ID   M7ANH5_CHEMY            Unreviewed;      1197 AA.
AC   M7ANH5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 64.
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};
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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; 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; 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; 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   Pfam; PF08703; PLC-beta_C; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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
//