ID   M7ANH5_CHEMY            Unreviewed;      1197 AA.
AC   M7ANH5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   29-OCT-2014, entry version 15.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
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   Testudines + Archosauria group; Testudines; Cryptodira; Chelonioidea;
OC   Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP26786.1};
RN   [1] {ECO:0000313|EMBL:EMP26786.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang G., Huang Z., Wang Z.;
RT   "Development and evolution of a turtle-specific body plan assessed by
RT   genome-wide analyses.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol. {ECO:0000256|RuleBase:RU361133}.
CC   -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000256|RuleBase:RU361133}.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC       {ECO:0000256|RuleBase:RU361133}.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC       {ECO:0000256|RuleBase:RU361133}.
CC   -!- SIMILARITY: Contains C2 domain. {ECO:0000256|SAAS:SAAS00128627}.
CC   -!- SIMILARITY: Contains Cdomain. {ECO:0000256|SAAS:SAAS00128627}.
CC   -!- SIMILARITY: Contains PI-PLC X-box domain.
CC       {ECO:0000256|SAAS:SAAS00037385}.
CC   -!- SIMILARITY: Contains PI-PLC Y-box domain.
CC       {ECO:0000256|SAAS:SAAS00128585}.
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DR   EMBL; KB576442; EMP26786.1; -; Genomic_DNA.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.10; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   Gene3D; 3.20.20.190; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR028403; PLC-beta2.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLipase_C_EF-hand-like.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336; PTHR10336; 1.
DR   PANTHER; PTHR10336:SF10; PTHR10336:SF10; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; EF-hand_like; 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; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW   Transducer {ECO:0000256|SAAS:SAAS00128599}.
FT   ACT_SITE    325    325       {ECO:0000256|PIRSR:PIRSR000956-1}.
FT   ACT_SITE    372    372       {ECO:0000256|PIRSR:PIRSR000956-1}.
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
//