PLD1_RAT
ID PLD1_RAT Reviewed; 1074 AA.
AC P70496; O08959; O35856; O54765; P70497; Q9QWJ6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Phospholipase D1 {ECO:0000305};
DE Short=PLD 1;
DE Short=rPLD1;
DE EC=3.1.4.4 {ECO:0000250|UniProtKB:Q13393};
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=Pld1 {ECO:0000312|RGD:3349};
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] (ISOFORMS PLD1A AND PLD1B).
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] OF 467-673 (ISOFORMS PLD1A AND PLD1B).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1B).
RX PubMed=9361006; DOI=10.1074/jbc.272.46.29263;
RA Park S.K., Provost J.J., Bae C.D., Ho W.T., Exton J.H.;
RT "Cloning and characterization of phospholipase D from rat brain.";
RL J. Biol. Chem. 272:29263-29271(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
RX PubMed=9445394; DOI=10.1042/bj3290647;
RA Katayama K., Kodaki T., Nagamachi Y., Yamashita S.;
RT "Cloning, differential regulation and tissue distribution of alternatively
RT spliced isoforms of ADP-ribosylation-factor-dependent phospholipase D from
RT rat liver.";
RL Biochem. J. 329:647-652(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-511.
RA Lassegue B., Alexander R.W., Griendling K.;
RT "Molecular cloning of a cDNA homologous to a phospholipase D1 segment.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1C).
RC TISSUE=Lung;
RA Park S.K., Exton J.H.;
RT "Phospholipase D not having transphosphatidylation reaction.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PALMITOYLATION AT CYS-240 AND CYS-241, MUTAGENESIS OF CYS-240 AND CYS-241,
RP AND PHOSPHORYLATION.
RX PubMed=11121416; DOI=10.1074/jbc.m009425200;
RA Xie Z., Ho W.T., Exton J.H.;
RT "Requirements and effects of palmitoylation of rat PLD1.";
RL J. Biol. Chem. 276:9383-9391(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-629, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Function as phospholipase selective for phosphatidylcholine
CC (By similarity). Implicated as a critical step in numerous cellular
CC pathways, including signal transduction, membrane trafficking, and the
CC regulation of mitosis. May be involved in the regulation of perinuclear
CC intravesicular membrane traffic (By similarity).
CC {ECO:0000250|UniProtKB:Q13393, ECO:0000250|UniProtKB:Q9Z280}.
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:0000250|UniProtKB:Q13393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000250|UniProtKB:Q13393};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + ethanol = 1,2-
CC diacyl-sn-glycero-3-phosphoethanol + choline; Xref=Rhea:RHEA:44868,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:16236, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:84672; Evidence={ECO:0000250|UniProtKB:Q13393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44869;
CC Evidence={ECO:0000250|UniProtKB:Q13393};
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:Q13393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873;
CC Evidence={ECO:0000250|UniProtKB:Q13393};
CC -!- ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, activated by
CC the phosphokinase C-alpha, by the ADP-ribosylation factor-1 (ARF-1),
CC and to a lesser extent by GTP-binding proteins: RHO A, RAC-1 and CDC42.
CC Inhibited by oleate. {ECO:0000250|UniProtKB:Q13393}.
CC -!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000250|UniProtKB:Q13393}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z280}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=PLD1A;
CC IsoId=P70496-1; Sequence=Displayed;
CC Name=PLD1B;
CC IsoId=P70496-2; Sequence=VSP_005024;
CC Name=PLD1C;
CC IsoId=P70496-3; Sequence=VSP_005025, VSP_005026;
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:11121416}.
CC -!- PTM: It is uncertain whether palmitoylation is on Cys-240 and/or Cys-
CC 241. Palmitoylation is required prior to phosphorylation.
CC {ECO:0000269|PubMed:11121416}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; AB003170; BAA24076.1; -; mRNA.
DR EMBL; AB003171; BAA24077.1; -; mRNA.
DR EMBL; U69550; AAB86910.1; -; mRNA.
DR EMBL; AB000778; BAA24576.1; -; mRNA.
DR EMBL; AB000779; BAA24577.1; -; mRNA.
DR EMBL; U88986; AAB91329.1; -; mRNA.
DR EMBL; AF017251; AAD01609.1; -; mRNA.
DR PIR; T13725; T13725.
DR PIR; T13732; T13732.
DR PIR; T13943; T13943.
DR PIR; T46635; T46635.
DR RefSeq; NP_112254.1; NM_030992.1.
