PLCZ1_CHICK
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 03-AUG-2022, entry version 125.
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; Q2VRL0; -.
DR Ensembl; ENSGALT00000021418; ENSGALP00000021386; ENSGALG00000013123.
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; 368239at2759; -.
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 tissues.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
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; IBA:GO_Central.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0060470; P:positive regulation of cytosolic calcium ion concentration involved in egg activation; IBA:GO_Central.
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; 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; 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
