PLCZ1_RAT
ID PLCZ1_RAT Reviewed; 645 AA.
AC Q5FX52;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
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|RGD:1359567};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAW66659.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAW66659.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAW66659.1};
RA Saunders C.M.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION.
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:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:18322275,
CC ECO:0000305}.
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:Q8K4D7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q8K4D7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8K4D7};
CC -!- SUBUNIT: Interacts via its C2 domain with PtdIns(3)P and, to a lesser
CC extent, PtdIns(5)P in vitro. {ECO:0000250|UniProtKB:Q8K4D7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}.
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 pronucleus at interphase following meiosis and mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K4D7}.
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:0000250|UniProtKB:Q8K4D7}.
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:0000250|UniProtKB:Q8K4D7}.
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DR EMBL; AY885259; AAW66659.1; -; mRNA.
DR RefSeq; NP_001012234.1; NM_001012234.1.
DR RefSeq; XP_006237659.1; XM_006237597.3.
DR RefSeq; XP_017448259.1; XM_017592770.1.
DR AlphaFoldDB; Q5FX52; -.
DR SMR; Q5FX52; -.
DR STRING; 10116.ENSRNOP00000011376; -.
DR iPTMnet; Q5FX52; -.
DR PhosphoSitePlus; Q5FX52; -.
DR PaxDb; Q5FX52; -.
DR Ensembl; ENSRNOT00000011376; ENSRNOP00000011376; ENSRNOG00000008514.
DR GeneID; 497197; -.
DR KEGG; rno:497197; -.
DR UCSC; RGD:1359567; rat.
DR CTD; 89869; -.
DR RGD; 1359567; Plcz1.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000159950; -.
DR HOGENOM; CLU_002738_0_3_1; -.
DR InParanoid; Q5FX52; -.
DR OMA; YLTCTLV; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q5FX52; -.
DR TreeFam; TF313216; -.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:Q5FX52; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008514; Expressed in testis.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045120; C:pronucleus; ISO:RGD.
DR GO; GO:0061827; C:sperm head; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISO:RGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:RGD.
DR GO; GO:0004629; F:phospholipase C activity; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0007343; P:egg activation; ISS:UniProtKB.
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:RGD.
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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Developmental protein; Fertilization; Hydrolase;
KW Lipid degradation; Lipid metabolism; Nucleus; Reference proteome;
KW Transducer.
FT CHAIN 1..645
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase zeta-1"
FT /id="PRO_0000347248"
FT DOMAIN 42..77
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 162..306
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 385..501
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 501..625
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ACT_SITE 177
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 222
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 645 AA; 74315 MW; 73767CFE3AF62B8D CRC64;
MESHYELAEA RWFMSKIQDY FRGGKISAGI THKLLEKLDF PCHFAHVKRI FKENDRHNQG
RITTEDFRTI YRCIVHREEI VEIFNTYTEN RKILPEDSLI EFLTQEQYEM EMDESSSVEI
IQKYEPIAEV KNERQMSIEG FARYMFSSEC LLFKETCNTV YQDMNKPLND YYISSSHNTY
LISDQILGPS DIWGYISALV KGCRCLEIDC WDGAQNEPIV YHGYTLTSKL LFKTVIQAIN
KYAFVTSDYP VVLSLENHCS PGQQEVMTDI LQSTFGDFLL SDILDEFPDS LPSPEALKFK
ILVKNKKVGT LSETRERLGT DKRGIALDLE EEIYENEDED SGKEPETWDD FLSRVKEEQE
ADPSTLSGIA DAKKKIRKLR VALALSDLVI YTKAEKFRNF QYSRVYQQFN ETTSMGESRA
RKLSKLRAHE FIFHTAAFIT RVYPKFTRAD SSNFNPQEFW NVGCQMVALN FQTPGLPMDL
QNGKFLDNGG SGYVLKPDFL RDTTLGFNPN EPEGDGHPVT LTIRLISGIQ LPVNVPSNTS
DIIVIIEVYG VPNDHMKQQS RAVKNNAFSP RWNETFTFLI QVPELALIRF VVETQGFLSG
NELLGQYTLP VLCMNKGYRR VPLFSKSGAN LEPSSLFIYV WYYRE
