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Database: UniProt
Entry: A0A3F2Z1Y3_ANOQN
LinkDB: A0A3F2Z1Y3_ANOQN
Original site: A0A3F2Z1Y3_ANOQN 
ID   A0A3F2Z1Y3_ANOQN        Unreviewed;      1050 AA.
AC   A0A3F2Z1Y3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-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   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA017058-PB, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA017058-PB}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA017058-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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};
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DR   STRING; 34691.A0A3F2Z1Y3; -.
DR   EnsemblMetazoa; AQUA017058-RB; AQUA017058-PB; AQUA017058.
DR   VEuPathDB; VectorBase:AQUA017058; -.
DR   Proteomes; UP000076407; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF149; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE CLASSES I AND II; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF17787; PH_14; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 2.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361133}.
FT   DOMAIN          326..442
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          445..570
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          760..787
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          882..909
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        232..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1050 AA;  114414 MW;  750BF2E38683BEAA CRC64;
     MASLLTAADR QHSTTQSPQS LSGSCSPRNA ASPNANAAAA ATTAGGQPTA GGGGNTAVAL
     NNPTAVKLGV MDVPKALQDG EKFIKWDEDS CNGTPVTLRV DVKGFFLYWV DQNHEMDMLD
     IATIRDVRTG QYAKKPRDMK LRQIVTMGSQ DTLEEKTVTV CYGADFVNVN FINFCCTRKE
     IARLWCDELI RMAYNLTQLN GPAIMFLQKA YTKLCLQVDK SGKIPVKXXA NPSLPPSQQD
     EPNGTVVVSN NNGTATPLQA TGNGEIPHHA PPLQQIRQSS KESTGSSDTD SSSDDESMPG
     TVVGPIGASE ADKVPQTKET EAGAEISALV NYVQPVHFSS FENSEKKARF YEMSSFDEKQ
     ATTLLKERPI EFVNYNKHQL SRVYPAGTRF DSSNFMPQLF WNAGCQLVAL NYQTLDLAMQ
     LNLGIFEYNH RCGYILKPEF MRRKDRRLDP FAESTVDGII AGTVMVTVIS GQFLTDKKVG
     TYVEVDMFGL PADTVRKKFR TKIVRDNGIN PVYDEEPFVF KKVVLPELAS IRIAAYEEGG
     KLIGHRVLPV IGLCPGYRHL TLRTEVGQPI PLATLFLCIV VKDYVPDGLS DFAEALANPI
     KYQSEQEKRS KQLAVLQEDM EPSDEDSCTN KKGDTLRSSE TNNTTSSPAR QRSVAGTQSS
     QGGAGGTADS DAEAPLEAIT KMVALPVAQS SSLDHSNVPA AKLSTTSREP TTTGGGGGGG
     SGAPIITTTT NTPNVATGEG LNAANGGKIV ADPLEKIFED KQIRKKREAL EKELKALKKS
     HDKEKLKIHA AQKSTDLGGG DAPVKKSKFG MGNKLVKRFS SKNMADMNVK VPPCASVSDA
     EGTGDAQAER LRQICRDHAG SYREVLEKYH DIIYTLAEDL LRQSQDAQMK QLKTQLERET
     SEVMRQLQLS RKSEVKQLAM VHKDKDELER MKREVDSTLV EKGVTERVRL TATYERKRDE
     LQRQHDSVKQ GLEDHKLKAR SMLEKEAESH AFISDTFLAH LNTSNSTTSC SSVGATTNHP
     PATSVSSGNI CGAGGTAGST HENNVNNAHA
//
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