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Database: UniProt
Entry: A0A0E0JHN7_ORYPU
LinkDB: A0A0E0JHN7_ORYPU
Original site: A0A0E0JHN7_ORYPU 
ID   A0A0E0JHN7_ORYPU        Unreviewed;      1026 AA.
AC   A0A0E0JHN7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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:OPUNC01G12780.2};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC01G12780.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC01G12780.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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; A0A0E0JHN7; -.
DR   EnsemblPlants; OPUNC01G12780.2; OPUNC01G12780.2; OPUNC01G12780.
DR   Gramene; OPUNC01G12780.2; OPUNC01G12780.2; OPUNC01G12780.
DR   Proteomes; UP000026962; Chromosome 1.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 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:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT   DOMAIN          388..415
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          822..849
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          525..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  116164 MW;  DB8E7CB7BFCB14CF CRC64;
     MSGGWSAAPE GEEEEEEYGP RYVRMPQGEA AAGSFLRLPE SAGAFDELPR ARIVGVSRPD
     AGDITPMLLS YTIEVQYKQV KEWLQNLGIG EHMPVVHDDD EADDVHVPSQ HDEHSVKNRN
     VPSSAVLPVI RPALGRQQSV SDRAKVAMQD YLNHFLGNLE IVNSREVWAV LKPGFLALLQ
     DPFDPKLLDI VIFDVSPHMG RNGEGQSALA REIKEHNPLH FAFEVSSGGR TIKLRTRSSA
     KVKDWVSAIN TARRPPEGWS HPHRFGSFAP PRGLTEDGSV VQWFLDGKAA FNAIASSIEE
     AKSEIFITDW 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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