ID PLD1_HUMAN Reviewed; 1074 AA.
AC Q13393;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 215.
DE RecName: Full=Phospholipase D1 {ECO:0000305};
DE Short=PLD 1;
DE Short=hPLD1;
DE EC=3.1.4.4 {ECO:0000269|PubMed:25936805, ECO:0000269|PubMed:8530346};
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=PLD1 {ECO:0000312|HGNC:HGNC:9067};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1A), CATALYTIC ACTIVITY, FUNCTION,
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=8530346; DOI=10.1074/jbc.270.50.29640;
RA Hammond S.M., Altshuller Y.M., Sung T.-C., Rudge S.A., Rose K.,
RA Engebrecht J., Morris A.J., Frohman M.A.;
RT "Human ADP-ribosylation factor-activated phosphatidylcholine-specific
RT phospholipase D defines a new and highly conserved gene family.";
RL J. Biol. Chem. 270:29640-29643(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
RX PubMed=9013646; DOI=10.1074/jbc.272.6.3860;
RA Hammond S.M., Jenco J.M., Nakashima S., Cadwallader K., Gu Q.-M., Cook S.,
RA Nozawa Y., Prestwich G.D., Frohman M.A., Morris A.J.;
RT "Characterization of two alternately spliced forms of phospholipase D1.
RT Activation of the purified enzymes by phosphatidylinositol 4,5-
RT bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding
RT proteins and protein kinase C-alpha.";
RL J. Biol. Chem. 272:3860-3868(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A; PLD1B AND PLD1C).
RC TISSUE=Brain, Cervix carcinoma, Chondrocyte, and Skeletal muscle;
RX PubMed=9761774; DOI=10.1096/fasebj.12.13.1309;
RA Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.;
RT "Characterization of human PLD2 and the analysis of PLD isoform splice
RT variants.";
RL FASEB J. 12:1309-1317(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD1A).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 739-1074 (ISOFORM PLD1D).
RA Hughes W.E., Parker P.J.;
RT "A novel human phospholipase D1 splice variant displays conserved
RT regulation in vitro but altered localisation in vivo.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9582313; DOI=10.1074/jbc.273.21.12846;
RA Lopez I., Arnold R.S., Lambeth J.D.;
RT "Cloning and initial characterization of a human phospholipase D2 (hPLD2).
RT ADP-ribosylation factor regulates hPLD2.";
RL J. Biol. Chem. 273:12846-12852(1998).
RN [7]
RP INTERACTION WITH PIP5K1B.
RX PubMed=11032811; DOI=10.1093/emboj/19.20.5440;
RA Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M.,
RA Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
RT "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for
RT the local generation of phosphatidylinositol 4, 5-bisphosphate in the
RT regulation of PLD2 activity.";
RL EMBO J. 19:5440-5449(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-629, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25936805; DOI=10.1016/j.molcel.2015.03.028;
RA Yoon M.S., Rosenberger C.L., Wu C., Truong N., Sweedler J.V., Chen J.;
RT "Rapid mitogenic regulation of the mTORC1 inhibitor, DEPTOR, by
RT phosphatidic acid.";
RL Mol. Cell 58:549-556(2015).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INVOLVEMENT IN CVDP1, AND VARIANT CVDP1 PRO-442.
RX PubMed=27799408; DOI=10.1136/jmedgenet-2016-104259;
RA Ta-Shma A., Zhang K., Salimova E., Zernecke A., Sieiro-Mosti D.,
RA Stegner D., Furtado M., Shaag A., Perles Z., Nieswandt B., Rein A.J.,
RA Rosenthal N., Neiman A.M., Elpeleg O.;
RT "Congenital valvular defects associated with deleterious mutations in the
RT PLD1 gene.";
RL J. Med. Genet. 54:278-286(2017).
