PLCD1_MOUSE
ID PLCD1_MOUSE Reviewed; 756 AA.
AC Q8R3B1; Q9Z1B4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1;
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:P51178};
DE AltName: Full=Phosphoinositide phospholipase C-delta-1;
DE AltName: Full=Phospholipase C-delta-1;
DE Short=PLC-delta-1;
GN Name=Plcd1 {ECO:0000312|MGI:MGI:97614}; 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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10425196; DOI=10.1006/bbrc.1999.1035;
RA Lee W.K., Kim J.K., Seo M.S., Cha J.H., Lee K.J., Rha H.K., Min D.S.,
RA Jo Y.H., Lee K.H.;
RT "Molecular cloning and expression analysis of a mouse phospholipase C-
RT delta1.";
RL Biochem. Biophys. Res. Commun. 261:393-399(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RA Wu K., Bai J., Marks D.L., Pagano R.E.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-457 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
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 Essential for trophoblast and placental development. Binds
CC phosphatidylinositol 4,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:P51178, ECO:0000269|PubMed:16314520}.
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:P51178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:P51178};
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:P51178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:P51178};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P51178};
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:P51178};
CC -!- SUBUNIT: Interacts with TGM2. {ECO:0000250|UniProtKB:P10688}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, epididymis
CC and testis. Detected at lower levels in kidney and skeletal muscle.
CC {ECO:0000269|PubMed:10425196}.
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 ---------------------------------------------------------------------------
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; AF133125; AAD32616.1; -; mRNA.
DR EMBL; U85711; AAD00570.1; -; mRNA.
DR EMBL; AK028749; BAC26096.1; -; mRNA.
DR EMBL; AK082890; BAC38671.1; -; mRNA.
DR EMBL; CH466587; EDL09242.1; -; Genomic_DNA.
DR EMBL; BC025798; AAH25798.1; -; mRNA.
DR CCDS; CCDS23607.1; -.
DR RefSeq; NP_001280577.1; NM_001293648.1.
DR RefSeq; NP_062650.1; NM_019676.3.
DR AlphaFoldDB; Q8R3B1; -.
DR SMR; Q8R3B1; -.
DR BioGRID; 202236; 2.
DR STRING; 10090.ENSMUSP00000010804; -.
DR GlyGen; Q8R3B1; 2 sites.
DR iPTMnet; Q8R3B1; -.
DR PhosphoSitePlus; Q8R3B1; -.
DR EPD; Q8R3B1; -.
DR jPOST; Q8R3B1; -.
DR MaxQB; Q8R3B1; -.
DR PaxDb; Q8R3B1; -.
DR PeptideAtlas; Q8R3B1; -.
DR PRIDE; Q8R3B1; -.
DR ProteomicsDB; 289923; -.
DR Antibodypedia; 4086; 181 antibodies from 27 providers.
DR DNASU; 18799; -.
DR Ensembl; ENSMUST00000010804; ENSMUSP00000010804; ENSMUSG00000010660.
DR GeneID; 18799; -.
DR KEGG; mmu:18799; -.
DR UCSC; uc009saf.2; mouse.
DR CTD; 5333; -.
DR MGI; MGI:97614; Plcd1.
DR VEuPathDB; HostDB:ENSMUSG00000010660; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158392; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; Q8R3B1; -.
DR OMA; VRWTVWN; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q8R3B1; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 3474.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR BioGRID-ORCS; 18799; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8R3B1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R3B1; protein.
DR Bgee; ENSMUSG00000010660; Expressed in esophagus and 249 other tissues.
DR ExpressionAtlas; Q8R3B1; baseline and differential.
DR Genevisible; Q8R3B1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO: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:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1900274; P:regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
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; PF16457; PH_12; 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; 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 Calcium; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..756
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-1"
FT /id="PRO_0000088505"
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 609..737
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 30..57
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 CONFLICT 212
FT /note="A -> V (in Ref. 5; AAH25798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 85873 MW; 71F17810F9B0B938 CRC64;
MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR
SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADVQH
WVQGLRKIID RSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKEVKDFLK ELNVQVDDSY
ARKIFRECDH SQTDSLEDEE IETFYRMLTQ RAEIDRAFAE AAGSAETLSV EKLVTFLQHQ
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMNQ
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MAHHLRAILG PMLLDQPLDG
VTTSLPSPEQ LKEKILLKGK KLGGLLPAGG ENGPEATDVS DEDEAAEMED EAVRSQVQHK
PKEDKLKLVP ELSDMVIYCK SVHFGGFSSP STSGQAFYEM ASFSESRALR LLQESGNSFV
RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG
YVLKPAFLRD PDTTFNSRAL TQGPWWAPKK LRVWIISGQQ LPKVNKNKNS IVDPKVIVEI
HGVGQDVASR QTAVITNNGF NPRWDTEFEF VVAVPDLALV RFMVEDYDSS SKNDFIGQST
IPWNSLKQGY RHVHLLSKNG DLHPSATLFV KISIQD
