ID A0A0E0FKU0_ORYNI Unreviewed; 1034 AA.
AC A0A0E0FKU0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 18-JUN-2025, entry version 44.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G15550.4};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G15550.4}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G15550.4}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G15550.4};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [3] {ECO:0000313|EnsemblPlants:ONIVA01G15550.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang J., Kudrna D., Lee S., Talag J., Rajasekar S., Welchert J.,
RA Hsing Y.-I., Wing R.A.;
RT "OnivRS2 (Oryza nivara Reference Sequence Version 2).";
RL Submitted (APR-2018) 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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR AlphaFoldDB; A0A0E0FKU0; -.
DR EnsemblPlants; ONIVA01G15550.4; ONIVA01G15550.4; ONIVA01G15550.
DR Gramene; ONIVA01G15550.4; ONIVA01G15550.4; ONIVA01G15550.
DR Proteomes; UP000006591; Chromosome 1.
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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
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; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00233; PH; 1.
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:UP000006591};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 395..422
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 830..857
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..585
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 116884 MW; CDFBC3B73ED8D8B7 CRC64;
MSGGRSAARE GEEAEEEEYG GGYVRMPQEP EGEAAAAGAG SFLRLPESAG AFDELPRARI
VGVSRPDAGD ITPMLLSYTV EVQYKQVKEW LQNLGIGEHM PVVHDDDEAD DVHVPSQHDE
HSVKNRNVPS SAVLPVIRPA LGRQQSVSDR AKVAMQEYLN HFLGNMEIVN SREVWAVLKP
GFLALLQDPF DPKLLDIVIF DVSPHMDRNG EGQSTLAREI KEHNPLHFAF EVSSGGRTIK
LRTRSSAKVK DWVSAINTAR RPPEGWSHPH RFGSFAPPRG LTEDGSVVQW FLDGQAAFNA
IASSIEEAKS EIFITDWWLC PELYLRRPFH HHESSRLDIL LESRAKQGVQ IYILLYKEVS
LALKINSMYS KQRLLNIHEN VKVLRYPDHF STGIYLWSHH EKIVIVDNQV CYIGGLDLCF
GRYDTPEHKV VDVPPSIWPG KDYYNPRESE PNSWEDTMKD ELDRTKYPRM PWHDVQCALY
GPACRDIARH FVQRWNYAKR NKAPNEQAIP LLMPQHHMVI PHYMGKIKES NEEVSKQTHV
EDIKGQKLSS LKAPASCQDI PLLLPHEPDH QASNNGELGL NGLDNNHGHS DHPNKTHWKQ
PIPNRKAKQD TSLQDLQMKG FVDNLGTPDV SSVIGHYDTS KQNVHHMDNE WWETQERGDQ
VDYVLDIGEV GPRATCCCQV VRSVGPWSAG TTQIEGSIHN AYFSLIEKAE HFVYIENQFF
ISGLSGDDTI KNRVLEALYR RILRAEKEKR CFRVIIVIPL LPGFQGGIDD GGAASVRAIM
HWQYRTICRG PNSILKNLYD VVGSKAHDYI SFYGLRAHGR LGDGGPLVTN QIYVHSKLMI
IDDRMTLIGS ANINDRSLLG SRDSEIGMII EDKEVVSSIM DGRHWEAGKF SLSLRLSLWA
EHLGLHPGEV SQIMDPVDDL TYNNIWMGTA KANTKIYQNV FSCVPDDHIH SRSQFRQGFA
HRKEKIGHTT IDLGVAVEIT ETHKDGDLAG TDPMEKLQAV RGHLVSFPLE FMCQEDLRPF
FGESEYYTSP QVFH
//
