ID A0A0L0CID1_LUCCU Unreviewed; 1302 AA.
AC A0A0L0CID1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN ORFNames=FF38_14384 {ECO:0000313|EMBL:KNC31249.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC31249.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC31249.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC31249.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC31249.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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.
CC {ECO:0000256|PIRNR:PIRNR000956}.
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|PIRNR:PIRNR000956,
CC ECO:0000256|RuleBase:RU361133};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC31249.1}.
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DR EMBL; JRES01000438; KNC31249.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0CID1; -.
DR EnsemblMetazoa; KNC31249; KNC31249; FF38_14384.
DR OMA; DQQIGNG; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
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; cd16213; EFh_PI-PLC21; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.30.29.240; -; 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; 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; IPR011992; EF-hand-dom_pair.
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; 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:SF149; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE CLASSES I AND II; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 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 Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000956};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 598..714
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 717..842
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 465..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 992..1019
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 465..484
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 377
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1302 AA; 147013 MW; 64766B025551D940 CRC64;
MLSTGTYVSS GPIEVSQAMQ DGEKFIKWDD DSCMGVPVTM RVDPSGFFLL WVDQNNEMDI
LDISTIRDVR TGQYAKKPKD PKLSQIVTLG SQDTLEEKTV TICHGADFVN LTFVNFCCTK
KEIAQHWCDG LMRLAYSLVQ LNGSVNMFLK KAHTKLCLQT DKTDKIPVKN IVKMFAQNKD
DRKRVEKALE NTGIPSGKLE SVPISKFTFE EFYNLYKNLT QRSEVEKVFD NIVGNTKRKY
MTTNQFMDFL NNTQRDPRLN EILYPYADTE RAKEIIKQYE PNQFNIQKGL LSLDGFLRYL
MSDDNPIMAA SKWDLNDDMN QPLSHYFINS SHNTYLTGHQ LTGKSSVEIY RQCLLAGCRC
VELDFWNGRT DEPVIVHGYT FVPEIFAKDV LEAIAESAFK TSEYPVILSF ENHCNPRQQA
KIANYCREIF GDMLLDKPLD SHPLEPNVDL PPPSFLRRKI IIKNKKKHHH HHHHHHHHHK
KSTSGSTSNN KQLISANSVD ATNKVASIAP SLLNMQPQVS IQEDGNTTAT TNGDIGNGSN
HAPPLQQLRQ SSKDSTGSSD TDSSSDDESL PNTTPILPSG NEPPPEKAQK ETEAGAEISA
LVNYVQPIHF SSFENAEKKN RNYEMSSFDE KQATTLLKER PIEFVNYNKH QLSRVYPAGT
RFDSSNFMPQ LFWNAGCQLV ALNFQTLDLA MQLNLGIFEY NGRCGYLLKP EFMRRTDRRL
DPFAESTVDG IIAGSVSITV LSGQFLSDKR VGTYVEVDMF GLPADTVRKK FRTKIVRDNG
INPIYDEEPF VFKKVVLPAL ASIRIAAYEE NGKFIGHRVL PVIGLRPGYR HLSLRTEMGQ
ALPLTSLFLC IVVKDYVPDD IAIFAEALAN PIKYQNELEK RDKQLAVLQE DTEPITEEDI
TNSLGGQKKE LKPVESNTIS PKHRSSITAS ATMSVEISNA RDTADSASAT MQSIQHQHSL
DSTAPTSVRQ IESSQFDVES LAAEPLEKIL EHKTVREKRL EMEKKLESLR KKHDKEKIKI
CGSKLSPMDS SKKTKFAITN KLVKRLSNKN LESTTEVPPC AIDLGENQEE CSGDTMQSLE
GTVDERLLNS CRQYSQQYRE LQKKYHEAIY ATAEKVLQAS QDSQLKLLKS SLDKVNNEVM
HQLREARKVE VKNLALVHKD KDEFVRMKRE VRRSVVERGV AERTRLMDVY KQRHEDLRKQ
HDIVKNNLME HKTMARQIVD KECESRTCVT TNGFLVLFQN TSATSTCTSS SLSNDHHHHL
SLDVGSSSNK LALSPARSNS SISNSTAACS ASATTVVLPH KC
//