CC -!- FUNCTION: Function as phospholipase selective for phosphatidylcholine
CC (PubMed:8530346, PubMed:9582313, PubMed:25936805). Implicated as a
CC critical step in numerous cellular pathways, including signal
CC transduction, membrane trafficking, and the regulation of mitosis. May
CC be involved in the regulation of perinuclear intravesicular membrane
CC traffic (By similarity). {ECO:0000250|UniProtKB:Q9Z280,
CC ECO:0000269|PubMed:25936805, ECO:0000269|PubMed:8530346,
CC ECO:0000269|PubMed:9582313}.
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:25936805, ECO:0000269|PubMed:8530346,
CC ECO:0000269|PubMed:9582313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000305|PubMed:25936805, ECO:0000305|PubMed:8530346,
CC ECO:0000305|PubMed:9582313};
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:0000269|PubMed:8530346};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44869;
CC Evidence={ECO:0000305|PubMed:8530346};
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:0000269|PubMed:8530346, ECO:0000269|PubMed:9582313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873;
CC Evidence={ECO:0000305|PubMed:8530346, ECO:0000305|PubMed:9582313};
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:0000269|PubMed:8530346,
CC ECO:0000269|PubMed:9582313}.
CC -!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000269|PubMed:11032811}.
CC -!- INTERACTION:
CC Q13393; P05067: APP; NbExp=3; IntAct=EBI-2827556, EBI-77613;
CC Q13393; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-2827556, EBI-10254793;
CC Q13393; P23528: CFL1; NbExp=4; IntAct=EBI-2827556, EBI-352733;
CC Q13393; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-2827556, EBI-10213520;
CC Q13393; O15287: FANCG; NbExp=3; IntAct=EBI-2827556, EBI-81610;
CC Q13393; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2827556, EBI-6509505;
CC Q13393; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-2827556, EBI-25830459;
CC Q13393; Q15382: RHEB; NbExp=2; IntAct=EBI-2827556, EBI-1055287;
CC Q13393; Q08AE8: SPIRE1; NbExp=3; IntAct=EBI-2827556, EBI-1055655;
CC Q13393; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-2827556, EBI-11285923;
CC Q13393; P15923-3: TCF3; NbExp=3; IntAct=EBI-2827556, EBI-12000326;
CC Q13393; Q12888: TP53BP1; NbExp=3; IntAct=EBI-2827556, EBI-396540;
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=4;
CC Name=PLD1A;
CC IsoId=Q13393-1; Sequence=Displayed;
CC Name=PLD1B;
CC IsoId=Q13393-2; Sequence=VSP_005020;
CC Name=PLD1C;
CC IsoId=Q13393-3; Sequence=VSP_005018, VSP_005019;
CC Name=PLD1D;
CC IsoId=Q13393-4; Sequence=VSP_005021, VSP_005022;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the pancreas and heart and
CC at high levels in brain, placenta, spleen, uterus and small intestine.
CC {ECO:0000269|PubMed:9582313}.
CC -!- DISEASE: Cardiac valvular dysplasia 1 (CVDP1) [MIM:212093]: An
CC autosomal recessive form of congenital heart defects, characterized by
CC valvular malformations involving the pulmonic, tricuspid and mitral
CC valves. {ECO:0000269|PubMed:27799408}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phospholipase D entry;
CC URL="https://en.wikipedia.org/wiki/Phospholipase_D";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/43716/PLD1";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U38545; AAB49031.1; -; mRNA.
DR EMBL; BC068976; AAH68976.1; -; mRNA.
DR EMBL; AJ276230; CAB76564.1; -; mRNA.
DR CCDS; CCDS3216.1; -. [Q13393-1]
DR CCDS; CCDS46957.1; -. [Q13393-2]
DR RefSeq; NP_002653.1; NM_002662.4. [Q13393-1]
DR RefSeq; XP_005247590.1; XM_005247533.2. [Q13393-1]
DR RefSeq; XP_005247591.1; XM_005247534.2. [Q13393-2]
DR RefSeq; XP_011511199.1; XM_011512897.1. [Q13393-4]
DR PDB; 6U8Z; X-ray; 1.80 A; A=330-1074.
