ID PLCZ1_MOUSE Reviewed; 647 AA. AC Q8K4D7; Q3KPE5; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 158. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1; DE EC=3.1.4.11; DE AltName: Full=Phosphoinositide phospholipase C-zeta-1; DE AltName: Full=Phospholipase C-zeta-1 {ECO:0000250|UniProtKB:Q86YW0}; DE Short=PLC-zeta-1 {ECO:0000250|UniProtKB:Q86YW0}; GN Name=Plcz1 {ECO:0000312|MGI:MGI:2150308}; 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] {ECO:0000305, ECO:0000312|EMBL:AAM95914.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM95914.1}; RC TISSUE=Spermatid {ECO:0000269|PubMed:12117804}; RX PubMed=12117804; DOI=10.1242/dev.129.15.3533; RA Saunders C.M., Larman M.G., Parrington J., Cox L.J., Royse J., RA Blayney L.M., Swann K., Lai F.A.; RT "PLC zeta: a sperm-specific trigger of Ca(2+) oscillations in eggs and RT embryo development."; RL Development 129:3533-3544(2002). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR RP LOCATION. RC TISSUE=Testis {ECO:0000269|PubMed:14701816}; RX PubMed=14701816; DOI=10.1074/jbc.m313801200; RA Kouchi Z., Fukami K., Shikano T., Oda S., Nakamura Y., Takenawa T., RA Miyazaki S.; RT "Recombinant phospholipase Czeta has high Ca2+ sensitivity and induces Ca2+ RT oscillations in mouse eggs."; RL J. Biol. Chem. 279:10408-10412(2004). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis {ECO:0000269|PubMed:16141072}; 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] {ECO:0000305, ECO:0000312|EMBL:AAI06768.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] {ECO:0000305} RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15385165; DOI=10.1016/j.ydbio.2004.07.025; RA Fujimoto S., Yoshida N., Fukui T., Amanai M., Isobe T., Itagaki C., RA Izumi T., Perry A.C.F.; RT "Mammalian phospholipase Czeta induces oocyte activation from the sperm RT perinuclear matrix."; RL Dev. Biol. 274:370-383(2004). RN [6] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-377. RX PubMed=15159452; DOI=10.1242/jcs.01109; RA Larman M.G., Saunders C.M., Carroll J., Lai F.A., Swann K.; RT "Cell cycle-dependent Ca2+ oscillations in mouse embryos are regulated by RT nuclear targeting of PLCzeta."; RL J. Cell Sci. 117:2513-2521(2004). RN [7] {ECO:0000305} RP SUBCELLULAR LOCATION. RX PubMed=15809052; DOI=10.1016/j.bbrc.2005.03.032; RA Sone Y., Ito M., Shirakawa H., Shikano T., Takeuchi H., Kinoshita K., RA Miyazaki S.; RT "Nuclear translocation of phospholipase C-zeta, an egg-activating factor, RT during early embryonic development."; RL Biochem. Biophys. Res. Commun. 330:690-694(2005). RN [8] {ECO:0000305} RP FUNCTION, COFACTOR, INTERACTION WITH PTDINS(3)P AND PTDINS(5)P, AND DOMAIN. RX PubMed=15790568; DOI=10.1074/jbc.m412123200; RA Kouchi Z., Shikano T., Nakamura Y., Shirakawa H., Fukami K., Miyazaki S.; RT "The role of EF-hand domains and C2 domain in regulation of enzymatic RT activity of phospholipase Czeta."; RL J. Biol. Chem. 280:21015-21021(2005). RN [9] {ECO:0000305} RP DOMAIN, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=16000311; DOI=10.1074/jbc.m500629200; RA Nomikos M., Blayney L.M., Larman M.G., Campbell K., Rossbach A., RA Saunders C.M., Swann K., Lai F.A.; RT "Role of phospholipase C-zeta domains in Ca2+-dependent RT phosphatidylinositol 4,5-bisphosphate hydrolysis and cytoplasmic Ca2+ RT oscillations."; RL J. Biol. Chem. 280:31011-31018(2005). RN [10] {ECO:0000305} RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-210; LYS-299; LYS-301; ARG-376; RP LYS-377; ARG-378; LYS-379 AND LYS-381. RX PubMed=16854985; DOI=10.1074/jbc.m603473200; RA Kuroda K., Ito M., Shikano T., Awaji T., Yoda A., Takeuchi H., RA Kinoshita K., Miyazaki S.; RT "The role of X/Y linker region and N-terminal EF-hand domain in nuclear RT translocation and Ca2+ oscillation-inducing activities of phospholipase RT Czeta, a mammalian egg-activating factor."; RL J. Biol. Chem. 281:27794-27805(2006). RN [11] {ECO:0000305} RP FUNCTION, AND OVEREXPRESSION. RX PubMed=17933795; DOI=10.1242/dev.007930; RA Yoshida N., Amanai M., Fukui T., Kajikawa E., Brahmajosyula M., Iwahori A., RA Nakano Y., Shoji S., Diebold J., Hessel H., Huss R., Perry A.C.; RT "Broad, ectopic expression of the sperm protein PLCZ1 induces RT parthenogenesis and ovarian tumours in mice."; RL Development 134:3941-3952(2007). RN [12] {ECO:0000305} RP FUNCTION, AND DOMAIN. RX PubMed=18028898; DOI=10.1016/j.ydbio.2007.09.040; RA Kurokawa M., Yoon S.Y., Alfandari D., Fukami K., Sato K., Fissore R.A.; RT "Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations RT during mammalian fertilization."; RL Dev. Biol. 312:407-418(2007). RN [13] {ECO:0000305} RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18322275; DOI=10.1095/biolreprod.108.067801; RA Ito M., Shikano T., Oda S., Horiguchi T., Tanimoto S., Awaji T., Mitani H., RA Miyazaki S.; RT "Difference in Ca2+ oscillation-inducing activity and nuclear translocation RT ability of PLCZ1, an egg-activating sperm factor candidate, between mouse, RT rat, human, and medaka fish."; RL Biol. Reprod. 