ID A0CKY8_PARTE Unreviewed; 773 AA.
AC A0CKY8;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN ORFNames=GSPATT00008002001 {ECO:0000313|EMBL:CAK71455.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK71455.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK71455.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK71455.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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|RuleBase:RU361133};
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DR EMBL; CT868097; CAK71455.1; -; Genomic_DNA.
DR RefSeq; XP_001438852.1; XM_001438815.1.
DR AlphaFoldDB; A0CKY8; -.
DR STRING; 5888.A0CKY8; -.
DR EnsemblProtists; CAK71455; CAK71455; GSPATT00008002001.
DR GeneID; 5024637; -.
DR KEGG; ptm:GSPATT00008002001; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_1_2_1; -.
DR InParanoid; A0CKY8; -.
DR OMA; SSYRRCT; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd08558; PI-PLCc_eukaryota; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 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; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 133..168
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 523..627
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 628..755
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 773 AA; 90791 MW; 7851B5CD3D32D14C CRC64;
MNYSTVLSKK PFPPQKQDQA INLLVYGCEI QKITSGNKFE KLFIYMSHEV SYQLIYIINQ
YTNYIDLRKI RFITDDIRDS KKFTDDKSVL LQIFVSEECW YLKFANQTLK ELWWQGLQYF
YTKVKEDLKE KLQIQLMAWE MFIKFDEDRD GSLNKEEQQG FLNWIKLVYP NKSFIENKCI
QSSFQNKLEF MQFEEIVRLL YKQSILIKLN KLYLNSQNLL IEADFEKFIR TAQRQQDTDY
FFGFPMTADK FNDFLFSQQN SIFEMGHSDD MTKPLSHYYI NSSHNTYLTK DQLAGDSSVG
QYVIALLNGC RCFELDCWDS ISDRNPVVYH GYTLTSKILF EDAILALDKF GFMFSSYPII
LSLELHCSID QQEVLGQIMR AQFKDELYIY EQNLSVLPSL DKLKRKFLIK SSGILEESYS
LHKNNQEIHK TMQSQKIVKT QKTLELIQVD QDPEPGLVRE IAQKQRISNK TLKNLNYENK
QKQFIRHDAI CDFKMIGDQI DLVIPVSMNV KHHPQFLSCI SLFNSPFEIN KKRSIWNISS
LSEDKVDKIF KEKKVKEVQQ HLNNYLVRIY PSGMRVDSSN FDPIPSFILG AQIIALNFQT
KDEPMLINRA RFSQNLGIGY VLKPKYLIEG LDQVTNFESP DYPKKLVTLE IISCQLFLLH
TKNVINPQVI VKLKGNKVDE NGQELQTNVI YNNGLNPEFD QNYSKTTFEV KDVDQAIFIF
KVFNKSDDNK QTIIGQYALP FKNMREGFRA IPLKDENLMV MEYCYIFAQV TIQ
//
