PLCD3_HUMAN
ID PLCD3_HUMAN Reviewed; 789 AA.
AC Q8N3E9; Q8TEC1; Q8TF37; Q96FL6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:10336610};
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|HGNC:HGNC:9061}; Synonyms=KIAA1964;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-789.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-789.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [5]
RP PURIFICATION.
RX PubMed=9360711;
RA Pawelczyk T., Matecki A.;
RT "Expression, purification and kinetic properties of human recombinant
RT phospholipase C delta 3.";
RL Acta Biochim. Pol. 44:221-229(1997).
RN [6]
RP PURIFICATION.
RX PubMed=9056492; DOI=10.1006/prep.1996.0682;
RA Ghosh S., Pawelczyk T., Lowenstein J.M.;
RT "Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-
RT yield expression in Escherichia coli, simple purification, and
RT properties.";
RL Protein Expr. Purif. 9:262-278(1997).
RN [7]
RP SUBCELLULAR LOCATION, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=9799116; DOI=10.1046/j.1432-1327.1998.2570169.x;
RA Pawelczyk T., Matecki A.;
RT "Localization of phospholipase C delta3 in the cell and regulation of its
RT activity by phospholipids and calcium.";
RL Eur. J. Biochem. 257:169-177(1998).
RN [8]
RP IDENTIFICATION.
RX PubMed=10702670; DOI=10.1159/000015469;
RA Kim H., Suh P.-G., Ryu S.H., Park S.H.;
RT "Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band
RT 17q21 by fluorescence in situ hybridization.";
RL Cytogenet. Cell Genet. 87:209-210(1999).
RN [9]
RP ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DOMAIN
RP PH, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10336610; DOI=10.1046/j.1432-1327.1999.00388.x;
RA Pawelczyk T., Matecki A.;
RT "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol
RT 4,5-bisphosphate and phosphatidic acid in bilayer membranes.";
RL Eur. J. Biochem. 262:291-298(1999).
RN [10]
RP INDUCTION.
RX PubMed=11500033; DOI=10.1006/bbrc.2001.5371;
RA Lin F.-G., Cheng H.-F., Lee I.-F., Kao H.-J., Loh S.-H., Lee W.-H.;
RT "Downregulation of phospholipase C delta3 by cAMP and calcium.";
RL Biochem. Biophys. Res. Commun. 286:274-280(2001).
RN [11]
RP DOMAIN C2.
RX PubMed=11706040; DOI=10.1074/jbc.m109705200;
RA Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.;
RT "Membrane targeting of C2 domains of phospholipase C-delta isoforms.";
RL J. Biol. Chem. 277:3568-3575(2002).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=15505048; DOI=10.1167/iovs.04-0084;
RA Landreville S., Coulombe S., Carrier P., Gelb M.H., Guerin S.L.,
RA Salesse C.;
RT "Expression of phospholipases A2 and C in human corneal epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 45:3997-4003(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=17041247; DOI=10.1093/jb/mvj209;
RA Naito Y., Okada M., Yagisawa H.;
RT "Phospholipase C isoforms are localized at the cleavage furrow during
RT cytokinesis.";
RL J. Biochem. 140:785-791(2006).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-496 AND SER-573, 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).
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 (PubMed:10336610). Regulates neurite outgrowth through the inhibition
CC of RhoA/Rho kinase signaling (By similarity).
CC {ECO:0000250|UniProtKB:Q8K2J0, ECO:0000269|PubMed:10336610}.
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:10336610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:10336610};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000305|PubMed:9799116};
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:9799116};
CC -!- ACTIVITY REGULATION: Strongly activated by phosphatidic acid. Inhibited
CC by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho),
CC sphingomyelin and phosphatidylserine (PtdSer).
CC {ECO:0000269|PubMed:10336610, ECO:0000269|PubMed:9799116}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=105.3 uM for PIP2 {ECO:0000269|PubMed:10336610};
CC Vmax=28.5 umol/min/mg enzyme {ECO:0000269|PubMed:10336610};
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm.
CC Cleavage furrow {ECO:0000269|PubMed:17041247}. Note=Localizes at the
CC cleavage furrow during cytokinesis. {ECO:0000269|PubMed:17041247}.
CC -!- TISSUE SPECIFICITY: Present in corneal epithelial cells (at protein
CC level). {ECO:0000269|PubMed:15505048}.
CC -!- INDUCTION: Down-regulated by Ca(2+) and cAMP.
CC {ECO:0000269|PubMed:11500033}.
CC -!- DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting module.
CC {ECO:0000269|PubMed:11706040}.
CC -!- DOMAIN: The PH domain mediates interaction with the surface membrane by
CC binding to PIP2. {ECO:0000269|PubMed:10336610}.
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DR EMBL; AK074240; BAB85029.1; -; mRNA.
DR EMBL; BC010668; AAH10668.2; -; mRNA.
DR EMBL; BC072384; AAH72384.1; -; mRNA.
DR EMBL; AL834392; CAD39054.2; -; mRNA.
DR EMBL; AB075844; BAB85550.1; -; mRNA.
DR CCDS; CCDS74077.1; -.
DR RefSeq; NP_588614.1; NM_133373.4.
DR AlphaFoldDB; Q8N3E9; -.
DR SMR; Q8N3E9; -.
DR BioGRID; 125222; 151.