78:1081-1090(2008). 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. In CC vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers CC intracellular Ca(2+) oscillations in oocytes solely during M phase and CC is involved in inducing oocyte activation and initiating embryonic CC development up to the blastocyst stage. Is therefore a strong candidate CC for the egg-activating soluble sperm factor that is transferred from CC the sperm into the egg cytoplasm following gamete membrane fusion. May CC exert an inhibitory effect on phospholipase-C-coupled processes that CC depend on calcium ions and protein kinase C, including CFTR trafficking CC and function. {ECO:0000250|UniProtKB:Q86YW0, CC ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, CC ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, CC ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311, CC ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:17933795, CC ECO:0000269|PubMed:18028898, ECO:0000269|PubMed:18322275}. 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:16000311}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000269|PubMed:16000311}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311}; CC -!- SUBUNIT: Interacts via its C2 domain with PtdIns(3)P and, to a lesser CC extent, PtdIns(5)P in vitro. {ECO:0000269|PubMed:15790568}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14701816, CC ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, CC ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, CC perinuclear region {ECO:0000269|PubMed:14701816, CC ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, CC ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. CC Note=Exhibits alternative cytoplasmic/nuclear localization during CC development. Translocates from the pronucleus into cytoplasm upon CC nuclear envelope breakdown for mitosis and localizes again to the CC pronuclei at interphase following meiosis and mitosis. CC {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, CC ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, CC ECO:0000269|PubMed:18322275}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, CC ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072}; CC IsoId=Q8K4D7-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14701816}; CC IsoId=Q8K4D7-2; Sequence=VSP_052863; CC -!- TISSUE SPECIFICITY: Highly expressed in postpuberal testis, where CC expression is sperm cell-specific. Also expressed in brain of both CC sexes. {ECO:0000269|PubMed:12117804}. CC -!- DOMAIN: The EF-hand and C2 domains are essential for triggering Ca(2+) CC oscillating activity and the regulation of PLCZ1 enzyme activity. CC {ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311, CC ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:18028898}. CC -!- DOMAIN: The X-Y linker region between PI-PLC X-box and Y-box domains CC may be a target for proteolysis and may play an important regulatory CC role during fertilization. {ECO:0000269|PubMed:15790568, CC ECO:0000269|PubMed:16000311, ECO:0000269|PubMed:16854985, CC ECO:0000269|PubMed:18028898}. CC -!- MISCELLANEOUS: Transgenic mice, where broad ectopic expression is CC forced, initially appear healthy and their oocytes undergo unperturbed CC meiotic maturation to metaphase II but subsequently exhibit autonomous CC intracellular free calcium oscillations, second polar body extrusion, CC pronucleus formation and parthenogenetic development. Transgenic males CC remained largely asymptomatic, whereas transgenic females develop CC abdominal swellings caused by benign ovarian teratomas. 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; AF435950; AAM95914.1; -; mRNA. DR EMBL; AK006672; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC106767; AAI06768.1; -; mRNA. DR CCDS; CCDS20671.1; -. [Q8K4D7-1] DR RefSeq; NP_473407.2; NM_054066.4. [Q8K4D7-1] DR AlphaFoldDB; Q8K4D7; -. DR SMR; Q8K4D7; -. DR BioGRID; 227896; 1. DR STRING; 10090.ENSMUSP00000032356; -. DR SwissLipids; SLP:000001073; -. DR iPTMnet; Q8K4D7; -. DR PhosphoSitePlus; Q8K4D7; -. DR PaxDb; 10090-ENSMUSP00000032356; -. DR ProteomicsDB; 288231; -. [Q8K4D7-1] DR ProteomicsDB; 288232; -. [Q8K4D7-2] DR Antibodypedia; 52401; 154 antibodies from 18 providers. DR DNASU; 114875; -. DR Ensembl; ENSMUST00000032356.13; ENSMUSP00000032356.7; ENSMUSG00000030230.16. [Q8K4D7-1] DR GeneID; 114875; -. DR KEGG; mmu:114875; -. DR UCSC; uc012evc.2; mouse. [Q8K4D7-1] DR AGR; MGI:2150308; -. DR CTD; 89869; -. DR MGI; MGI:2150308; Plcz1. DR VEuPathDB; HostDB:ENSMUSG00000030230; -. DR eggNOG; KOG0169; Eukaryota. DR GeneTree; ENSGT00940000159950; -. DR HOGENOM; CLU_002738_0_3_1; -. DR InParanoid; Q8K4D7; -. DR OMA; YLTCTLV; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q8K4D7; -. 