PLCZ1_MOUSE
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 03-AUG-2022, entry version 151.
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.
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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; Q8K4D7; -.
DR PRIDE; Q8K4D7; -.
DR ProteomicsDB; 288231; -. [Q8K4D7-1]
DR ProteomicsDB; 288232; -. [Q8K4D7-2]
DR Antibodypedia; 52401; 130 antibodies from 18 providers.
DR DNASU; 114875; -.
DR Ensembl; ENSMUST00000032356; ENSMUSP00000032356; ENSMUSG00000030230. [Q8K4D7-1]
DR GeneID; 114875; -.
DR KEGG; mmu:114875; -.
DR UCSC; uc012evc.2; mouse. [Q8K4D7-1]
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; 368239at2759; -.
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 73 CRISPR screens.
DR PRO; PR:Q8K4D7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8K4D7; protein.
DR Bgee; ENSMUSG00000030230; Expressed in spermatid and 27 other tissues.
DR ExpressionAtlas; Q8K4D7; baseline and differential.
DR Genevisible; Q8K4D7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
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 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; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR028395; PLC-zeta1.
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:SF29; PTHR10336:SF29; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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.
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
