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 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. DR Genevisible; Q13393; HS. 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 //