQGPPRGQ VYGYRMSLWA EHLGAVEECF GRPETGECVR
RVREMAEENW RAYVSPEMEE TKGHLMCYPL KVDKDGRVRS LPGHDCFPDV GGKVLGTQTS
LPNALTT
//