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Database: UniProt
Entry: A0A0E0JHN9_ORYPU
LinkDB: A0A0E0JHN9_ORYPU
Original site: A0A0E0JHN9_ORYPU 
ID   A0A0E0JHN9_ORYPU        Unreviewed;       946 AA.
AC   A0A0E0JHN9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   18-JUN-2025, entry version 37.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G12780.4};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC01G12780.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC01G12780.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang J., Kudrna D., Lee S., Talag J., Welchert J., Wing R.A.;
RT   "OpunRS2 (Oryza punctata Reference Sequence Version 2).";
RL   Submitted (MAY-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; A0A0E0JHN9; -.
DR   EnsemblPlants; OPUNC01G12780.4; OPUNC01G12780.4; OPUNC01G12780.
DR   Gramene; OPUNC01G12780.4; OPUNC01G12780.4; OPUNC01G12780.
DR   HOGENOM; CLU_000690_2_0_1; -.
DR   Proteomes; UP000026962; 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; 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   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; 4.
DR   SMART; SM00155; PLDc; 2.
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:UP000026962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          308..335
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          742..769
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          445..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..498
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   946 AA;  107486 MW;  91670D240B6F3BBB CRC64;
     MSGGWSAAPE GEEEEEEYGP RYVRMPQGEA AAGSFLRLPE SAGAFDELPR ARIVGVSRPD
     AGDITPMLLS YTIEVQYKQV KEWLQNLGIG EHMPVVHDDD EADDVHVPSQ HDEHSVKNRN
     VPSSAVLPVI RPALGRQQSV SDRAKVAMQD YLNHFLGNLE IVNSREVWAV LKPGFLALLQ
     DPFDPKLLDI VIFDVSPHMG RNGEGQSALA REIKEHNPLH FAFEIFITDW WLCPELYLRR
     PFHHHEFSRL DILLESRAKQ GVQIYILLYK EVSLALKINS MYSKQRLLNI HENVKVLRYP
     DHFSTGIYLW SHHEKIVIVD NQVCYIGGLD LCFGRYDTPE HKVVDVPPSI WPGKDYYNPR
     ESEPNSWEDT MKDELDRTKY PRMPWHDVQC ALYGPACRDI ARHFVQRWNY AKRNKAPNEQ
     AIPLLMPQHH MVIPHYMGTI KETNEEASKQ THDEDIKGQR LSSLKTPASC QDIPLLLPHE
     PDHQASNNGD LGLNGLDNNH GHSDHPNKTH WKQPIPNRKA KQDTSLQDLQ MKGFVDNLGT
     PDASVIGHYD TSKQNVHHID NEWWETQERG DQVDSVLNIG EVGPRATCCC QVVRSVGPWS
     AGTTQIEGSI HNAYFSLIEK AEHFVYIENQ FFISGLSGDD TIKNRVLEAL YRRILRAEKE
     KRCFRVIIVI PLLPGFQGGI DDGGAASVRA IMHWQYRTIC RGPNSILKNL YDVVGSKAHD
     YISFYGLRAH GRLGDGGPLV TNQIYVHSKL MIIDDRMTLI GSANINDRSL LGSRDSEIGM
     IIEDKEFVSS IMDGRHWEAG KFSLSLRLSL WAEHLGLHPG EVSQIMDPVD DLTYNTIWMG
     TAKANTKIYQ NVFSCVPNDH IHSRSQFRQG FAHRKEKIGH TTIDLGVVVE TTETHKDGNL
     AGTDPMEKLQ AVRGHLVSFP LEFMCQEDLR PFFGESEYFT SPQVFH
//
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