PLCD3_MOUSE
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 03-AUG-2022, entry version 158.
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;
CC Evidence={ECO:0000255|PROSITE-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};
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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 SwissLipids; SLP:000001068; -.
DR iPTMnet; Q8K2J0; -.
DR PhosphoSitePlus; Q8K2J0; -.
DR jPOST; Q8K2J0; -.
DR MaxQB; Q8K2J0; -.
DR PaxDb; Q8K2J0; -.
DR PeptideAtlas; Q8K2J0; -.
DR PRIDE; Q8K2J0; -.
DR ProteomicsDB; 289529; -.
DR Antibodypedia; 8300; 93 antibodies from 24 providers.
DR DNASU; 72469; -.
DR Ensembl; ENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
DR GeneID; 72469; -.
DR KEGG; mmu:72469; -.
DR UCSC; uc007ltf.2; mouse.
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; HTWIHSY; -.
DR OrthoDB; 368239at2759; -.
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 74 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 205 other tissues.
DR ExpressionAtlas; Q8K2J0; baseline and differential.
DR Genevisible; Q8K2J0; MM.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
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:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR CDD; cd16218; EFh_PI-PLCdelta3; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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; IPR028406; PLC-delta3.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF33; PTHR10336:SF33; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
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
