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Phospholipase D2 (PLD 2) (rPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2)

 PLD2_RAT                Reviewed;         933 AA.
P70498; O08768;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
22-NOV-2017, entry version 130.
RecName: Full=Phospholipase D2;
Short=PLD 2;
Short=rPLD2;
EC=3.1.4.4;
AltName: Full=Choline phosphatase 2;
AltName: Full=PLD1C;
AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D2;
Name=Pld2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9533024;
Nakashima S., Matsuda Y., Akao Y., Yoshimura S., Sakai H.,
Hayakawa K., Andoh M., Nozawa Y.;
"Molecular cloning and chromosome mapping of rat phospholipase D
genes, Pld1a, Pld1b and Pld2.";
Cytogenet. Cell Genet. 79:109-113(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=9111050; DOI=10.1074/jbc.272.17.11408;
Kodaki T., Yamashita S.;
"Cloning, expression, and characterization of a novel phospholipase D
complementary DNA from rat brain.";
J. Biol. Chem. 272:11408-11413(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 445-535.
TISSUE=Glial cell;
PubMed=8753790; DOI=10.1006/bbrc.1996.1201;
Yoshimura S., Nakashima S., Ohguchi K., Sakai H., Shinoda J.,
Sakai N., Nozawa Y.;
"Differential mRNA expression of phospholipase D (PLD) isozymes during
cAMP-induced differentiation in C6 glioma cells.";
Biochem. Biophys. Res. Commun. 225:494-499(1996).
[4]
FUNCTION IN MAST CELL ACTIVATION, AND PHOSPHORYLATION BY FGR.
PubMed=15282299; DOI=10.1128/MCB.24.16.6980-6992.2004;
Choi W.S., Hiragun T., Lee J.H., Kim Y.M., Kim H.P., Chahdi A.,
Her E., Han J.W., Beaven M.A.;
"Activation of RBL-2H3 mast cells is dependent on tyrosine
phosphorylation of phospholipase D2 by Fyn and Fgr.";
Mol. Cell. Biol. 24:6980-6992(2004).
-!- FUNCTION: May have a role in signal-induced cytoskeletal
regulation and/or endocytosis. {ECO:0000250,
ECO:0000269|PubMed:15282299}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate.
-!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4,5-
bisphosphate and phosphatidylethanolamine. Inhibited by
phosphatidylserine and by oleate. Is not responsive to ADP-
ribosylation factor 1 (ARF1), nor to GTP-binding protein RhoA.
-!- SUBUNIT: Interacts with PIP5K1B and EGFR. {ECO:0000250}.
-!- INTERACTION:
P33535:Oprm1; NbExp=3; IntAct=EBI-6140589, EBI-4392569;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, lung, heart, kidney,
stomach, small intestine, colon, and testis, and at a much lower
levels in thymus, liver and muscle.
-!- PTM: Phosphorylated on Tyr-11; most likely by EGFR (By
similarity). Phosphorylated by FGR. {ECO:0000250,
ECO:0000269|PubMed:15282299}.
-!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB003172; BAA24078.1; -; mRNA.
EMBL; D88672; BAA19882.1; -; mRNA.
PIR; PC4194; PC4194.
RefSeq; NP_150641.2; NM_033299.2.
UniGene; Rn.9798; -.
ProteinModelPortal; P70498; -.
BioGrid; 247169; 6.
IntAct; P70498; 2.
MINT; MINT-132445; -.
iPTMnet; P70498; -.
SwissPalm; P70498; -.
PRIDE; P70498; -.
GeneID; 25097; -.
KEGG; rno:25097; -.
UCSC; RGD:3350; rat.
CTD; 5338; -.
RGD; 3350; Pld2.
HOGENOM; HOG000246972; -.
HOVERGEN; HBG006650; -.
InParanoid; P70498; -.
KO; K01115; -.
PhylomeDB; P70498; -.
BRENDA; 3.1.4.4; 5301.
PRO; PR:P70498; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031526; C:brush border membrane; ISO:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0030027; C:lamellipodium; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0004630; F:phospholipase D activity; IDA:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0002031; P:G-protein coupled receptor internalization; ISO:RGD.
GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
GO; GO:0009395; P:phospholipid catabolic process; IMP:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:RGD.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0043434; P:response to peptide hormone; IMP:RGD.
GO; GO:0036465; P:synaptic vesicle recycling; IBA:GO_Central.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR001683; Phox.
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; 2.
Pfam; PF00614; PLDc; 1.
Pfam; PF13091; PLDc_2; 1.
Pfam; PF00787; PX; 1.
PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
SMART; SM00233; PH; 1.
SMART; SM00155; PLDc; 2.
SMART; SM00312; PX; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50035; PLD; 2.
PROSITE; PS50195; PX; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism;
Membrane; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 933 Phospholipase D2.
/FTId=PRO_0000218807.
DOMAIN 65 195 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 203 311 PH.
DOMAIN 437 464 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 751 778 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
REGION 441 788 Catalytic.
MOD_RES 11 11 Phosphotyrosine.
{ECO:0000250|UniProtKB:P97813}.
CONFLICT 26 26 V -> E (in Ref. 2; BAA19882).
{ECO:0000305}.
CONFLICT 125 125 N -> P (in Ref. 2; BAA19882).
{ECO:0000305}.
CONFLICT 599 599 G -> A (in Ref. 2; BAA19882).
{ECO:0000305}.
CONFLICT 792 792 K -> E (in Ref. 2; BAA19882).
{ECO:0000305}.
CONFLICT 817 818 GR -> KH (in Ref. 2; BAA19882).
{ECO:0000305}.
CONFLICT 919 924 HWGAKR -> PLGSKE (in Ref. 2; BAA19882).
{ECO:0000305}.
SEQUENCE 933 AA; 106037 MW; D430843B4D541EEA CRC64;
MTVTQTDLFP YGDYLNSSQL HMEPDVVDTL KEGEDPADRM HPFLAIYDLQ PLRAHPLVFA
PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLQRHKVL
MSLLNLARFA AAHSPAREAA NENIPSLPRG GSEGSARHTA SKQKYLENYL NRLLTMSFYR
NYHAMTEFLE VSQLSFIPDL GSKGLEGVIR KRSGGHRVPG FTCCGRDQVC YRWSKRWLVV
KDSFLLYMRP ETGAISFVQL FDPGFEVQVG KRSTEARYGV RIDTSHRSLI LKCSSYRQAR
WWGQEITELA QGPGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAREEIF
ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRTL
MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ AVAFLGGLDL AYGRWDDVQY RLTDLGDPSE
SADSQTPTPG SDPAATPDLS HNHFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW
RDVGVVVHGV AARDLARHFI QRWNFTKTIK ARYKIPQYPY LLPKSASTAN HLPFIIPGGQ
CATVQVLRSV DRWSAGTLES SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE
IVDRILKAHE QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR
LKAAMGTAWR DYMSICGLRT HGELGGHPIS ELIYIHSKLL IADDRTVIIG SANINDRSLL
GKRDSELAIL IKDTEMEPSL MDGVEYQAGR FALSLRGRCF SVILGANTWP DLDLRDPVCD
DFFQLWQETA ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIR
GHLVHFPLKF LEDESLLPHW GAKRGMIPLE VWT


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