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; 114875; 0 hits in 78 CRISPR screens. DR PRO; PR:Q8K4D7; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q8K4D7; Protein. DR Bgee; ENSMUSG00000030230; Expressed in spermatid and 28 other cell types or tissues. DR ExpressionAtlas; Q8K4D7; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0045120; C:pronucleus; IDA:UniProtKB. DR GO; GO:0061827; C:sperm head; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:CACAO. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI. DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI. DR GO; GO:0004629; F:phospholipase C activity; IDA:MGI. DR GO; GO:0006816; P:calcium ion transport; IDA:MGI. DR GO; GO:0007343; P:egg activation; IDA:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0060470; P:positive regulation of cytosolic calcium ion concentration involved in egg activation; IDA:UniProtKB. DR CDD; cd00275; C2_PLC_like; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 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; 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:SF29; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ZETA-1; 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; PF00388; PI-PLC-X; 1. DR Pfam; PF00387; PI-PLC-Y; 1. DR PRINTS; PR00390; PHPHLIPASEC. DR SMART; SM00239; C2; 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; SSF51695; PLC-like phosphodiesterases; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. DR Genevisible; Q8K4D7; MM. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasm; Developmental protein; KW Fertilization; Hydrolase; Lipid degradation; Lipid metabolism; Nucleus; KW Reference proteome; Transducer. FT CHAIN 1..647 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase zeta-1" FT /id="PRO_0000347246" FT DOMAIN 43..78 FT /note="EF-hand" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 163..307 FT /note="PI-PLC X-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT DOMAIN 386..502 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271" FT DOMAIN 502..627 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT ACT_SITE 178 FT /evidence="ECO:0000250|UniProtKB:P10688, FT ECO:0000255|PROSITE-ProRule:PRU00270" FT ACT_SITE 223 FT /evidence="ECO:0000250|UniProtKB:P10688, FT ECO:0000255|PROSITE-ProRule:PRU00270" FT VAR_SEQ 1..110 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14701816, FT ECO:0000303|PubMed:16141072" FT /id="VSP_052863" FT MUTAGEN 210 FT /note="D->R: Defective in Ca(2+) oscillation activity and FT shows slower nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 299 FT /note="K->E: Defective in Ca(2+) oscillation activity and FT loss of nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 301 FT /note="K->E: Defective in Ca(2+) oscillation activity and FT loss of nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 376 FT /note="R->E: Abolishes nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 377 FT /note="K->E: Abolishes nuclear translocation. Prolongs FT Ca(2+) oscillations allowing them to occur during FT interphase." FT /evidence="ECO:0000269|PubMed:15159452, FT ECO:0000269|PubMed:16854985" FT MUTAGEN 378 FT /note="R->E: Abolishes nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 379 FT /note="K->E: Abolishes nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT MUTAGEN 381 FT /note="K->E: Abolishes nuclear translocation." FT /evidence="ECO:0000269|PubMed:16854985" FT CONFLICT 58 FT /note="Q -> H (in Ref. 4; AAI06768)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="R -> K (in Ref. 4; AAI06768)" FT /evidence="ECO:0000305" SQ SEQUENCE 647 AA; 74614 MW; ABE24E5CCCC63CA2 CRC64; MESQLHELAE ARWFLSKVQD DFRGGKINVE ITHKLLEKLD FPCHFAHVKH IFKENDRQNQ GRITIEEFRA IYRCIVHREE ITEIFNTYTE NRKILSENSL IEFLTQEQYE MEIDHSDSVE IINKYEPIEE VKGERQMSIE GFARYMFSSE CLLFKENCKT VYQDMNHPLS DYFISSSHNT YLISDQILGP SDIWGYVSAL VKGCRCLEID CWDGSQNEPI VYHGYTFTSK LLFKTVVQAI NKYAFVTSDY PVVLSLENHC SPGQQEVMAS ILQSTFGDFL LSDMLEEFPD TLPSPEALKF KILVKNRKVG TLSETHERIG TDKSGQVLEW KEVIYEDGDE DSGMDPETWD VFLSRIKEER EADPSTLSGI AGVKKRKRKM KIAMALSDLV IYTKAEKFRN FQYSRVYQQF NETNSIGESR ARKLSKLRVH EFIFHTAAFI TRVYPKMMRA DSSNFNPQEF WNVGCQMVAL NFQTPGLPMD LQNGKFLDNG GSGYILKPDI LRDTTLGFNP NEPEYDDHPV TLTIRIISGI QLPVSSSSNT PDIVVIIEVY GVPNDHVKQQ TRVVKNNAFS PKWNETFTFL IQVPELALIR FVVETQQGLL SGNELLGQYT LPVLCMNKGY RRVPLFSKSG ANLEPSSLFI YVWYFRE //