DR IntAct; Q8N3E9; 18.
DR MINT; Q8N3E9; -.
DR STRING; 9606.ENSP00000479636; -.
DR SwissLipids; SLP:000001067; -.
DR iPTMnet; Q8N3E9; -.
DR PhosphoSitePlus; Q8N3E9; -.
DR SwissPalm; Q8N3E9; -.
DR BioMuta; PLCD3; -.
DR DMDM; 158706388; -.
DR EPD; Q8N3E9; -.
DR jPOST; Q8N3E9; -.
DR MassIVE; Q8N3E9; -.
DR MaxQB; Q8N3E9; -.
DR PaxDb; Q8N3E9; -.
DR PeptideAtlas; Q8N3E9; -.
DR PRIDE; Q8N3E9; -.
DR ProteomicsDB; 71794; -.
DR Antibodypedia; 8300; 93 antibodies from 24 providers.
DR DNASU; 113026; -.
DR Ensembl; ENST00000619929.5; ENSP00000479636.1; ENSG00000161714.12.
DR GeneID; 113026; -.
DR KEGG; hsa:113026; -.
DR MANE-Select; ENST00000619929.5; ENSP00000479636.1; NM_133373.5; NP_588614.1.
DR UCSC; uc032fjs.2; human.
DR CTD; 113026; -.
DR DisGeNET; 113026; -.
DR GeneCards; PLCD3; -.
DR HGNC; HGNC:9061; PLCD3.
DR HPA; ENSG00000161714; Tissue enhanced (skeletal).
DR MIM; 608795; gene.
DR neXtProt; NX_Q8N3E9; -.
DR OpenTargets; ENSG00000161714; -.
DR PharmGKB; PA33389; -.
DR VEuPathDB; HostDB:ENSG00000161714; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000156993; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; Q8N3E9; -.
DR OMA; HTWIHSY; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q8N3E9; -.
DR TreeFam; TF313216; -.
DR PathwayCommons; Q8N3E9; -.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SABIO-RK; Q8N3E9; -.
DR SignaLink; Q8N3E9; -.
DR BioGRID-ORCS; 113026; 9 hits in 269 CRISPR screens.
DR ChiTaRS; PLCD3; human.
DR GeneWiki; PLCD3; -.
DR GenomeRNAi; 113026; -.
DR Pharos; Q8N3E9; Tbio.
DR PRO; PR:Q8N3E9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N3E9; protein.
DR Bgee; ENSG00000161714; Expressed in mucosa of transverse colon and 131 other tissues.
DR ExpressionAtlas; Q8N3E9; baseline and differential.
DR Genevisible; Q8N3E9; HS.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IEA:Ensembl.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
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; IEA:Ensembl.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 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..789
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-3"
FT /id="PRO_0000306821"
FT DOMAIN 63..172
FT /note="PH"
FT DOMAIN 182..217
FT /note="EF-hand 1"
FT DOMAIN 218..253
FT /note="EF-hand 2"
FT DOMAIN 250..285
FT /note="EF-hand 3"
FT DOMAIN 337..482
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 528..644
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 644..769
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 73..101
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT REGION 461..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 557
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 683
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 739
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 652
FT /note="P -> L (in dbSNP:rs734921)"
FT /id="VAR_035316"
FT CONFLICT 207
FT /note="I -> T (in Ref. 3; CAD39054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 89258 MW; C6901404D2C9D070 CRC64;
MLCGRWRRCR RPPEEPPVAA QVAAQVAAPV ALPSPPTPSD GGTKRPGLRA LKKMGLTEDE
DVRAMLRGSR LRKIRSRTWH KERLYRLQED GLSVWFQRRI PRAPSQHIFF VQHIEAVREG
HQSEGLRRFG GAFAPARCLT IAFKGRRKNL DLAAPTAEEA QRWVRGLTKL RARLDAMSQR
ERLDHWIHSY LHRADSNQDS KMSFKEIKSL LRMVNVDMND MYAYLLFKEC DHSNNDRLEG
AEIEEFLRRL LKRPELEEIF HQYSGEDRVL SAPELLEFLE DQGEEGATLA RAQQLIQTYE
LNETAKQHEL MTLDGFMMYL LSPEGAALDN THTCVFQDMN QPLAHYFISS SHNTYLTDSQ
IGGPSSTEAY VRAFAQGCRC VELDCWEGPG GEPVIYHGHT LTSKILFRDV VQAVRDHAFT
LSPYPVILSL ENHCGLEQQA AMARHLCTIL GDMLVTQALD SPNPEELPSP EQLKGRVLVK
GKKLPAARSE DGRALSDREE EEEDDEEEEE EVEAAAQRRL AKQISPELSA LAVYCHATRL
RTLHPAPNAP QPCQVSSLSE RKAKKLIREA GNSFVRHNAR QLTRVYPLGL RMNSANYSPQ
EMWNSGCQLV ALNFQTPGYE MDLNAGRFLV NGQCGYVLKP ACLRQPDSTF DPEYPGPPRT
TLSIQVLTAQ QLPKLNAEKP HSIVDPLVRI EIHGVPADCA RQETDYVLNN GFNPRWGQTL
QFQLRAPELA LVRFVVEDYD ATSPNDFVGQ FTLPLSSLKQ GYRHIHLLSK DGASLSPATL
FIQIRIQRS
