ID   PLCZ1_CHICK             Reviewed;         637 AA.
AC   Q2VRL0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 130.
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:0000250|UniProtKB:Q86YW0};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAX48001.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis {ECO:0000269|PubMed:16049153};
RX   PubMed=16049153; DOI=10.1530/rep.1.00707;
RA   Coward K., Ponting C.P., Chang H.-Y., Hibbitt O., Savolainen P.,
RA   Jones K.T., Parrington J.;
RT   "Phospholipase Czeta, the trigger of egg activation in mammals, is present
RT   in a non-mammalian species.";
RL   Reproduction 130:157-163(2005).
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:16049153,
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   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC       {ECO:0000269|PubMed:16049153}.
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; AY843531; AAX48001.1; -; mRNA.
DR   RefSeq; NP_001034362.1; NM_001039273.1.
DR   AlphaFoldDB; Q2VRL0; -.
DR   SMR; Q2VRL0; -.
DR   STRING; 9031.ENSGALP00000021386; -.
DR   PaxDb; 9031-ENSGALP00000021386; -.
DR   Ensembl; ENSGALT00000021418; ENSGALP00000021386; ENSGALG00000013123.
DR   Ensembl; ENSGALT00010032802.1; ENSGALP00010019429.1; ENSGALG00010013636.1.
DR   GeneID; 418182; -.
DR   KEGG; gga:418182; -.
DR   CTD; 89869; -.
DR   VEuPathDB; HostDB:geneid_418182; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   GeneTree; ENSGT00940000159950; -.
DR   HOGENOM; CLU_002738_0_2_1; -.
DR   InParanoid; Q2VRL0; -.
DR   OMA; YLTCTLV; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; Q2VRL0; -.
DR   TreeFam; TF313216; -.
DR   Reactome; R-GGA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   PRO; PR:Q2VRL0; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000013123; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR   GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0060470; P:positive regulation of cytosolic calcium ion concentration involved in egg activation; IBA:GO_Central.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16204; EFh_PI-PLCzeta; 1.
DR   CDD; cd08595; PI-PLCc_zeta; 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; 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; 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..637
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase zeta-1"
FT                   /id="PRO_0000347249"
FT   DOMAIN          36..72
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          157..302
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          377..493
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          493..619
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          310..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250|UniProtKB:P10688,
FT                   ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000250|UniProtKB:P10688,
FT                   ECO:0000255|PROSITE-ProRule:PRU00270"
SQ   SEQUENCE   637 AA;  72533 MW;  8FFFA824997BA401 CRC64;
     MEENRWFLNI IQDGFMNGKI DFDSTVKLLE KLHMPFNLAH VKHVFKKTVD KRKIHTINIE
     DFRAIYRAIV HRNEFHEIFC AYSENRKNLA DTELTAFLKK EQFKTEGAET TALEVILKYE
     PIDEVRKRRQ LSFEGFIRYM SSEDCTIFKK EHRTVYQDMN HPLCDYFISS SHNTYLVSDQ
     LIGPSDLNGY ISALLKGCRC LEIDCWDGSN NDPVVYHGHT LTSKITFCSV IHVVDKYAFA
     ASDYPVVLSL ENHCSTKQQE RIAQYLLNIL GDKLLTSPIG DIEVTQLPSP EALKFKILVK
     NKKCGTIEET MLRKGRDSHG ETGEVSEEEI TSSDEETDEK TPLYPKSGSS KRKSEGRSSP
     PPRKKAKVKK MKIAMGLSDL VIYTKSEKFV SFEHSLAHQK CYENNSIGEL KAQKFVKHAA
     NQFVSHTSRF ITRIYPKGTR AGSSNYNPQE FWNVGCQMVA LNFQTSGTPM ELQNGKFLDN
     GGCGYILKPE FLRNRNSTFN PHNVGRYSNP LSLSIRLISG HQLPPSNLSK SNKADPLVQL
     EIYGVPEDQA KRKSSVIKSN ALSPRWDETF SFTVQVPELA LIRFCVQDEI SLVANDFLGQ
     YTLPLLSLSK GYCTVPLFSK SGGKLEPASL FVYVWYY
//