DR PDBsum; 6U8Z; -.
DR AlphaFoldDB; Q13393; -.
DR SMR; Q13393; -.
DR BioGRID; 111353; 132.
DR CORUM; Q13393; -.
DR DIP; DIP-40821N; -.
DR IntAct; Q13393; 48.
DR MINT; Q13393; -.
DR STRING; 9606.ENSP00000342793; -.
DR BindingDB; Q13393; -.
DR ChEMBL; CHEMBL2536; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB05301; LAX-101.
DR DrugBank; DB09031; Miltefosine.
DR DrugCentral; Q13393; -.
DR GuidetoPHARMACOLOGY; 1433; -.
DR SwissLipids; SLP:000000149; -.
DR GlyGen; Q13393; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q13393; -.
DR PhosphoSitePlus; Q13393; -.
DR SwissPalm; Q13393; -.
DR BioMuta; PLD1; -.
DR DMDM; 2499703; -.
DR EPD; Q13393; -.
DR jPOST; Q13393; -.
DR MassIVE; Q13393; -.
DR MaxQB; Q13393; -.
DR PaxDb; 9606-ENSP00000342793; -.
DR PeptideAtlas; Q13393; -.
DR ProteomicsDB; 59360; -. [Q13393-1]
DR ProteomicsDB; 59361; -. [Q13393-2]
DR ProteomicsDB; 59362; -. [Q13393-3]
DR ProteomicsDB; 59363; -. [Q13393-4]
DR Pumba; Q13393; -.
DR TopDownProteomics; Q13393-2; -. [Q13393-2]
DR Antibodypedia; 3866; 333 antibodies from 40 providers.
DR DNASU; 5337; -.
DR Ensembl; ENST00000351298.9; ENSP00000342793.4; ENSG00000075651.17. [Q13393-1]
DR Ensembl; ENST00000356327.9; ENSP00000348681.5; ENSG00000075651.17. [Q13393-2]
DR GeneID; 5337; -.
DR KEGG; hsa:5337; -.
DR MANE-Select; ENST00000351298.9; ENSP00000342793.4; NM_002662.5; NP_002653.1.
DR UCSC; uc003fhs.4; human. [Q13393-1]
DR AGR; HGNC:9067; -.
DR CTD; 5337; -.
DR DisGeNET; 5337; -.
DR GeneCards; PLD1; -.
DR HGNC; HGNC:9067; PLD1.
DR HPA; ENSG00000075651; Tissue enhanced (gallbladder).
DR MalaCards; PLD1; -.
DR MIM; 212093; phenotype.
DR MIM; 602382; gene.
DR neXtProt; NX_Q13393; -.
DR OpenTargets; ENSG00000075651; -.
DR PharmGKB; PA164742228; -.
DR VEuPathDB; HostDB:ENSG00000075651; -.
DR eggNOG; KOG1329; Eukaryota.
DR GeneTree; ENSGT00940000155015; -.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; Q13393; -.
DR OMA; EWRLDQI; -.
DR OrthoDB; 335467at2759; -.
DR PhylomeDB; Q13393; -.
DR TreeFam; TF300589; -.
DR BioCyc; MetaCyc:HS01185-MONOMER; -.
DR BRENDA; 3.1.4.4; 2681.
DR PathwayCommons; Q13393; -.
DR Reactome; R-HSA-1483148; Synthesis of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q13393; -.
DR SIGNOR; Q13393; -.
DR BioGRID-ORCS; 5337; 12 hits in 1159 CRISPR screens.
DR ChiTaRS; PLD1; human.
DR GeneWiki; Phospholipase_D1; -.
DR GenomeRNAi; 5337; -.
DR Pharos; Q13393; Tchem.
