ID A0A8M9PW40_DANRE Unreviewed; 1275 AA. AC A0A8M9PW40; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 14-DEC-2022, entry version 3. 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 (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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; cd13361; PH_PLC_beta; 1. DR Gene3D; 1.20.1230.10; -; 1. DR Gene3D; 2.60.40.150; -; 1. DR Gene3D; 3.20.20.190; -; 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; 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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. PE 4: Predicted; 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 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" 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 //