ID   A0A8M9PW40_DANRE        Unreviewed;      1275 AA.
AC   A0A8M9PW40;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   28-JUN-2023, entry version 6.
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|RefSeq:XP_021326566.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021326566.1};
RN   [1] {ECO:0000313|RefSeq:XP_021326566.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-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   RefSeq; XP_021326566.1; XM_021470891.1.
DR   KEGG; dre:407700; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:SF36; 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|PIRNR:PIRNR000956, ECO:0000256|RuleBase:RU361133};
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:UP000000437};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1275
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035439033"
FT   DOMAIN          654..750
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          750..878
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          533..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1143..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          990..1050
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1181..1218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        948..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   BINDING         386
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         415
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         417
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         466
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ   SEQUENCE   1275 AA;  144845 MW;  C6A445DC012D14C5 CRC64;
     MCVDVRRITV IWLLALRLAA SAVSRGRSAV LRHAAXXXXX XXXXXXXXXX XXGLRAVMTK
     SYEFNWQKHI PDFLQEGAAF DRFDEDPFLF EPSCLFKVDE FGFFLTWKSD GKEGQLLECS
     LINSVRPAVV SKDSKILACL EAAGRSEADL DGRIICVCSG PDLVNLSFMY MVTDNTDTAK
     KWMEGLKSVI HNFKANNVCP MTCLKKHWMR LSFLTNVNGK IPVRGITRTF GSGKTEKGIF
     QALKELGLPS GKNDEIEHSA FTFDIFYALT QKICPRTDIE ELFKKINGDK SDYLTVEQLV
     SFLNENQRDP RLNEILFPFY EAKRVTQIIE KYERDAELKK KGRMSSDGFC RYLMSDENAP
     VFLDRLDLCQ EMEHPLSHYF ISSSHNTYLT GRQFGGKSSV EMYRQVLLSG CRCVELDCWD
     GKGEDQEPII THGKAMCTDI LFKDVIQAIR ETAFVTSEYP VILSFENHCC KPQQYKMAKY
     CEEIFGDLLL KQPLEGFPLE AGQQLPSPND LRRKILIKNK RLKPEVEQKQ LESFKKHMEA
     GEISIPAGED ENEEDLDSAL DGKEVSSELK AGLLQCVSED QDAPDSSFRR KITDDDATEI
     SEVTEITDAT DVSEASDIES KKKGVESSED ADAEQQLIAS YKYEGATTNI HPYLSAMVNY
     AQPVKFQSFE VAEGQSESQT RSYNKRQMSR IYPKGGRVDS SNYMPQIFWN AGCQMVSLNF
     QTPDLGMQLN QGKFEYNGAC GYLLKPDFMR RGDRMFXPFS ETPVDGVIAA TCSVQVFSGQ
     FLSDKKIGTY VEVDMYGLPT DTIRKEFRTR MVMNNGLNPY YNEEPFVFRK VILPDLAVLR
     IAVFDDNSKL IGQRLLPLDG LQAGYRHISL RNEGNKPLSL PTVFCNIVLK TYVPDGFGAI
     VDALSDPKKF LTIAEKRADQ MRALGIETSD IADVPNESSK SDKKSKVSQV KSSVTPQSSA
     ETNNTHNNTN DTRGDHSVVN QVNIEDLKQM KTFIKLLKKQ QKELNTLKKR HAKEHNAMQK
     SHCTQVDKLV AQHDKEKNTL EKLLEKAIKK RGETNCSELK KETAVKIETL TTDHKEKVKD
     MVAQHTKEWS EMLSGCSSEE QELKDTHITQ QSELLKRLMS SVQEQQTSQM KLIHERQSKE
     MKANQAKSSM ENSKAISQDK SIKNKAERER RVRELNSSNT KKFLEERKRL AMKQAKEMEQ
     LQKSQREQLE KLEKFNEQLL KSHHSQTAGT LIPHSSLSPL IPLSTHPSLH SXQARDMQKM
     VKLEEDMERR PATVV
//