ID PLCD4_MOUSE Reviewed; 807 AA. AC Q8K3R3; Q3USN9; Q6NZF7; Q8CAB1; Q9CUC1; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 24-JAN-2024, entry version 163. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q9BRC7}; DE AltName: Full=Phosphoinositide phospholipase C-delta-4; DE AltName: Full=Phospholipase C-delta-4; DE Short=PLC-delta-4; GN Name=Plcd4 {ECO:0000312|MGI:MGI:107469}; Synonyms=Plcd; 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 [MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Kim J., Kim H., Lee K.-H.; RT "Molecular cloning of PLC delta4."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC STRAIN=C57BL/6J; RC TISSUE=Corpora quadrigemina, Hypothalamus, and Testis; 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 MRNA] (ISOFORM 2). RC STRAIN=CD-1; TISSUE=Neural stem cell; 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 [4] RP INDUCTION. RX PubMed=10601847; DOI=10.1046/j.1432-1327.2000.00943.x; RA Fukami K., Takenaka K., Nagano K., Takenawa T.; RT "Growth factor-induced promoter activation of murine phospholipase C delta4 RT gene."; RL Eur. J. Biochem. 267:28-36(2000). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11340203; DOI=10.1126/science.1059042; RA Fukami K., Nakao K., Inoue T., Kataoka Y., Kurokawa M., Fissore R.A., RA Nakamura K., Katsuki M., Mikoshiba K., Yoshida N., Takenawa T.; RT "Requirement of phospholipase Cdelta4 for the zona pellucida-induced RT acrosome reaction."; RL Science 292:920-923(2001). RN [6] RP FUNCTION. RX PubMed=12695499; DOI=10.1083/jcb.200210057; RA Fukami K., Yoshida M., Inoue T., Kurokawa M., Fissore R.A., Yoshida N., RA Mikoshiba K., Takenawa T.; RT "Phospholipase Cdelta4 is required for Ca2+ mobilization essential for RT acrosome reaction in sperm."; RL J. Cell Biol. 161:79-88(2003). RN [7] RP INTERACTION WITH GRIP1. RX PubMed=16272139; DOI=10.1093/jb/mvi135; RA Irino Y., Ichinohe M., Nakamura Y., Nakahara M., Fukami K.; RT "Phospholipase Cdelta4 associates with glutamate receptor interacting RT protein 1 in testis."; RL J. Biochem. 138:451-456(2005). RN [8] RP FUNCTION. RX PubMed=16998201; DOI=10.1093/jb/mvj194; RA Akutagawa A., Fukami K., Banno Y., Takenawa T., Kannagi R., Yokoyama Y., RA Oda K., Nagino M., Nimura Y., Yoshida S., Tamiya-Koizumi K.; RT "Disruption of phospholipase Cdelta4 gene modulates the liver regeneration RT in cooperation with nuclear protein kinase C."; RL J. Biochem. 140:619-625(2006). 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. Required for acrosome reaction in sperm during fertilization, CC probably by acting as an important enzyme for intracellular Ca(2+) CC mobilization in the zona pellucida-induced acrosome reaction. May play CC a role in cell growth. Modulates the liver regeneration in cooperation CC with nuclear PKC. Overexpression up-regulates the Erk signaling pathway CC and proliferation. {ECO:0000269|PubMed:11340203, CC ECO:0000269|PubMed:12695499, ECO:0000269|PubMed:16998201}. 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:0000250|UniProtKB:Q9BRC7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000250|UniProtKB:Q9BRC7}; 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:0000250|UniProtKB:Q9BRC7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485; CC Evidence={ECO:0000250|UniProtKB:Q9BRC7}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound CC to the C2 domain. {ECO:0000250}; CC -!- SUBUNIT: Interacts with GRIP1 (PubMed:16272139). Interacts (via GBA CC motif) with guanine nucleotide-binding protein G(i) alpha subunit GNAI3 CC (inactive GDP-bound form)l low-affinity interaction (By similarity). CC {ECO:0000250|UniProtKB:Q9BRC7, ECO:0000269|PubMed:16272139}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. CC Endoplasmic reticulum {ECO:0000250}. Note=Localizes primarily to CC intracellular membranes mostly to the endoplasmic reticulum. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8K3R3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8K3R3-2; Sequence=VSP_028503; CC Name=3; CC IsoId=Q8K3R3-3; Sequence=VSP_028503, VSP_028506; CC Name=4; CC IsoId=Q8K3R3-4; Sequence=VSP_028504, VSP_028505; CC -!