DR PRO; PR:Q13393; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q13393; Protein.
DR Bgee; ENSG00000075651; Expressed in gall bladder and 178 other cell types or tissues.
DR ExpressionAtlas; Q13393; baseline and differential.
DR Genevisible; Q13393; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
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:UniProtKB.
DR GO; GO:0031670; P:cellular response to nutrient; IDA:UniProt.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IMP:CACAO.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0032534; P:regulation of microvillus assembly; IMP:UniProtKB.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09842; PLDc_vPLD1_1; 1.
DR CDD; cd09844; PLDc_vPLD1_2; 1.
DR CDD; cd07296; PX_PLD1; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1074
FT /note="Phospholipase D1"
FT /id="PRO_0000218802"
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 219..328
FT /note="PH"
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:0007744|PubMed:23186163"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
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 514..597
FT /note="PAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQ
FT LHRHHLHDADSISSIDSTSSYFNHYRSHHNLI -> IPGPSVVYRQVWESCMGKPDSGM
FT ERTTAISSSKTGFNLINLLLISLTGTPRPGCPGMTLPLQSTGRRLVMWHVTSSSAGTSQ
FT KL (in isoform PLD1C)"
FT /evidence="ECO:0000303|PubMed:9761774"
FT /id="VSP_005018"
FT VAR_SEQ 585..623
FT /note="SYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHAD -> N (in
FT isoform PLD1B)"
FT /evidence="ECO:0000303|PubMed:9013646,
FT ECO:0000303|PubMed:9761774"
FT /id="VSP_005020"
FT VAR_SEQ 598..1074
FT /note="Missing (in isoform PLD1C)"
FT /evidence="ECO:0000303|PubMed:9761774"
FT /id="VSP_005019"
FT VAR_SEQ 962..971
FT /note="VVLGYLDDPS -> SKMTPGVEDP (in isoform PLD1D)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005021"
FT VAR_SEQ 972..1074
FT /note="Missing (in isoform PLD1D)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005022"
FT VARIANT 49
FT /note="P -> A (in dbSNP:rs9819927)"
FT /id="VAR_034387"
FT VARIANT 442
FT /note="H -> P (in CVDP1; dbSNP:rs769669104)"
FT /evidence="ECO:0000269|PubMed:27799408"
FT /id="VAR_078985"
FT VARIANT 622
FT /note="A -> S (in dbSNP:rs2290480)"
FT /id="VAR_022056"
FT VARIANT 820
FT /note="V -> M (in dbSNP:rs2287579)"
FT /id="VAR_022057"
FT VARIANT 1024
FT /note="V -> I (in dbSNP:rs9827333)"
FT /id="VAR_051703"
FT CONFLICT 832
FT /note="S -> P (in Ref. 3; CAB76564)"
FT /evidence="ECO:0000305"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 347..357
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:6U8Z"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:6U8Z"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:6U8Z"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 681..686
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 688..707
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 738..748
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 750..753
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 761..772
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 797..810
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 816..820
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 836..850
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 857..865
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 866..871
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 873..884
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 887..892
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 898..902
FT /evidence="ECO:0007829|PDB:6U8Z"
FT TURN 903..905
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 906..911
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 916..919
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 920..932
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 934..941
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 944..949
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 950..964
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 972..974
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 980..985
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 987..1002
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 1013..1021
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 1030..1037
FT /evidence="ECO:0007829|PDB:6U8Z"
FT STRAND 1042..1046
FT /evidence="ECO:0007829|PDB:6U8Z"
FT TURN 1049..1052
FT /evidence="ECO:0007829|PDB:6U8Z"
FT HELIX 1070..1072
FT /evidence="ECO:0007829|PDB:6U8Z"
SQ SEQUENCE 1074 AA; 124184 MW; 734F285790A0BF7A CRC64;
MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF
KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR
KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG
YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS
IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL
PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE
NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ
AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARGLRLQCF
RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT
//
