PLD2_RAT
ID PLD2_RAT Reviewed; 933 AA.
AC P70498; O08768;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phospholipase D2 {ECO:0000305};
DE Short=PLD 2;
DE Short=rPLD2;
DE EC=3.1.4.4 {ECO:0000269|PubMed:9111050};
DE AltName: Full=Choline phosphatase 2;
DE AltName: Full=PLD1C;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D2;
GN Name=Pld2 {ECO:0000312|RGD:3350};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9533024; DOI=10.1159/000134694;
RA Nakashima S., Matsuda Y., Akao Y., Yoshimura S., Sakai H., Hayakawa K.,
RA Andoh M., Nozawa Y.;
RT "Molecular cloning and chromosome mapping of rat phospholipase D genes,
RT Pld1a, Pld1b and Pld2.";
RL Cytogenet. Cell Genet. 79:109-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, FUNCTION,
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=9111050; DOI=10.1074/jbc.272.17.11408;
RA Kodaki T., Yamashita S.;
RT "Cloning, expression, and characterization of a novel phospholipase D
RT complementary DNA from rat brain.";
RL J. Biol. Chem. 272:11408-11413(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 445-535.
RC TISSUE=Glial cell;
RX PubMed=8753790; DOI=10.1006/bbrc.1996.1201;
RA Yoshimura S., Nakashima S., Ohguchi K., Sakai H., Shinoda J., Sakai N.,
RA Nozawa Y.;
RT "Differential mRNA expression of phospholipase D (PLD) isozymes during
RT cAMP-induced differentiation in C6 glioma cells.";
RL Biochem. Biophys. Res. Commun. 225:494-499(1996).
RN [4]
RP FUNCTION IN MAST CELL ACTIVATION, AND PHOSPHORYLATION BY FGR.
RX PubMed=15282299; DOI=10.1128/mcb.24.16.6980-6992.2004;
RA Choi W.S., Hiragun T., Lee J.H., Kim Y.M., Kim H.P., Chahdi A., Her E.,
RA Han J.W., Beaven M.A.;
RT "Activation of RBL-2H3 mast cells is dependent on tyrosine phosphorylation
RT of phospholipase D2 by Fyn and Fgr.";
RL Mol. Cell. Biol. 24:6980-6992(2004).
CC -!- FUNCTION: Function as phospholipase selective for phosphatidylcholine
CC (By similarity) (PubMed:15282299, PubMed:9111050). May have a role in
CC signal-induced cytoskeletal regulation and/or endocytosis (By
CC similarity) (PubMed:15282299). {ECO:0000250|UniProtKB:P97813,
CC ECO:0000269|PubMed:15282299, ECO:0000269|PubMed:9111050}.
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:0000269|PubMed:9111050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000305|PubMed:9111050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:44872, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72859, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P97813};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873;
CC Evidence={ECO:0000250|UniProtKB:P97813};
CC -!- ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylethanolamine. Inhibited by
CC phosphatidylserine and by oleate. Is not responsive to ADP-ribosylation
CC factor 1 (ARF1), nor to GTP-binding protein RhoA.
CC {ECO:0000269|PubMed:9111050}.
CC -!- SUBUNIT: Interacts with PIP5K1B (By similarity). Interacts with EGFR
CC (By similarity). {ECO:0000250|UniProtKB:O14939,
CC ECO:0000250|UniProtKB:P97813}.
CC -!- INTERACTION:
CC P70498; P33535: Oprm1; NbExp=3; IntAct=EBI-6140589, EBI-4392569;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97813};
CC Lipid-anchor {ECO:0000250|UniProtKB:P97813}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, heart, kidney, stomach,
CC small intestine, colon, and testis, and at a much lower levels in
CC thymus, liver and muscle. {ECO:0000269|PubMed:9111050}.
CC -!- PTM: Phosphorylated by FGR (PubMed:15282299). Phosphorylated on Tyr-11;
CC most likely by EGFR (By similarity). {ECO:0000250|UniProtKB:P97813,
CC ECO:0000269|PubMed:15282299}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; AB003172; BAA24078.1; -; mRNA.
DR EMBL; D88672; BAA19882.1; -; mRNA.
DR PIR; PC4194; PC4194.
DR RefSeq; NP_150641.2; NM_033299.2.
DR AlphaFoldDB; P70498; -.
DR SMR; P70498; -.
DR BioGRID; 247169; 6.
DR IntAct; P70498; 2.
DR MINT; P70498; -.
DR STRING; 10116.ENSRNOP00000053831; -.
DR iPTMnet; P70498; -.
DR SwissPalm; P70498; -.
DR jPOST; P70498; -.
DR PRIDE; P70498; -.
DR GeneID; 25097; -.
DR KEGG; rno:25097; -.
DR UCSC; RGD:3350; rat.
DR CTD; 5338; -.
DR RGD; 3350; Pld2.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; P70498; -.
DR OrthoDB; 755722at2759; -.
DR PhylomeDB; P70498; -.
DR BRENDA; 3.1.4.4; 5301.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR PRO; PR:P70498; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IDA:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:RGD.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IMP:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IMP:RGD.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1520.10; -; 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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896; PTHR18896; 2.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..933
FT /note="Phospholipase D2"
FT /id="PRO_0000218807"
FT DOMAIN 65..195
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 203..311
FT /note="PH"
FT DOMAIN 437..464
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 751..778
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 441..788
FT /note="Catalytic"
FT REGION 476..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97813"
FT CONFLICT 26
FT /note="V -> E (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> P (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="G -> A (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="K -> E (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
FT CONFLICT 817..818
FT /note="GR -> KH (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
FT CONFLICT 919..924
FT /note="HWGAKR -> PLGSKE (in Ref. 2; BAA19882)"
FT /evidence="ECO:0000305"
SQ 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
