ID M7ANH5_CHEMY Unreviewed; 1197 AA. AC M7ANH5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 02-OCT-2024, entry version 66. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956}; DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956}; GN ORFNames=UY3_16186 {ECO:0000313|EMBL:EMP26786.1}; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira; OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP26786.1, ECO:0000313|Proteomes:UP000031443}; RN [1] {ECO:0000313|Proteomes:UP000031443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23624526; DOI=10.1038/ng.2615; RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C., RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y., RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J., RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S., RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.; RT "The draft genomes of soft-shell turtle and green sea turtle yield insights RT into the development and evolution of the turtle-specific body plan."; RL Nat. Genet. 45:701-706(2013). 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}; 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 EMBL; KB576442; EMP26786.1; -; Genomic_DNA. DR AlphaFoldDB; M7ANH5; -. DR STRING; 8469.M7ANH5; -. DR eggNOG; KOG1204; Eukaryota. DR eggNOG; KOG1265; Eukaryota. DR Proteomes; UP000031443; 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; cd16209; EFh_PI-PLCbeta2; 1. DR CDD; cd13361; PH_PLC_beta; 1. DR CDD; cd08624; PI-PLCc_beta2; 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; IPR028403; PLC-beta2_cat. DR InterPro; IPR014815; PLC-beta_C. DR InterPro; IPR042531; PLC-beta_C_sf. DR InterPro; IPR037862; PLC-beta_PH. DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl. DR InterPro; IPR053945; PLCB1-4-like_EFh. DR InterPro; IPR046969; PLCbeta2_EF. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y. DR PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF17787; PH_14; 1. DR Pfam; PF00388; PI-PLC-X; 1. DR Pfam; PF00387; PI-PLC-Y; 1. DR Pfam; PF08703; PLC-beta_C; 1. DR Pfam; PF22631; PLCB1-4-like_EFh; 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:UP000031443}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}. FT DOMAIN 537..653 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000259|PROSITE:PS50008" FT DOMAIN 647..772 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT REGION 460..491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..516 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1145..1169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 880..907 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1063..1127 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 460..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..511 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 325 FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1" FT ACT_SITE 372 FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1" FT BINDING 326 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 355 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 357 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 406 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" SQ SEQUENCE 1197 AA; 137129 MW; 33E299BA4930FFB2 CRC64; MFTSILTPPE VKEYLSKGER FIKWDDDTTN ASPVILRVDP KGFYLYWTYQ NKEMEFLDIT SIRDTRVGKF AKIPKSQKLR EVFNLDFPDN NFLLKTLTVV TGPDMVDLTF HNFVSYKESV GKSWAEDIMA IVRNPLTSNA SRYTFLEKIL VKLKMQLSAE GKIPVRNIFQ MFPADRKRVE AALHACHLPK GKNDAINPED FPEKVYKTFL MNLCPRPEID EIFTSLHSKA KPYMTKEHLA KFINKKQRDS RLNDMLFPPA KPEQVQGLIE KYEPSGINIQ RGQLSPEGMV WFLCGPENNI VSLDKVVLYQ DMTQPLSHYF INSSHNTYLT AGQFSGISSP EMYRQSLLSG CRCVELDCWK GRPPDEEPII THGFTMTTEI LFKDVIEAIA ESAFKTSLYP VILSFENHVD SPRQQAKMAE YCRTIFGDTL LTEPLEKYPL KPGVPLPSPQ DLLGKILIKN KKKQSASEER QDSLKKERNE TTDQPFTVDG IVWAGEVTEE DPEEEEEESG NLDEEQIKKM QSDEGTAGLE VTAYEEMSSL VNYIQPIKFD SFDISTEQNR SYVISSFTEM KAYDLLTKSP VQFVEYNKRQ MSRIYPKGTR MDSSNYLPQM FWNVGCQMVA LNFQTMDVPM QQNMALFEFN GQSGYLLKHE FMRRPDKQFD PFSVDRIDVI LSGQFLSERS VKSYVEVELF GLPGDPKRKY RTKLTSSANS LNPVWKEEAF VFEKIMMPEL ASLRIVALEE GGKFIGQRII PIIAVHSGYH HVCLRSESNM PLTMPSLFVY LEMKDYVPDT WADLTVALSN PIKFFNNQDK RSVKLKQGSA EKKLTAAQTN GIPNSTRTFS FHSSNGPAGA MALGKEETIK EVAKEVAELQ TASLEELQKM KLFMKLLKKQ EKELKELERK GSKRREELLQ RYSALFSELV TQCGRKKIAC PRKTQKKKSS LTVEEVIAGG NPAEMAENAD SRVLELKEKL EMHLMQLWEE QHDGIRKKKE QHATEQISRL IEVAREKQAA ELKALKESSE SDTKEIKKKL EAKRLDRIQA MTKSTIDKTA QERLKREINN SHIQEVVQMI KLVTEKMAKY QEKLEEKQAD CLEKIKEKES QLQKEALAEY EEKVKTLSME VQDLARNCVK ICFPLEANIK KEEALNASSE GKQGSKDQPE GKIPGAEISW LETSMAETSI AQTQKVELSE QNEESRL //