PLD1_MOUSE
ID PLD1_MOUSE Reviewed; 1074 AA.
AC Q9Z280; O35911;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phospholipase D1 {ECO:0000305};
DE Short=PLD 1;
DE Short=mPLD1;
DE EC=3.1.4.4 {ECO:0000269|PubMed:9395408};
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=Pld1 {ECO:0000312|MGI:MGI:109585};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
RC STRAIN=129; TISSUE=Embryonic brain, and Neonatal brain;
RX PubMed=9307024; DOI=10.1042/bj3260745;
RA Colley W.C., Altshuller Y.M., Sue-Ling C.K., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Branch K.D., Tsirka S.E., Bollag R.J., Bollag W.B.,
RA Frohman M.A.;
RT "Cloning and expression analysis of murine phospholipase D1.";
RL Biochem. J. 326:745-753(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PLD1A).
RC STRAIN=129;
RX PubMed=9813240; DOI=10.1016/s0378-1119(98)00465-x;
RA Redina O.E., Frohman M.A.;
RT "Genomic analysis of murine phospholipase D1 and comparison to
RT phospholipase D2 reveals an unusual difference in gene size.";
RL Gene 222:53-60(1998).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9395408; DOI=10.1016/s0960-9822(97)70090-3;
RA Colley W.C., Sung T.-C., Roll R., Jenco J.M., Hammond S.M.,
RA Altshuller Y.M., Bar-Sagi D., Morris A.J., Frohman M.A.;
RT "Phospholipase D2, a distinct phospholipase D isoform with novel regulatory
RT properties that provokes cytoskeletal reorganization.";
RL Curr. Biol. 7:191-201(1997).
CC -!- FUNCTION: Function as phospholipase selectivefor phosphatidylcholine
CC (PubMed:9395408). 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 (PubMed:9395408).
CC {ECO:0000269|PubMed:9395408}.
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:9395408};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000305|PubMed:9395408};
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 -!- INTERACTION:
CC Q9Z280; P49769: Psen1; NbExp=2; IntAct=EBI-15566315, EBI-990067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:9395408}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PLD1A;
CC IsoId=Q9Z280-1; Sequence=Displayed;
CC Name=PLD1B;
CC IsoId=Q9Z280-2; Sequence=VSP_005023;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung, and at a much lower
CC levels, in brain, liver, heart, testis and spleen.
CC -!- DEVELOPMENTAL STAGE: Expressed most strikingly in selected ventricular
CC cells lining the spinal cord and brain. The level of expression
CC decreases dramatically as the cells differentiate into neurons and
CC migrate to the outer layer of the spinal cord and brain. Expression is
CC observed during development in a restricted region of the nasal
CC neuroepithelium.
CC -!- DISEASE: Note=Defects in Pld1 may result in coa which is associated
CC with coat color dilution and white spotting. It is also associated with
CC platelet-storage pool deficiency characterized by decreased levels in
CC serotonin and dense granules.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; U87868; AAB81245.1; -; mRNA.
DR EMBL; AF083497; AAC84041.1; -; Genomic_DNA.
DR EMBL; AF083475; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083476; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083478; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083479; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083480; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083481; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083483; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083484; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083485; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083486; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083488; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083489; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083490; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083492; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083494; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083495; AAC84041.1; JOINED; Genomic_DNA.
DR EMBL; AF083496; AAC84041.1; JOINED; Genomic_DNA.
DR CCDS; CCDS17275.1; -. [Q9Z280-2]
DR CCDS; CCDS89617.1; -. [Q9Z280-1]
DR PIR; T17203; T17203.
DR PIR; T42093; T42093.
DR AlphaFoldDB; Q9Z280; -.
DR SMR; Q9Z280; -.
DR DIP; DIP-61103N; -.
DR IntAct; Q9Z280; 1.
DR STRING; 10090.ENSMUSP00000113810; -.
DR ChEMBL; CHEMBL3309054; -.
DR iPTMnet; Q9Z280; -.
DR PhosphoSitePlus; Q9Z280; -.
DR SwissPalm; Q9Z280; -.
DR MaxQB; Q9Z280; -.
DR PaxDb; Q9Z280; -.
DR PRIDE; Q9Z280; -.
DR ProteomicsDB; 289542; -. [Q9Z280-1]
DR ProteomicsDB; 289543; -. [Q9Z280-2]
DR MGI; MGI:109585; Pld1.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; Q9Z280; -.
DR PhylomeDB; Q9Z280; -.
DR BRENDA; 3.1.4.4; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR ChiTaRS; Pld1; mouse.
DR PRO; PR:Q9Z280; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z280; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0098981; C:cholinergic synapse; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0032534; P:regulation of microvillus assembly; ISO:MGI.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:MGI.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
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_0000218803"
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:0000250|UniProtKB:P70496"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13393"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13393"
FT LIPID 240
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 241
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 585..623
FT /note="SYFSHCRSHQNLIHGLKPHLKLFHPSSESEQGLTRHSTD -> N (in
FT isoform PLD1B)"
FT /evidence="ECO:0000303|PubMed:9307024"
FT /id="VSP_005023"
FT CONFLICT 71..74
FT /note="NIQT -> QHPD (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="A -> V (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="R -> G (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="N -> I (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="C -> V (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="T -> A (in Ref. 1; AAB81245)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071..1073
FT /note="EVW -> SLT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1074 AA; 123969 MW; E11260982A217280 CRC64;
MSLKSETRVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPK AQEGCIPFSS
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTSRVPSI NLYTIELTHG EFTWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENA IQEEQFFGRR
KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGVNC
CGHGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRVKVGRKE TETKYGLRID
NLSRTLILKC NSYRHARWWG GAIEEFIRKH GADFLKDHRF GSYAALHENT LAKWYVNAKG
YFEDIANAME EASEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYSKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVTSGLSLG SLTAASVESM ESLSLKDKHE FHKKEPISKI
VDETDMKLKG IGKSRKFSKF SLYRQLHRHH LHNADSISSI DSTSSYFSHC RSHQNLIHGL
KPHLKLFHPS SESEQGLTRH STDTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
DKPFADFIDR YSTPRMPWHD IGSVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL
PKSQATAHEL RYQVPGAVPA KVQLLRSAAD WSAGIKHHEE SIHAAYIHVI ENSKHYIYIE
NQFFISCADD KVVFNKVGDR IAQRILKAHR EGQRYRVYIV IPLLPGFEGD ISTGGGNALQ
AIMHFNYRTM CRGESSILEQ LKPELGNKWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARDLRLECF
RLVLGYLSDP SEDLQDPVSD KFFKEIWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
NKPILAKEDA LRAEEELRKI RGFLVQFPLY FLSEENLLPS VGTKEAIVPM EVWT
