ID A0A0V1C2R4_TRISP Unreviewed; 1192 AA.
AC A0A0V1C2R4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN Name=Plcb4 {ECO:0000313|EMBL:KRY43409.1};
GN ORFNames=T01_9074 {ECO:0000313|EMBL:KRY43409.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY43409.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY43409.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY43409.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY43409.1}.
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DR EMBL; JYDH01000001; KRY43409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1C2R4; -.
DR STRING; 6334.A0A0V1C2R4; -.
DR eggNOG; KOG1265; Eukaryota.
DR InParanoid; A0A0V1C2R4; -.
DR Proteomes; UP000054776; 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; 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; IPR009535; PLC-beta_CS.
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:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 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 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:UP000054776};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 570..686
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 689..814
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 484..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 377
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 360
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 1192 AA; 137025 MW; E9316373FEA8B0E2 CRC64;
MNKDLEFKWQ VSVPDHLRRG LHFDRWDEET NTFELRCFVQ VDEYGFFLYW TAEGKEAQIL
DLTQVSDVRS GCWLKDTKAP PDFELRFTGS RESLESRAVT VVSGVDFVNL NFTCFIAEEA
TIAQEWKIAM MKVLKNFRVA HVCPMTCLLK HWKMLSLSLN ANRKIPVKNI VRTFISGRTE
KFIIQCLVDS RLCEGKNLEI DPEKFTFDTF YHLCVRICPR PEIHELFSQI AGSEEFITVA
QLISFLNEKQ RDPRLNEILY PECDKSKAMI VLRKYEQVEE HVNQEKLYYD GFLRFMMSED
NAPMLYDRIE LNQDMDQPLS DYLINSSHNT YLTGRQFGGR SSVEMYRQVL LSGCRCIELD
CWDGTSGVGK DEPIITHGKA MCTDILFKDV IAAIKETAFV TSVYPVILSF ENHCSKKNQL
KMAAYCMKIF GDMLLSSPLS SHPLEPGVPL PSPNQLKGKI LIKSKRLNPD VEKQELEQFL
KKGQLDEDVE EVSENPEVDE TPGTDSTTDV LNENEAHPEL KGTESVTFRS KLRSLAGAKI
KEMALSKEEE ERLLAQYHYI SATTNIHPLL SSLVNYTQPV KFAGFDVAEQ NNCHFHMSSF
SESTGLGYLK TSAIELVNYN KRQISRIYPK GGRVDSSNYL PQIFWNAGCQ MVSLNFQTPD
LAMQLNQGKF EYNGTCGYLL KPDFLRRADR MFDPFSESPV DGVVAAYCSV RVISGQFLSE
KKIGTYVEVE MYGLPTDTIR KEFKTKMVPS NGLNPVYNEE PFVFRKIVLP ELAVLRFAVY
DENSKLLGQR ILPLDGLQPG YRHISLRSEI NFPLTLPTLF CHIVLKTYIP EGLGDIVEAL
SDPKGYLSMI EKRQQQMEHM GIRREDIDEV PSDRKPITVK NSGGDSVDSI SEVKSTACPA
TPISSSSTQT SGKAIKEMGL LQLKLDEHVT YEELKLEKAY VKLTKKHLKE YEYIKRRHAK
ERLGMQRQQT LAFEKITAKK QPLAFVRNQS KSLSQNRSEH RSVYQSKSLD VTGPNNRLHD
GVGPSRMMHI RHAIAEQTRD WSELTKRQLE AEHRMRKTQI EEEWTLLKKL LVQVHQQQRT
AAKQQLEAES KLLRQKQTKK SMDDSKAIQL GKTVKTKAER DRRVKEVQEK NCKIFLEERR
RLAVKHQRQE ELLAKFQAEQ MERLDKEARH ASDLEDQMYM EALLASKPET LV
//
