PLCZ1_PIG
ID PLCZ1_PIG Reviewed; 636 AA.
AC Q7YRU3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=PLCZ {ECO:0000312|EMBL:BAC78817.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC78817.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Landrace {ECO:0000269|PubMed:16940280};
RC TISSUE=Testis {ECO:0000269|PubMed:16940280};
RX PubMed=16940280; DOI=10.1530/rep.1.01018;
RA Yoneda A., Kashima M., Yoshida S., Terada K., Nakagawa S., Sakamoto A.,
RA Hayakawa K., Suzuki K., Ueda J., Watanabe T.;
RT "Molecular cloning, testicular postnatal expression, and oocyte-activating
RT potential of porcine phospholipase Czeta.";
RL Reproduction 132:393-401(2006).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=16098961; DOI=10.1016/j.ydbio.2005.06.029;
RA Kurokawa M., Sato K., Wu H., He C., Malcuit C., Black S.J., Fukami K.,
RA Fissore R.A.;
RT "Functional, biochemical, and chromatographic characterization of the
RT complete [Ca2+]i oscillation-inducing activity of porcine sperm.";
RL Dev. Biol. 285:376-392(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:16098961,
CC ECO:0000269|PubMed:16940280, 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:16940280}.
CC -!- DEVELOPMENTAL STAGE: In testes, detected only when the elongated
CC spermatids have differentiated from 96 days after birth.
CC {ECO:0000269|PubMed:16940280}.
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; AB113581; BAC78817.1; -; mRNA.
DR RefSeq; NP_999515.1; NM_214350.1.
DR AlphaFoldDB; Q7YRU3; -.
DR SMR; Q7YRU3; -.
DR STRING; 9823.ENSSSCP00000000621; -.
DR PaxDb; Q7YRU3; -.
DR GeneID; 397632; -.
DR KEGG; ssc:397632; -.
DR CTD; 89869; -.
DR eggNOG; KOG0169; Eukaryota.
DR InParanoid; Q7YRU3; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IEA:InterPro.
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: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; Coiled coil; Cytoplasm; Developmental protein; Fertilization;
KW Hydrolase; Lipid degradation; Lipid metabolism; Nucleus;
KW Reference proteome; Transducer.
FT CHAIN 1..636
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase zeta-1"
FT /id="PRO_0000347247"
FT DOMAIN 35..70
FT /note="EF-hand"
FT /evidence="ECO:0000255"
FT DOMAIN 155..299
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 375..491
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 491..617
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 311..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..345
FT /evidence="ECO:0000255"
FT COMPBIAS 323..338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 215
FT /evidence="ECO:0000250|UniProtKB:P10688,
FT ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 636 AA; 73702 MW; A558E05243ECF479 CRC64;
MENKWFLSMV RDDFKGGKIN LEKAQKLLEK LDIQCNTIHV KCIFKDNDRL KQGRITIEEF
RTIYRIIAHR EEIIEIFNAY PENRKILFER NLIDFLTQEQ YSLDINRSIV YEIIQKYEPI
EEVKQAHQMS FEGFTRDMGS SECLLFNNEC GSVYQDMTHP LSDYFISSSH NTYLISDQIM
GPSNLWGYVS ALVKGCRCLE IDCWDGSQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFITS
DYPVVLSLEN HCSLSQQEVM ADNLQSVFGD ALLSDVLDDC PDRLPSPEAL KFKILVRNKK
IGTLKETHER KGFDKHGQVQ ECEEEEEAEQ EEEENEVRDS EILDILQDDL EKEELKRGVG
IKFFKKKKVK IATALSDLVI YTKVEKFRSF HYSRLYQQFN ETNSIGETQA RKLSKLRASE
FILHTRKFIT RIYPKATRAD SSNFNPQEFW NIGCQMVALN FQTPGLPMDL QNGKFLENGN
SGYILKPHFL RDGKSIFNPN KAPINSNPIT LTIRLISGIQ LPPSYHSSSN KADTLVIIEI
FGVPNDQMKQ QTRVIKKNAF SPRWNETFTF IIQVPELALI RFVVENQGLI TGNEFLGQYT
LPVLCMNKGY RRVPLFSKMG ESLEPASLFI YVWYIR
