ID PLCD3_MOUSE Reviewed; 785 AA. AC Q8K2J0; A2AHR0; A2AHR1; Q3UME8; Q69Z55; Q8BL19; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 24-JAN-2024, entry version 166. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000269|PubMed:21187285}; DE AltName: Full=Phosphoinositide phospholipase C-delta-3; DE AltName: Full=Phospholipase C-delta-3; DE Short=PLC-delta-3; GN Name=Plcd3 {ECO:0000312|MGI:MGI:107451}; Synonyms=Kiaa1964; 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 [LARGE SCALE MRNA]. RC TISSUE=Embryonic intestine; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16314520; DOI=10.1128/mcb.25.24.10979-10988.2005; RA Nakamura Y., Hamada Y., Fujiwara T., Enomoto H., Hiroe T., Tanaka S., RA Nose M., Nakahara M., Yoshida N., Takenawa T., Fukami K.; RT "Phospholipase C-delta1 and -delta3 are essential in the trophoblast for RT placental development."; RL Mol. Cell. Biol. 25:10979-10988(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-393, RP AND DEVELOPMENTAL STAGE. RX PubMed=21187285; DOI=10.1074/jbc.m110.171223; RA Kouchi Z., Igarashi T., Shibayama N., Inanobe S., Sakurai K., Yamaguchi H., RA Fukuda T., Yanagi S., Nakamura Y., Fukami K.; RT "Phospholipase Cdelta3 regulates RhoA/Rho kinase signaling and neurite RT outgrowth."; RL J. Biol. Chem. 286:8459-8471(2011). CC -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) CC to generate 2 second messenger molecules diacylglycerol (DAG) and CC inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of CC protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular CC stores. Essential for trophoblast and placental development. May CC participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow. CC Regulates neurite outgrowth through the inhibition of RhoA/Rho kinase CC signaling (PubMed:21187285). {ECO:0000269|PubMed:16314520, CC ECO:0000269|PubMed:21187285}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2- CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, CC ChEBI:CHEBI:203600; EC=3.1.4.11; CC Evidence={ECO:0000269|PubMed:21187285}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000269|PubMed:21187285}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound CC to the C2 domain. {ECO:0000250|UniProtKB:Q8N3E9}; CC -!- ACTIVITY REGULATION: Strongly activated by phosphatidic acid. Inhibited CC by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), CC sphingomyelin and phosphatidylserine (PtdSer) (By similarity). CC {ECO:0000250|UniProtKB:Q8N3E9}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N3E9}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3E9}. Cytoplasm CC {ECO:0000250|UniProtKB:Q8N3E9}. Cleavage furrow CC {ECO:0000250|UniProtKB:Q8N3E9}. Note=Localizes at the cleavage furrow CC during cytokinesis. {ECO:0000250|UniProtKB:Q8N3E9}. CC -!- TISSUE SPECIFICITY: Expressed in cerebellum and cerebral cortex. CC {ECO:0000269|PubMed:21187285}. CC -!- DEVELOPMENTAL STAGE: Expression increases during embryonic or postnatal CC brain development from cerebral cortex at 14 dpc to P7 stage. CC {ECO:0000269|PubMed:21187285}. CC -!- DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting module. CC {ECO:0000250|UniProtKB:Q8N3E9}. CC -!- DOMAIN: The PH domain mediates interaction with the surface membrane by CC binding to PIP2. {ECO:0000250|UniProtKB:Q8N3E9}. CC -!- DISRUPTION PHENOTYPE: Mice lacking Plcd1 and Plcd3 die between 11.5 and CC 13.5 dpc. They exhibit severe disruption of the normal labyrinth CC architecture in the placenta and decreased placental vascularization, CC as well as abnormal proliferation and apoptosis of trophoblasts in the CC labyrinth area. Furthermore, Plcd1 and Plcd3 double knockout embryos CC supplied with a normal placenta by the tetraploid aggregation method CC survive beyond 14.5 dpc, indicating that the embryonic lethality is CC caused by a defect in trophoblasts. {ECO:0000269|PubMed:16314520}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC32829.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD32589.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=CAM22088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AK173311; BAD32589.1; ALT_SEQ; Transcribed_RNA. DR EMBL; AK046669; BAC32829.1; ALT_INIT; mRNA. DR EMBL; AK144950; BAE26150.1; -; mRNA. DR EMBL; AL731805; CAM22088.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL731805; CAM22089.1; -; Genomic_DNA. DR EMBL; BC031392; AAH31392.1; -; mRNA. DR CCDS; CCDS25512.1; -. DR RefSeq; NP_690026.2; NM_152813.3. DR AlphaFoldDB; Q8K2J0; -. DR SMR; Q8K2J0; -. DR BioGRID; 215387; 3. DR STRING; 10090.ENSMUSP00000099366; -. DR ChEMBL; CHEMBL4879495; -. DR SwissLipids; SLP:000001068; -. DR iPTMnet; Q8K2J0; -. DR PhosphoSitePlus; Q8K2J0; -. DR jPOST; Q8K2J0; -. DR MaxQB; Q8K2J0; -. DR PaxDb; 10090-ENSMUSP00000099366; -. DR PeptideAtlas; Q8K2J0; -. DR ProteomicsDB; 289529; -. DR Pumba; Q8K2J0; -. DR Antibodypedia; 8300; 107 antibodies from 24 providers. DR DNASU; 72469; -. DR Ensembl; ENSMUST00000103077.2; ENSMUSP00000099366.2; ENSMUSG00000020937.15. DR GeneID; 72469; -. DR KEGG; mmu:72469; -. DR UCSC; uc007ltf.2; mouse. DR AGR; MGI:107451; -. DR CTD; 113026; -. DR MGI; MGI:107451; Plcd3. DR VEuPathDB; HostDB:ENSMUSG00000020937; -. DR eggNOG; KOG0169; Eukaryota. DR GeneTree; ENSGT00940000156993; -. DR HOGENOM; CLU_002738_0_2_1; -. DR InParanoid; Q8K2J0; -. DR OMA; LAVYCHA; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q8K2J0; -. DR TreeFam; TF313216; -. DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol. DR BioGRID-ORCS; 72469; 2 hits in 79 CRISPR screens. DR ChiTaRS; Plcd3; mouse. DR PRO; PR:Q8K2J0; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q8K2J0; Protein. DR Bgee; ENSMUSG00000020937; Expressed in retinal neural layer and 208 other cell types or tissues. DR ExpressionAtlas; Q8K2J0; baseline and differential. