ID Q5CR08_CRYPI Unreviewed; 883 AA.
AC Q5CR08;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=cgd4_2560 {ECO:0000313|EMBL:EAK87844.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK87844.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK87844.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAK87844.1}.
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DR EMBL; AAEE01000008; EAK87844.1; -; Genomic_DNA.
DR RefSeq; XP_625844.1; XM_625844.1.
DR AlphaFoldDB; Q5CR08; -.
DR STRING; 353152.Q5CR08; -.
DR EnsemblProtists; EAK87844; EAK87844; cgd4_2560.
DR GeneID; 3372851; -.
DR KEGG; cpv:cgd4_2560; -.
DR VEuPathDB; CryptoDB:cgd4_2560; -.
DR InParanoid; Q5CR08; -.
DR OMA; HWQREMS; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000006726; Chromosome 4.
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: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; cd15898; EFh_PI-PLC; 1.
DR CDD; cd08558; PI-PLCc_eukaryota; 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; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
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; PF13499; EF-hand_7; 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; SM00054; EFh; 2.
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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000006726};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 210..245
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 246..281
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 586..681
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 691..829
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 883 AA; 100509 MW; F5EE00A722B8C342 CRC64;
MFRPLLDCNG EISINRLLGS QDLSEYVISV RTFEDVVNKL NIVVSDRLMQ LLHEVDVDIA
LDTCKSGSYL YKYPRSCIGS RRFSRYNFEI DLDSGCVKWY KKKKTLICSR KVVFIQTLYL
NDVNHILPGS DSDFWRSKKC TKKEYINSNF GIELVVIGKR NKTLRLLCAN KEEWKFWMVG
LLVSHALAQR EKLVSKIKGT KKIVDAKHFY THDYIRRQWE LSDLDNSGSI SFTELMRLTK
RLQMPVSKDY THALFCEYDN DNNGALDYKE FRNLLTQLLI LPELRDLFDE YKDPDTNVMG
ANKFRNFLID VQGMDPSNSL ESLVNAVLNM KEPFIERGGI TEIGFNILMS SEFNSAFDPL
KRDVYQSMDE PISHYWIASS HNTYLTGDQL TSKSEIGQYI TVLLQGCRCV ELDVWNGPDG
SPIIYHGHTL TSKVYFEDVI RACKDYAFQI SPYPIILSLE MHASDKQREK VAEIILNVLG
DSLYIPPNDG SDRLPTPNEL KYKFLVKAKV PKEDISFDLR AGVINEDDEK NDLNPDILEV
DLEVSNNTRI ENEKQASSYN QNQTKRRLYS SLISLPGNAI QLSNFENRRR MSIGSLVETK
FLRLAKDSSM SLAKFHQDHL CRVYPSGTRI SSSNYNPLIP WSYGAQIVAL NYQAVGTALL
LNEGRFRQNG GSKSGYVLKP KMCLKKCFDG RVFDPMNPLE TLELFDIPPV RVCIQILSAH
QLPDNLSQFS RGIAGLISGN KLSPYITISV FGGPSEEFKS YRTPVINNNG FNPKWENLSP
FTFNVLCPEI SIINFEVKSS DSIQSEFIAA ASIPVSCLRP GLRWIQLFDA NFIDIQCCGI
LANISITTEL PKTYMLSSIL TGNNGSSSTN LQETLQQFRG IKF
//
