PLCD4_MOUSE
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 03-AUG-2022, entry version 155.
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; 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}.
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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; Q8K3R3; -.
DR PRIDE; Q8K3R3; -.
DR ProteomicsDB; 289673; -. [Q8K3R3-1]
DR ProteomicsDB; 289674; -. [Q8K3R3-2]
DR ProteomicsDB; 289675; -. [Q8K3R3-3]
DR ProteomicsDB; 289676; -. [Q8K3R3-4]
DR Antibodypedia; 4087; 118 antibodies from 21 providers.
DR DNASU; 18802; -.
DR Ensembl; ENSMUST00000027362; ENSMUSP00000027362; ENSMUSG00000026173. [Q8K3R3-1]
DR Ensembl; ENSMUST00000067916; ENSMUSP00000064413; ENSMUSG00000026173. [Q8K3R3-2]
DR Ensembl; ENSMUST00000113747; ENSMUSP00000109376; ENSMUSG00000026173. [Q8K3R3-2]
DR Ensembl; ENSMUST00000113749; ENSMUSP00000109378; ENSMUSG00000026173. [Q8K3R3-1]
DR Ensembl; ENSMUST00000113750; ENSMUSP00000109379; ENSMUSG00000026173. [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 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; 368239at2759; -.
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 74 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 120 other tissues.
DR ExpressionAtlas; Q8K3R3; baseline and differential.
DR Genevisible; Q8K3R3; MM.
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:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028387; PLC-delta4.
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:SF31; PTHR10336:SF31; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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.
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