- INDUCTION: By treatment with growth factors such as bradykinin, CC lysophosphatidic acid, and Ca(2+) ionophore in addition to serum. CC {ECO:0000269|PubMed:10601847}. CC -!- DOMAIN: The PDZ-binding motif mediates the interaction with GRIP1. CC -!- DOMAIN: The C2 domain mediates pre-localization to the membrane prior CC to Ca(2+) import and non-selective Ca(2+)-mediated targeting to various CC cellular membranes. {ECO:0000250}. CC -!- DOMAIN: The PH domain is not a critical determinant of the membrane CC localization. {ECO:0000250}. CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding CC to the alpha subunits of guanine nucleotide-binding proteins (G CC proteins). {ECO:0000250|UniProtKB:Q9BRC7}. CC -!- DISRUPTION PHENOTYPE: Mice are either sterile or produce few small CC litters. In these mice, fewer eggs become activated and the Ca(2+) CC transients associated with fertilization are absent or delayed. Sperm CC are unable to initiate the acrosome reaction. CC {ECO:0000269|PubMed:11340203}. 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; AY033991; AAK61537.1; -; mRNA. DR EMBL; AK016945; BAB30513.1; -; mRNA. DR EMBL; AK039149; BAC30256.1; -; mRNA. DR EMBL; AK140231; BAE24292.1; -; mRNA. DR EMBL; BC066156; AAH66156.1; -; mRNA. DR CCDS; CCDS35616.1; -. [Q8K3R3-1] DR CCDS; CCDS35617.1; -. [Q8K3R3-2] DR RefSeq; NP_001074925.1; NM_001081456.1. [Q8K3R3-2] DR RefSeq; NP_683739.2; NM_148937.2. [Q8K3R3-1] DR RefSeq; XP_006495851.1; XM_006495788.3. [Q8K3R3-1] DR AlphaFoldDB; Q8K3R3; -. DR SMR; Q8K3R3; -. DR STRING; 10090.ENSMUSP00000027362; -. DR iPTMnet; Q8K3R3; -. DR PhosphoSitePlus; Q8K3R3; -. DR jPOST; Q8K3R3; -. DR MaxQB; Q8K3R3; -. DR PaxDb; 10090-ENSMUSP00000027362; -. DR ProteomicsDB; 289673; -. [Q8K3R3-1] DR ProteomicsDB; 289674; -. [Q8K3R3-2] DR ProteomicsDB; 289675; -. [Q8K3R3-3] DR ProteomicsDB; 289676; -. [Q8K3R3-4] DR Antibodypedia; 4087; 129 antibodies from 21 providers. DR DNASU; 18802; -. DR Ensembl; ENSMUST00000027362.14; ENSMUSP00000027362.8; ENSMUSG00000026173.17. [Q8K3R3-1] DR Ensembl; ENSMUST00000067916.13; ENSMUSP00000064413.7; ENSMUSG00000026173.17. [Q8K3R3-2] DR Ensembl; ENSMUST00000113747.8; ENSMUSP00000109376.2; ENSMUSG00000026173.17. [Q8K3R3-2] DR Ensembl; ENSMUST00000113750.8; ENSMUSP00000109379.2; ENSMUSG00000026173.17. [Q8K3R3-3] DR GeneID; 18802; -. DR KEGG; mmu:18802; -. DR UCSC; uc007bmg.1; mouse. [Q8K3R3-2] DR UCSC; uc007bmh.1; mouse. [Q8K3R3-1] DR UCSC; uc007bmi.1; mouse. [Q8K3R3-4] DR UCSC; uc011wnb.1; mouse. [Q8K3R3-3] DR AGR; MGI:107469; -. DR CTD; 84812; -. DR MGI; MGI:107469; Plcd4. DR VEuPathDB; HostDB:ENSMUSG00000026173; -. DR eggNOG; KOG0169; Eukaryota. DR GeneTree; ENSGT00940000156180; -. DR HOGENOM; CLU_002738_0_2_1; -. DR InParanoid; Q8K3R3; -. DR OMA; SSYRRCT; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q8K3R3; -. DR TreeFam; TF313216; -. DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol. DR BioGRID-ORCS; 18802; 2 hits in 79 CRISPR screens. DR ChiTaRS; Plcd4; mouse. DR PRO; PR:Q8K3R3; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q8K3R3; Protein. DR Bgee; ENSMUSG00000026173; Expressed in gastrocnemius medialis and 121 other cell types or tissues. DR ExpressionAtlas; Q8K3R3; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISO:MGI. DR GO; GO:0004629; F:phospholipase C activity; TAS:MGI. DR GO; GO:0007340; P:acrosome reaction; IMP:MGI. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; TAS:MGI. DR GO; GO:0007165; P:signal transduction; TAS:MGI. DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI. DR CDD; cd00275; C2_PLC_like; 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; IPR002048; EF_hand_dom. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR001192; PI-PLC_fam. 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:SF31; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-4; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF09279; EF-hand_like; 1. DR Pfam; PF00169; PH; 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; 3. 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; PS50222; EF_HAND_2; 3. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. DR Genevisible; Q8K3R3; MM. