PLCD1_HUMAN
ID PLCD1_HUMAN Reviewed; 756 AA.
AC P51178; B3KR14; Q86VN8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:7890667, ECO:0000269|PubMed:9188725};
DE AltName: Full=Phosphoinositide phospholipase C-delta-1;
DE AltName: Full=Phospholipase C-III;
DE Short=PLC-III;
DE AltName: Full=Phospholipase C-delta-1;
DE Short=PLC-delta-1;
GN Name=PLCD1 {ECO:0000312|HGNC:HGNC:9060};
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 1), CATALYTIC ACTIVITY, MUTAGENESIS OF
RP GLU-327; ARG-338; GLU-341; HIS-356; SER-381; SER-388; LYS-434; LYS-440;
RP LYS-441 AND ARG-549, AND TISSUE SPECIFICITY.
RC TISSUE=Aorta;
RX PubMed=7890667; DOI=10.1074/jbc.270.10.5495;
RA Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W.,
RA King K.;
RT "Cloning and identification of amino acid residues of human phospholipase C
RT delta 1 essential for catalysis.";
RL J. Biol. Chem. 270:5495-5505(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9188725; DOI=10.1021/bi9702288;
RA Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A.,
RA Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.;
RT "Phosphoinositide binding specificity among phospholipase C isozymes as
RT determined by photo-cross-linking to novel substrate and product analogs.";
RL Biochemistry 36:7239-7248(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP 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 [9]
RP VARIANTS NDNC3 ARG-209 AND THR-574.
RX PubMed=21665001; DOI=10.1016/j.ajhg.2011.05.014;
RA Kiuru M., Kurban M., Itoh M., Petukhova L., Shimomura Y., Wajid M.,
RA Christiano A.M.;
RT "Hereditary leukonychia, or porcelain nails, resulting from mutations in
RT PLCD1.";
RL Am. J. Hum. Genet. 88:839-844(2011).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes
CC (PubMed:9188725). Essential for trophoblast and placental development
CC (By similarity). Binds phosphatidylinositol 4,5-bisphosphate
CC (PubMed:7890667, PubMed:9188725). {ECO:0000250|UniProtKB:Q8R3B1,
CC ECO:0000269|PubMed:7890667, ECO:0000269|PubMed:9188725}.
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:7890667, ECO:0000269|PubMed:9188725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000269|PubMed:7890667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000269|PubMed:7890667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000269|PubMed:7890667};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7890667};
CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain. {ECO:0000305|PubMed:7890667};
CC -!- SUBUNIT: Interacts with TGM2. {ECO:0000250|UniProtKB:P10688}.
CC -!- INTERACTION:
CC P51178; O14964: HGS; NbExp=3; IntAct=EBI-4405387, EBI-740220;
CC P51178; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-4405387, EBI-741158;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51178-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51178-2; Sequence=VSP_042919;
CC -!- TISSUE SPECIFICITY: Strongly expressed in lung, liver and heart. Also
CC expressed at least in pancreas, kidney, skeletal muscle, placenta and
CC brain. {ECO:0000269|PubMed:7890667}.
CC -!- DISEASE: Nail disorder, non-syndromic congenital, 3 (NDNC3)
CC [MIM:151600]: A nail disorder characterized by a white appearance of
CC the nail plate (true leukonychia), the nail bed (pseudoleukonychia), or
CC neither (apparent leukonychia). Leukonychia may involve all of the nail
CC (leukonychia totalis) or only part of the nail (leukonychia partialis),
CC or can appear as one or more transverse bands (leukonychia striata) or
CC white spots (leukonychia punctata). {ECO:0000269|PubMed:21665001}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLCD1ID43927ch3p22.html";
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DR EMBL; U09117; AAA73567.1; -; mRNA.
DR EMBL; AK090774; BAG52226.1; -; mRNA.
DR EMBL; AC144536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64507.1; -; Genomic_DNA.
DR EMBL; BC050382; AAH50382.2; -; mRNA.
DR CCDS; CCDS2671.1; -. [P51178-1]
DR CCDS; CCDS46793.1; -. [P51178-2]
DR PIR; A55943; A55943.
DR RefSeq; NP_001124436.1; NM_001130964.1. [P51178-2]
DR RefSeq; NP_006216.2; NM_006225.3. [P51178-1]
DR AlphaFoldDB; P51178; -.
DR SMR; P51178; -.
DR BioGRID; 111349; 79.
DR IntAct; P51178; 14.
DR MINT; P51178; -.
DR STRING; 9606.ENSP00000430344; -.
DR BindingDB; P51178; -.
DR ChEMBL; CHEMBL3727; -.
DR DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate.
DR DrugBank; DB03956; Inositol 2,4,5-trisphosphate.
DR SwissLipids; SLP:000001065; -.
DR GlyGen; P51178; 2 sites.
DR iPTMnet; P51178; -.
DR PhosphoSitePlus; P51178; -.
DR SwissPalm; P51178; -.
DR BioMuta; PLCD1; -.
DR DMDM; 206729887; -.
DR REPRODUCTION-2DPAGE; IPI00746030; -.
DR EPD; P51178; -.
DR jPOST; P51178; -.
DR MassIVE; P51178; -.
DR MaxQB; P51178; -.
DR PaxDb; P51178; -.
DR PeptideAtlas; P51178; -.
DR PRIDE; P51178; -.
