ID G7PAX0_MACFA Unreviewed; 1043 AA.
AC G7PAX0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=EGM_15857 {ECO:0000313|EMBL:EHH62979.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH62979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH62979.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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; CM001282; EHH62979.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PAX0; -.
DR eggNOG; KOG1265; Eukaryota.
DR Proteomes; UP000009130; Chromosome 7.
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; 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; 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; 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; 2.
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|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 542..658
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 658..793
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 460..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 875..911
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 938..1002
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 462..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..517
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 374
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 328
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 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1043 AA; 118885 MW; B9EF6324C01CF0E4 CRC64;
MSLLNPVLLP PRVKAYLSQG ERFIKWDDET TIASPVILRV DPKGYYLYWT YQSKEMEFLD
ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE
NVGKVWAEDI LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR
VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE INEIFTSYHA KAKPYMTKEH
LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN
SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC
WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM
AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSSP TSSSKDPGGE
AEGSSPRSAP AVWAGEEGTE LEDEEVEEEE EEESGNLDEE EIKKMQSDEG TAGLEVMAYE
EMSSLVNYIQ PTKFISFEFS AQKNRSYVIS SFTELKAYDL LSKASVQFVD YNKRQMSRIY
PKGTRMDSSN YMPQMFWNAG CQMVALNFQT MDLPMQQNMA VFEFNGQSGY LLKHEFMRRP
DKQFNPFSVD RIDVVVATTL SITARPWDRQ VISGQFLSER SVRTYVEVEL FGLPGDPKRR
YRTKLSPSTN SINPVWKEEP FVFEKILVPE LASLRVAVME EGNKFLGHRI IPINALNSGY
HHLCLHSESN MPLTMPALFV FLEMKDYVPG AWADLTVALA NPIKFFSAHD KRSVKLKDIM
GGLPEKPFPL ASPVASQVNG ALAPRSNGSP QISKMMELAR EKQAAELKAL KETAEIDTKE
MKKKLETKRL ERIQGMTKVT ADKMAQERLK REINSSHIQE VVQVIKQMTE NLEKHQEKLE
EKQAACLEQI REMEKQFQKE ALAEYEARMK GLEAEVKESV RACFRTCFPS ETKDKPERDC
ECPPELCEQD PVVAKTDVQE SRL
//
