ID M7ANH5_CHEMY Unreviewed; 1197 AA. AC M7ANH5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 10-MAY-2017, entry version 34. 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 Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia; OC 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., RA Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., RA Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., RA Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J., RA Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G., RA Irie N.; RT "The draft genomes of soft-shell turtle and green sea turtle yield RT insights into the development and evolution of the turtle-specific RT body plan."; RL Nat. Genet. 45:701-706(2013). 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 --------------------------------------------------------------------------- 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 Proteomes; UP000031443; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:GOC. 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; 2.60.40.150; -; 1. DR Gene3D; 3.20.20.190; -; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR001192; PI-PLC_fam. DR InterPro; IPR016280; PLC-beta. DR InterPro; IPR028403; PLC-beta2. DR InterPro; IPR014815; PLC-beta_C. DR InterPro; IPR009535; PLC-beta_CS. 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; PTHR10336; 1. DR PANTHER; PTHR10336:SF122; PTHR10336:SF122; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF06631; DUF1154; 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; SSF47473; SSF47473; 1. DR SUPFAM; SSF49562; SSF49562; 1. DR SUPFAM; SSF50729; SSF50729; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031443}; KW Hydrolase {ECO:0000256|RuleBase:RU361133}; KW Lipid degradation {ECO:0000256|RuleBase:RU361133}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361133}; KW Reference proteome {ECO:0000313|Proteomes:UP000031443}; KW Transducer {ECO:0000256|SAAS:SAAS00123199}. FT DOMAIN 310 461 PI-PLC X-box. {ECO:0000259|PROSITE: FT PS50007}. FT DOMAIN 537 653 PI-PLC Y-box. {ECO:0000259|PROSITE: FT PS50008}. FT DOMAIN 670 749 C2. {ECO:0000259|PROSITE:PS50004}. FT COILED 880 907 {ECO:0000256|SAM:Coils}. FT COILED 1063 1127 {ECO:0000256|SAM:Coils}. 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 //