DR ProteomicsDB; 56300; -. [P51178-1]
DR ProteomicsDB; 56301; -. [P51178-2]
DR Antibodypedia; 4086; 181 antibodies from 27 providers.
DR DNASU; 5333; -.
DR Ensembl; ENST00000334661.5; ENSP00000335600.4; ENSG00000187091.14. [P51178-1]
DR Ensembl; ENST00000463876.5; ENSP00000430344.1; ENSG00000187091.14. [P51178-2]
DR GeneID; 5333; -.
DR KEGG; hsa:5333; -.
DR MANE-Select; ENST00000334661.5; ENSP00000335600.4; NM_006225.4; NP_006216.2.
DR UCSC; uc003chm.4; human. [P51178-1]
DR CTD; 5333; -.
DR DisGeNET; 5333; -.
DR GeneCards; PLCD1; -.
DR HGNC; HGNC:9060; PLCD1.
DR HPA; ENSG00000187091; Low tissue specificity.
DR MalaCards; PLCD1; -.
DR MIM; 151600; phenotype.
DR MIM; 602142; gene.
DR neXtProt; NX_P51178; -.
DR OpenTargets; ENSG00000187091; -.
DR Orphanet; 2387; Leukonychia totalis.
DR PharmGKB; PA33388; -.
DR VEuPathDB; HostDB:ENSG00000187091; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158392; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; P51178; -.
DR OMA; VRWTVWN; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; P51178; -.
DR TreeFam; TF313216; -.
DR BioCyc; MetaCyc:HS07195-MON; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; P51178; -.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SignaLink; P51178; -.
DR BioGRID-ORCS; 5333; 10 hits in 1080 CRISPR screens.
DR GeneWiki; PLCD1; -.
DR GenomeRNAi; 5333; -.
DR Pharos; P51178; Tchem.
DR PRO; PR:P51178; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P51178; protein.
DR Bgee; ENSG00000187091; Expressed in olfactory bulb and 189 other tissues.
DR ExpressionAtlas; P51178; baseline and differential.
DR Genevisible; P51178; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:BHF-UCL.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028391; PLC-delta1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
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:SF80; PTHR10336:SF80; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 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; SM00054; EFh; 2.
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; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disease variant; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..756
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-1"
FT /id="PRO_0000088504"
FT DOMAIN 21..130
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 140..175
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 296..440
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 492..609
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 611..737
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 30..57
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 677
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3B1"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 191
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 193
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..11
FT /note="MDSGRDFLTLH -> MQCLGIRSRSRSRELYLQERSLKVAALNGRRL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042919"
FT VARIANT 209
FT /note="T -> R (in NDNC3)"
FT /evidence="ECO:0000269|PubMed:21665001"
FT /id="VAR_066399"
FT VARIANT 257
FT /note="R -> H (in dbSNP:rs933135)"
FT /id="VAR_046560"
FT VARIANT 574
FT /note="I -> T (in NDNC3)"
FT /evidence="ECO:0000269|PubMed:21665001"
FT /id="VAR_066400"
FT MUTAGEN 327
FT /note="E->G: No effect on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 338
FT /note="R->L: Abolishes hydrolysis inositol phospholipids.
FT No effect on binding to phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 341
FT /note="E->G: Abolishes hydrolysis inositol phospholipids.
FT No effect on binding to phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 356
FT /note="H->L: Abolishes hydrolysis inositol phospholipids.
FT No effect on binding to phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 381
FT /note="S->A: Decreases hydrolysis inositol phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 388
FT /note="S->A: No effect on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 434
FT /note="K->Q: Decreases on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 440
FT /note="K->Q: No effect on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 441
FT /note="K->Q: Decreases on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT MUTAGEN 549
FT /note="R->G: Decreases on hydrolysis inositol
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:7890667"
FT CONFLICT 224
FT /note="S -> P (in Ref. 1; AAA73567)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> T (in Ref. 1; AAA73567)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="G -> D (in Ref. 1; AAA73567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 85665 MW; 6C6FD7F89BA08C83 CRC64;
MDSGRDFLTL HGLQDDEDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR
TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPEDRCFSIV FKDQRNTLDL IAPSPADAQH
WVLGLHKIIH HSGSMDQRQK LQHWIHSCLR KADKNKDNKM SFKELQNFLK ELNIQVDDSY
ARKIFRECDH SQTDSLEDEE IEAFYKMLTQ RVEIDRTFAE AAGSGETLSV DQLVTFLQHQ
QREEAAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFSLA HRRVYQDMGQ
PLSHYLVSSS HNTYLLEDQL AGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCTLEQQRV MARHLHAILG PMLLNRPLDG
VTNSLPSPEQ LKGKILLKGK KLGGLLPPGG EGGPEATVVS DEDEAAEMED EAVRSRVQHK
PKEDKLRLAQ ELSDMVIYCK SVHFGGFSSP GTPGQAFYEM ASFSENRALR LLQESGNGFV
RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYQ GRFQDNGACG
YVLKPAFLRD PNGTFNPRAL AQGPWWARKR LNIRVISGQQ LPKVNKNKNS IVDPKVTVEI
HGVSRDVASR QTAVITNNGF NPWWDTEFAF EVVVPDLALI RFLVEDYDAS SKNDFIGQST
IPLNSLKQGY RHVHLMSKNG DQHPSATLFV KISLQD
