ID A0A3B3U5Z3_9TELE Unreviewed; 507 AA.
AC A0A3B3U5Z3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000008054.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000008054.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3U5Z3; -.
DR STRING; 48699.ENSPLAP00000008054; -.
DR Ensembl; ENSPLAT00000003523.1; ENSPLAP00000008054.1; ENSPLAG00000010534.1.
DR GeneTree; ENSGT00940000159950; -.
DR Proteomes; UP000261500; Unplaced.
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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
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 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 Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 246..361
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 366..485
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 507 AA; 57813 MW; F228C5F508AF279D CRC64;
MQVMLKRTKV LQSRRVEILS LFQRYTEGIP TLPASALLTF LCKEQMELAA NKDTAEDLID
RYEIDEAGER LKNRCMTFEG FLRYMESKDC CVFNRTHKTV YQDMDQPLTS YFISTSHNTY
LTGDQLVGKS HLDAYVSALR KGCRCLEIDC WDGPDTEPVV YHGYTLTTKI LFKDVIRTVE
QHAFEVSAYP VILSLENHCC EEQQEVMAEY LTSILGDKLL KSPLDHPTTG DLPSPNQRKV
KVARALSDLV IYTRSVKFIS FSHSRDNQNC YENTSMAEKK ARKLIKASAS SFIQHNQRFL
SRIYPAGSRT SSSNYNPQEF WNVGAQLVAL NFQSPGLSMD LNNGRFQDNG GCGYVLKPAV
LMPSERSFDP STSCRYLKPI QLVLKVISGS NLPVIKSRNT LDPFVRVEIH GIAFDSRSKS
THTVKNNSMT PRWDTDMNFN ITVPELCLIR FCVRDQTTLF KSEFVGQYTM PFTSLKKVRY
TQLDLRIVSC NTQSLHQTSL HQSSVML
//