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC. DR GO; GO:0001525; P:angiogenesis; IGI:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IGI:MGI. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd16218; EFh_PI-PLCdelta3; 1. DR CDD; cd13363; PH_PLC_delta; 1. DR CDD; cd08630; PI-PLCc_delta3; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR001192; PI-PLC_fam. DR InterPro; IPR039504; PLC-delta3_EF-hand. DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y. DR PANTHER; PTHR10336:SF33; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-3; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF14788; EF-hand_10; 1. DR Pfam; PF00388; PI-PLC-X; 1. DR Pfam; PF00387; PI-PLC-Y; 1. DR PRINTS; PR00390; PHPHLIPASEC. DR SMART; SM00239; C2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00148; PLCXc; 1. DR SMART; SM00149; PLCYc; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. DR Genevisible; Q8K2J0; MM. PE 1: Evidence at protein level; KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; KW Transducer. FT CHAIN 1..785 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase delta-3" FT /id="PRO_0000306822" FT DOMAIN 65..168 FT /note="PH" FT DOMAIN 178..213 FT /note="EF-hand 1" FT DOMAIN 214..249 FT /note="EF-hand 2" FT DOMAIN 246..281 FT /note="EF-hand 3" FT DOMAIN 333..478 FT /note="PI-PLC X-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT DOMAIN 524..640 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271" FT DOMAIN 636..765 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 69..97 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT REGION 484..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..508 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 348 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT ACT_SITE 393 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT BINDING 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 195 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 202 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 227 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 229 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 231 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 233 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 238 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 349 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 378 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 380 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 427 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 476 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 478 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 553 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 580 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 679 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 681 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 705 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 734 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250" FT BINDING 735 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250" FT BINDING 736 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8N3E9" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8N3E9" FT MUTAGEN 393 FT /note="H->A: Loss of phosphatidylinositol 4,5-bisphosphate FT hydrolyzing activity. In neurons, generates supernumerary FT protrusions." FT /evidence="ECO:0000269|PubMed:21187285" FT CONFLICT 199 FT /note="S -> N (in Ref. 2; BAE26150)" FT /evidence="ECO:0000305" FT CONFLICT 301..302 FT /note="AK -> GE (in Ref. 1; BAD32589)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="E -> K (in Ref. 2; BAE26150)" FT /evidence="ECO:0000305" FT CONFLICT 540 FT /note="D -> E (in Ref. 4; AAH31392)" FT /evidence="ECO:0000305" FT CONFLICT 659 FT /note="A -> T (in Ref. 2; BAE26150)" FT /evidence="ECO:0000305" FT CONFLICT 660 FT /note="I -> V (in Ref. 2; BAE26150)" FT /evidence="ECO:0000305" SQ SEQUENCE 785 AA; 88607 MW; 8B3DE84FB7A52238 CRC64; MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM GLTEDEDVQA MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA SKHIFFVQHI EAVREGHQSE GLRRFGGAFA PACCLTIAFK GRRKNLDLAA PTAEEAQRWV RGLAKLRARL DAMSQRERLD HWIHSYLHRA DSDQDSKMSF KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE AFLRRLLKRP ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT YLTDSQIGGT SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK ILFRDVIQAV RDHAFTSSPY PVILSLENHC GLEQQAVMAR HLRSILGDML VTQALDSQNP EELPSPEQLK GRILVKGKKL PAARSEDGRI LSDREEEEEE EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD PSPGPPQSCT VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC PGPPRTTLAI QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET DYVLNNGFNP CWEQTLQFRL RAPELVLVRF VVEDYDTTSP NDFVGQSTLP LSSLKQGYRH IHLLSKDGAS LAPATLFVHI RIQNS //