ID A0A1L8G1P1_XENLA Unreviewed; 1205 AA.
AC A0A1L8G1P1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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.S {ECO:0000313|RefSeq:XP_018120570.1,
GN ECO:0000313|RefSeq:XP_018120571.1, ECO:0000313|RefSeq:XP_018120572.1,
GN ECO:0000313|RefSeq:XP_018120573.1, ECO:0000313|RefSeq:XP_018120575.1,
GN ECO:0000313|RefSeq:XP_018120576.1,
GN ECO:0000313|Xenbase:XB-GENE-1010448};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018120572.1};
RN [1] {ECO:0000313|RefSeq:XP_018120570.1, ECO:0000313|RefSeq:XP_018120571.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018120570.1,
RC ECO:0000313|RefSeq:XP_018120571.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018120570.1,
RC ECO:0000313|RefSeq:XP_018120571.1};
RG RefSeq;
RL Submitted (APR-2022) 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.
CC {ECO:0000256|PIRNR:PIRNR000956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
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|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
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};
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DR RefSeq; XP_018120570.1; XM_018265081.2.
DR RefSeq; XP_018120571.1; XM_018265082.2.
DR RefSeq; XP_018120572.1; XM_018265083.2.
DR RefSeq; XP_018120573.1; XM_018265084.2.
DR RefSeq; XP_018120575.1; XM_018265086.2.
DR RefSeq; XP_018120576.1; XM_018265087.2.
DR STRING; 8355.A0A1L8G1P1; -.
DR PaxDb; 8355-A0A1L8G1P1; -.
DR GeneID; 445848; -.
DR KEGG; xla:445848; -.
DR AGR; Xenbase:XB-GENE-1010448; -.
DR CTD; 445848; -.
DR Xenbase; XB-GENE-1010448; plcb4.S.
DR OMA; AMQKAHC; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 445848; Expressed in neurula embryo and 18 other cell types or tissues.
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; cd16211; EFh_PI-PLCbeta4; 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:UP000186698};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 577..693
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 696..821
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 876..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..915
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 375
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 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1205 AA; 136809 MW; 81C232E34BC03118 CRC64;
MAKVYEFNWQ KAVPSFMQDG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW KSEGKEGQVL
ECSLINSIRY GAVPKDPKIL SALEAVGKAE QELEGKILCV CCGTDLVNIS FTYMVAESAD
LAKQWVEGLK SITHNFRANN VSPMTCLKKH WMKLKFLTNI SGKIPVRSIT RTFASGKTEK
VIFQALKELG LPSGKNDEIE PSAFTFDKFY ELTQKICPRT DTEELFKKIN GDKSDYLTVD
QLVSFLNEHQ RDPRLNEILF PFFDAKRAMQ IIETYEPDDE LKKGGQISSH GFCRYLMSDE
NAPVFLDRLE LYQEMDQPLA HYFISSSHNT YLTGRQFGGK SAVEMYRQVL LAGCRCVELD
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKDTAFVTS EYPVILSFEN HCSKYQQYKM
SKYCEEIFGD LLLSKALESH PLDSGRPLPS PNDLKRKILI KNKRLKPEVE KKQLEALKSM
MEAGETATPV SILEDDIEEE TENADLEEEA HPEFKFGSEL SADDLSQKEA ASIAKKMAED
AEQENNNKKG AITVEDEQAW MASYKYVGAT TNIHPFLSSM INYAQPIKFQ GFKVAEERNI
HFNMSSFNES VGLGYLKTHA LEFVNYNKRQ MSRIYPKGGR VDSSNYMPQI FWNAGCQMVS
LNYQTPDLAM QLNQGKFEYN GSCGYLLKPD FMRRPDRTFD PFSETPVDGV IAATCSVQVI
SGQFLSDKKI GTYVEVDMYG LPTDTIRKEF RTRMVMNNGL NPVYNDEPFV FRKVILPDLA
VLRIAVYDDN NKLIGQRLLP LDGLQAGYRH ISLRNEGNKP LSLPTIFCNI VLKTYVPDGF
GDIVDALSDP KKFLSITEKR ADQMRAMGIE TSDIADVPAD NTKNDKKGKV SNTKTIVTPQ
SSSEVRPSVT TAPGAGTENK KAIDIPQVKV EELKQMKAFL KQQKKQQKEV AVLKKKHLKE
HSAMQKLQCT QVDKIVAQFD KEKVSQSRTL EKSIKKKGAS NCLEMKKETE NKIQVLTSDH
KSKVKDIVAQ HTKEFTEMVK AQNAEEQTLR DLHLSQQCEL LKELLRGIHA QQMQQLKLTH
ERESKEMKAN QAKLSMENCK AISQDKSIKN KAERERRVRE LNSSNTKKFL EERKRLAMKQ
SKEIEQLIKN QAEHMEILEK QNEQHMKVCH AVSQSQGKGD AADGEAGSRD GPPSSNCCVK
LQNVN
//