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasm; Endoplasmic reticulum; Hydrolase; KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transducer. FT CHAIN 1..807 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase delta-4" FT /id="PRO_0000306826" FT DOMAIN 16..124 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 134..169 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 170..205 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 203..237 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 290..435 FT /note="PI-PLC X-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT DOMAIN 538..654 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271" FT DOMAIN 654..781 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 26..53 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT REGION 442..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 213..243 FT /note="GBA" FT /evidence="ECO:0000250|UniProtKB:Q9BRC7" FT MOTIF 776..779 FT /note="PDZ-binding" FT COMPBIAS 444..460 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 305 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT ACT_SITE 350 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT BINDING 147 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 149 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 151 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 153 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 158 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 183 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 194 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 306 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 335 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 337 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 433 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 435 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 567 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 594 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 697 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 721 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 750 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250" FT BINDING 751 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250" FT VAR_SEQ 493..524 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_028503" FT VAR_SEQ 494..496 FT /note="MKC -> SQD (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_028504" FT VAR_SEQ 497..807 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_028505" FT VAR_SEQ 773..807 FT /note="GYRHVSLLSRDGTSLNPASIFVYTCMQEDLDMDEP -> EMALASIQLPSLY FT TPACRKTWIWMSPEKHREGLEEQSTDAQSFPTYNFLKIQSQPKDQ (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_028506" FT CONFLICT 180 FT /note="Q -> R (in Ref. 2; BAE24292)" FT /evidence="ECO:0000305" FT CONFLICT 310 FT /note="V -> A (in Ref. 3; AAH66156)" FT /evidence="ECO:0000305" FT CONFLICT 372 FT /note="F -> L (in Ref. 3; AAH66156)" FT /evidence="ECO:0000305" FT CONFLICT 445 FT /note="Missing (in Ref. 2; BAE24292)" FT /evidence="ECO:0000305" FT CONFLICT 470 FT /note="L -> F (in Ref. 1; AAK61537)" FT /evidence="ECO:0000305" FT CONFLICT 594 FT /note="R -> C (in Ref. 3; AAH66156)" FT /evidence="ECO:0000305" FT CONFLICT 653 FT /note="L -> V (in Ref. 1; AAK61537)" FT /evidence="ECO:0000305" SQ SEQUENCE 807 AA; 92694 MW; C109F6255CED45F7 CRC64; MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG SQPESMPKPT FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP NLDLVANSVE EAQIWMRGLQ LLVDLVASMD HQEQMDQMLN EWFQQADRNQ DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ EADVTQSDDL GSEEFVQFYK ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH APDLALELID RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GHTLTSRILF KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT EILGEQLLRN TLEGLLVDSM PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE EEEELEKDEG PDLDPASPEL DTQPQPETQG QAAGNKKERK KKVMKCPMSC LLICGHVMAQ APSSIPESIL LSKQFLLLSS TTIMCPDLSA LVVYLRTVPF CSFTHSKENY HIYDISSFSE SKAKNLIKEA GNEFVQHNAR QLCRVYPSGL RTDSSNFNPQ EHWNVGCQMV AMNMQTAGSA MDICDGLFRQ NGGSGYVLKP EFLRDTQSSF NPERPISLYK AQILVVQVIS GQQLPKVDKT KETTVVDPLV KVELYGVPED TKEQETSHVE NNGINPYWGE TFYFRLQVPE LAMLRFVVKD YSRKSRNNFI GQYTLPWTCM KQGYRHVSLL SRDGTSLNPA SIFVYTCMQE DLDMDEP //