ID A0A2I3FSY6_NOMLE Unreviewed; 415 AA.
AC A0A2I3FSY6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=PLCZ1 {ECO:0000313|Ensembl:ENSNLEP00000024861.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000024861.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000024861.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000024861.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003992}.
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:0000256|RuleBase:RU361133};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}.
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DR EMBL; ADFV01029126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01029127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3FSY6; -.
DR Ensembl; ENSNLET00000035314.1; ENSNLEP00000024861.1; ENSNLEG00000004405.2.
DR GeneTree; ENSGT00940000159950; -.
DR Proteomes; UP000001073; Chromosome 23.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00275; C2_PLC_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
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; 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; 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 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 156..272
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 272..396
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 415 AA; 47896 MW; 8FC0A1A9070352A0 CRC64;
MEMRWFLSKI QDDFRGGKIN LEKTQKLLEK LDIRCSYIHV KQIFKTSDYP VVLSLENHCS
TAQQEVMADN LQATFGESLL SDMLDDFPDT LPSPEALKFK ILVKNKKIGT LKETRERKGS
DKREDNQDKE TGVKKLPGVI LFKKKKTRKL KIALALSDLV IYTKAEKFKS FQHSRLYQQF
NENNSIGETQ ARKLSKLRVH EFIFHTRKFI TRIYPKATRA DSSNFNPQEF WNIGCQMVAL
NFQTPGLPMD LQNGKFLDNG GSGYILKPHF LRENKYYFNP SNIKEGMPIT LTIRLISGIQ
LPLTHSSSNK GDSLVIIEVF GVPNDQMKQQ TRVIKKNAFS PRWNETFTFI IHVPELALIR
FVVESQGSIA GNEFLGQYTL PLLCMNKGYR RVPLFSRMGE SLEPASLFVY VWYVR
//
