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Phospholipase (EC 3.1.4.4)

 A0A1I9LQ38_ARATH        Unreviewed;       990 AA.
A0A1I9LQ38;
15-FEB-2017, integrated into UniProtKB/TrEMBL.
15-FEB-2017, sequence version 1.
22-NOV-2017, entry version 8.
RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
Name=PLDP1 {ECO:0000313|EMBL:ANM64696.1};
Synonyms=PHOSPHOLIPASE D {ECO:0000313|EMBL:ANM64696.1},
PHOSPHOLIPASE D P1 {ECO:0000313|EMBL:ANM64696.1},
phospholipase D P1 {ECO:0000313|EMBL:ANM64696.1},
PHOSPHOLIPASE D ZETA 1 {ECO:0000313|EMBL:ANM64696.1},
PHOSPHOLIPASE D ZETA1 {ECO:0000313|EMBL:ANM64696.1},
PLD ZETA 1 {ECO:0000313|EMBL:ANM64696.1},
PLDZ1 {ECO:0000313|EMBL:ANM64696.1},
PLDZETA1 {ECO:0000313|EMBL:ANM64696.1};
OrderedLocusNames=At3g16785 {ECO:0000313|EMBL:ANM64696.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM64696.1, ECO:0000313|Proteomes:UP000006548};
[1] {ECO:0000313|EMBL:ANM64696.1, ECO:0000313|Proteomes:UP000006548}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=11130713; DOI=10.1038/35048706;
European Union Chromosome 3 Arabidopsis Sequencing Consortium;
Institute for Genomic Research;
Kazusa DNA Research Institute;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Blocker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schafer M., Muller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E.,
Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H.,
Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M.,
Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K.,
Kauer G., Lohnert T.H., Nordsiek G., Reichelt J., Scharfe M.,
Schon O., Bargues M., Terol J., Climent J., Navarro P., Collado C.,
Perez-Perez A., Ottenwalder B., Duchemin D., Cooke R., Laudie M.,
Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C.,
Alcaraz J.P., Cottet A., Casacuberta E., Monfort A., Argiriou A.,
flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H.,
Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S., Town C.D.,
Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A.,
Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R.,
Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P.,
Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T.,
Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T.,
Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N.,
Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2] {ECO:0000313|EMBL:ANM64696.1}
NUCLEOTIDE SEQUENCE.
TAIR;
Swarbreck D., Lamesch P., Wilks C., Huala E.;
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000213|PubMed:22223895}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large scale characterization of plant versus mammal
proteins reveals similar and idiosyncratic N-alpha-acetylation
features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[4] {ECO:0000313|EMBL:ANM64696.1, ECO:0000313|Proteomes:UP000006548}
GENOME REANNOTATION.
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
Lavstsen T., Jespersen J.S.;
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate. {ECO:0000256|PIRNR:PIRNR009376}.
-!- SIMILARITY: Belongs to the phospholipase D family.
{ECO:0000256|PIRNR:PIRNR009376}.
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EMBL; CP002686; ANM64696.1; -; Genomic_DNA.
EMBL; CP002686; ANM64697.1; -; Genomic_DNA.
RefSeq; NP_001326707.1; NM_001338259.1.
RefSeq; NP_001326708.1; NM_001338258.1.
UniGene; At.21958; -.
EnsemblPlants; AT3G16785.5; AT3G16785.5; AT3G16785.
EnsemblPlants; AT3G16785.6; AT3G16785.6; AT3G16785.
GeneID; 820932; -.
Gramene; AT3G16785.5; AT3G16785.5; AT3G16785.
Gramene; AT3G16785.6; AT3G16785.6; AT3G16785.
Proteomes; UP000006548; Chromosome 3.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR025202; PLD-like_dom.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
InterPro; IPR016555; PLipase_D_euk.
InterPro; IPR015679; PLipase_D_fam.
InterPro; IPR036871; PX_dom_sf.
PANTHER; PTHR18896; PTHR18896; 1.
Pfam; PF00614; PLDc; 1.
Pfam; PF13091; PLDc_2; 1.
PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
SMART; SM00233; PH; 1.
SMART; SM00155; PLDc; 2.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000006548};
Hydrolase {ECO:0000256|PIRNR:PIRNR009376};
Lipid degradation {ECO:0000256|PIRNR:PIRNR009376};
Lipid metabolism {ECO:0000256|PIRNR:PIRNR009376};
Reference proteome {ECO:0000313|Proteomes:UP000006548}.
DOMAIN 251 342 PH. {ECO:0000259|PROSITE:PS50003}.
DOMAIN 477 504 PLD phosphodiesterase.
{ECO:0000259|PROSITE:PS50035}.
DOMAIN 892 919 PLD phosphodiesterase.
{ECO:0000259|PROSITE:PS50035}.
SEQUENCE 990 AA; 112239 MW; 85F16E40A5631C95 CRC64;
MASEQLMSPA SGGGRYFQMQ PEQFPSMVSS LFSFAPAPTQ ETNRIFEELP KAVIVSVSRP
DAGDISPVLL SYTIECQYKQ FKWQLVKKAS QVFYLHFALK KRAFIEEIHE KQEQVKEWLQ
NLGIGDHPPV VQDEDADEVP LHQDESAKNR DVPSSAALPV IRPLGRQQSI SVRGKHAMQE
YLNHFLGNLD IVNSREVCRF LEVSMLSFSP EYGPKLKEDY IMVKHLPKFS KSDDDSNRCC
GCCWFCCCND NWQKVWGVLK PGFLALLEDP FDAKLLDIIV FDVLPVSNGN DGVDISLAVE
LKDHNPLRHA FKVTSGNRSI RIRAKNSAKV KDWVASINDA ALRPPEGWCH PHRFGSYAPP
RGLTDDGSQA QWFVDGGAAF AAIAAAIENA KSEIFICGWW VCPELYLRRP FDPHTSSRLD
NLLENKAKQG VQIYILIYKE VALALKINSV YSKRRLLGIH ENVRVLRYPD HFSSGVYLWS
HHEKLVIVDN QVCFIGGLDL CFGRYDTFEH KVGDNPSVTW PGKDYYNPRE SEPNTWEDAL
KDELERKKHP RMPWHDVHCA LWGPPCRDVA RHFVQRWNYA KRNKAPYEDS IPLLMPQHHM
VIPHYMGRQE ESDIESKKEE DSIRGIRRDD SFSSRSSLQD IPLLLPHEPV DQDGSSGGHK
ENGTNNRNGP FSFRKSKIEP VDGDTPMRGF VDDRNGLDLP VAKRGSNAID SEWWETQDHD
YQVGSPDETG QVGPRTSCRC QIIRSVSQWS AGTSQVEESI HSAYRSLIDK AEHFIYIENQ
FFISGLSGDD TVKNRVLEAL YKRILRAHNE KKIFRVVVVI PLLPGFQGGI DDSGAASVRA
IMHWQYRTIY RGHNSILTNL YNTIGVKAHD YISFYGLRAY GKLSEDGPVA TSQVYVHSKI
MIVDDRAALI GSANINDRSL LGSRDSEIGV LIEDTELVDS RMAGKPWKAG KFSSSLRLSL
WSEHLGLRTG EVCVIFSIMF LRSGLRYFSI


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