ID A0A3Q2ZCQ2_KRYMA Unreviewed; 1157 AA.
AC A0A3Q2ZCQ2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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|Ensembl:ENSKMAP00000001303.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000001303.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000001303.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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.
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 AlphaFoldDB; A0A3Q2ZCQ2; -.
DR STRING; 37003.ENSKMAP00000001303; -.
DR Ensembl; ENSKMAT00000001341.1; ENSKMAP00000001303.1; ENSKMAG00000000908.1.
DR GeneTree; ENSGT00940000156426; -.
DR OMA; AMQKAHC; -.
DR Proteomes; UP000264800; Unplaced.
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 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:UP000264800};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 545..661
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 664..789
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 843..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 907..934
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1075..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 373
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 356
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 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1157 AA; 132519 MW; DD5A4247ED622F46 CRC64;
MTKSYEFNWQ KHLPEFMQEG ASFDRFDEDP YIFEPNCQMK VDEYGFFITW KSEGKEGQLL
ECSLINSIRV GAVPKDPKIL SSFEAVGKTE ADLEGCIICI CSGTDLVNLS FMFMVAENPD
VKWIEGLRSV IHNFKANNVC PMTCLKKHWM RMCFLTNVNG KIPVRGITRT FASGKTEKGI
FQALKDLGLP SGKNDEIEPS DFTFDIFYAL TQKICPRTDI EELFKKINGN KTDYLTVDQL
VSFLNENQRD PRLNEILFPF YDPKRAMQII EKYERDEELK KKGHMSSDGF CRYLMSDENA
PVFLDRLELY QEMDQPLAHY FISSSHNTYL TGRQFGGKSS VEMYRQVLLS GCRCVELDCW
DGKGEDQEPI ITHGKAMCTD ILFKDVIQAI KETAFVTSEY PVILSFENHC SKLQQYKMAK
YCEEIFSDLL LRQPLENYSL EPGRPLPSPN DLKRKILIKN KRLKPEVEQR QLESLKKHME
AGETNTPAII MGEEDDTENG QLTDFIFTLS AFMCQVAGDV AEDSEEALIA SYQYESATTN
IHPYLSAMVN YAQPVKFQGF DVAEERNIHH NMSSFNESVG LGYLKTNAIE FVNYNKRQMS
RIYPKGGRVD SSNYMPQIFW NAGCQMVSLN FQTPDLAMQL NQGKFEYNGS CGYLLKPDFM
RRSDRTFDPF SETPVDGVIA ATCSVQVFSG QFLSDKKIGT YVEVDMYGLP TDTIRKEFRT
RMVMNNGLNP AYNEEPFVFR KVILPDLAVL RIAVYDDNNK LIGQRILPLD GLQAGYRHIS
LRNEGNKPLS LPTVFCQIIL KTYVPDGFGA IVDALSDPKK FLTIAEKRAD QMKALGIDTN
DIADVPSGSS KNDKKGKGKG DTMKVSVTQQ ASSEIAQTSN FINNNTTEAK KDTALVPSVS
IDDLKQMKTY LKLIKKQQKE INTLKKKHSK DQNAMQKAHC TQVDKMVSMH EKDKTTLEKL
LEKAIKKRGE NNCQELKKET EDKIQTLVGD HKAKVKDITA QHTKEWSELI SSHSSEEQEM
KDSHVTQQCV HLKKLLTSVQ EQQTIQLKLI HERQSKEMRA NQAKTSMENS KAISQDKTIK
NKAERERRVR ELNSSNTKKF LDERKRLAMK HQKEMEQLEK NQREQLDKLE KHNEQAKDIQ
QMVKLEEEMD RRPATVV
//