DR AlphaFoldDB; P70496; -.
DR SMR; P70496; -.
DR BioGRID; 247168; 1.
DR IntAct; P70496; 1.
DR MINT; P70496; -.
DR STRING; 10116.ENSRNOP00000034466; -.
DR ChEMBL; CHEMBL3308939; -.
DR iPTMnet; P70496; -.
DR PhosphoSitePlus; P70496; -.
DR SwissPalm; P70496; -.
DR PaxDb; P70496; -.
DR PeptideAtlas; P70496; -.
DR PRIDE; P70496; -.
DR GeneID; 25096; -.
DR KEGG; rno:25096; -.
DR CTD; 5337; -.
DR RGD; 3349; Pld1.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; P70496; -.
DR PhylomeDB; P70496; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:P70496; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0031985; C:Golgi cisterna; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0031982; C:vesicle; 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:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:MGI.
DR GO; GO:0009395; P:phospholipid catabolic process; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:0032534; P:regulation of microvillus assembly; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
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; 1.
DR Pfam; PF00169; PH; 1.
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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1074
FT /note="Phospholipase D1"
FT /id="PRO_0000218804"
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 219..328
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 459..486
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 891..918
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 463..928
FT /note="Catalytic"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13393"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 240
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:11121416"
FT LIPID 241
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:11121416"
FT VAR_SEQ 585..623
FT /note="SYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSAD -> N (in
FT isoform PLD1B)"
FT /evidence="ECO:0000303|PubMed:8753790,
FT ECO:0000303|PubMed:9361006, ECO:0000303|PubMed:9445394,
FT ECO:0000303|PubMed:9533024"
FT /id="VSP_005024"
FT VAR_SEQ 586..590
FT /note="YFNHY -> ESRLR (in isoform PLD1C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_005025"
FT VAR_SEQ 591..1074
FT /note="Missing (in isoform PLD1C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_005026"
FT MUTAGEN 240
FT /note="C->A: Abolishes palmitoylation and weakens membrane
FT association; when associated with A-241."
FT /evidence="ECO:0000269|PubMed:11121416"
FT MUTAGEN 241
FT /note="C->A: Abolishes palmitoylation and weakens membrane
FT association; when associated with A-240."
FT /evidence="ECO:0000269|PubMed:11121416"
FT CONFLICT 4
FT /note="R -> K (in Ref. 4; BAA24576)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="S -> R (in Ref. 3 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="R -> K (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="N -> D (in Ref. 1, 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="I -> L (in Ref. 4; BAA24576)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="P -> A (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..736
FT /note="PG -> EV (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 739..740
FT /note="HA -> QP (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="S -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="H -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="S -> T (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="A -> C (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="H -> T (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="D -> N (in Ref. 1; BAA24076/BAA24077)"
FT /evidence="ECO:0000305"
FT CONFLICT 934..935
FT /note="TE -> RQ (in Ref. 3; AAB86910)"
FT /evidence="ECO:0000305"
FT CONFLICT 951..954
FT /note="FAQG -> SLSTV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1074 AA; 123814 MW; 286943A447A881DB CRC64;
MSLRSEARVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPT AQEACIPFSS
IYNTQGFKEP NIQIYLSGCP VKAQVLEVER FTSTSRMPSV NLYTIELTHG EFTWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENA IQEEQFFGRR
KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGVNC
CGHGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRIKVGKKE TETKYGLRID
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTDFLKDHRF GSYAAVHENI LAKWYVNAKG
YFEDIANAME GATEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVTSGQSLG SLTAASVESM ESLSLKDKHQ SHKNEPVLKS
VNDTDMKLKG IGKSRKFSKF SLYRQLHRRN LHNSDSISSV DSASSYFNHY RSHQNLIHGI
KPHLKLFRPS SESEQGLTRH SADTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
DKPFADFIDR YSTPRMPWHD IGSVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL
PKSQATAHEL RYQVPGAVHA KAQLLRSAAD WSAGIKHHEE SIHAAYTHVI ENSKHYIYIE
NQFFISCADD KVVFNKVGNA IAQRILKAHR EGQRYRVYIV IPLLPGFEGD ISTGGGNALQ
AIMHFNYRTM CRGESSILEQ LKPELGNKWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FAQGLRLECF
RLVLGYLSDP SEDIQDPVSD KFFKEIWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
NKPILAKEDR LRAEEELRKI RGFLVQFPFY FLSEENLLPS VGTKEAIVPM EVWT
