ID   Q59F77_HUMAN            Unreviewed;       901 AA.
AC   Q59F77;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 140.
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};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92820.1};
RN   [1] {ECO:0000313|EMBL:BAD92820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAD92820.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AB209583; BAD92820.1; -; mRNA.
DR   RefSeq; NP_001271226.1; NM_001284297.1.
DR   RefSeq; NP_001271227.1; NM_001284298.1.
DR   RefSeq; NP_004564.2; NM_004573.2.
DR   AlphaFoldDB; Q59F77; -.
DR   PeptideAtlas; Q59F77; -.
DR   DNASU; 5330; -.
DR   GeneID; 5330; -.
DR   KEGG; hsa:5330; -.
DR   PharmGKB; PA33385; -.
DR   OrthoDB; 2900494at2759; -.
DR   BioGRID-ORCS; 5330; 15 hits in 1160 CRISPR screens.
DR   GenomeRNAi; 5330; -.
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   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; 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   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; 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.
DR   Genevisible; Q59F77; HS.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
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   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          553..669
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          669..797
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          467..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..528
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         366
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         415
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92820.1"
SQ   SEQUENCE   901 AA;  101751 MW;  8BFD658D0FA74529 CRC64;
     QRGTLGTMSL LNPVLLPPKV KAYLSQGERF IKWDDETTVA SPVILRVDPK GYYLYWTYQS
     KEMEFLDITS IRDTRFGKFA KMPKSQKLRD VFNMDFPDNS FLLKTLTVVS GPDMVDLTFH
     NFVSYKENVG KAWAEDVLAL VKHPLTANAS RSTFLDKILV KLKMQLNSEG KIPVKNFFQM
     FPADRKRVEA ALSACHLPKG KNDAINPEDF PEPVYKSFLM SLCPRPEIDE IFTSYHAKAK
     PYMTKEHLTK FINQKQRDSR LNSLLFPPAR PDQVQGLIDK YEPSGINAQR GQLSPEGMVW
     FLCGPENSVL AQDKLLLHHD MTQPLNHYFI NSSHNTYLTA GQFSGLSSAE MYRQVLLSGC
     RCVELDCWKG KPPDEEPIIT HGFTMTTDIF FKEAIEAIAE SAFKTSPYPI ILSFENHVDS
     PRQQAKMAEY CRTIFGDMLL TEPLEKFPLK PGVPLPSPED LRGKILIKNK KNQFSGPTSS
     SKDTGGEAEG SSPPSAPAGE GTVWAGEEGT ELEEEEVEEE EEEESGNLDE EEIKKMQSDE
     GTAGLEVTAY EEMSSLVNYI QPTKFVSFEF SAQKNRSYVI SSFTELKAYD LLSKASVQFV
     DYNKRQMSRI YPKGTRMDSS NYMPQMFWNA GCQMVALNFQ TMDLPMQQNM AVFEFNGQSG
     YLLKHEFMRR PDKQFNPFSV DRIDVVVATT LSITVISGQF LSERSVRTYV EVELFGLPGD
     PKRRYRTKLS PSTNSINPVW KEEPFVFEKI LMPELASLRV AVMEEGNKFL GHRIIPINAL
     NSGYHHLCLH SESNMPLTMP ALFIFLEMKD YIPGAWADLT VALANPIKFF SAHDTKSVKL
     KEAMGGLPEK PFPLASPVAS QVNGALAPTS NGSPGMSFGP HTYWGHLHLC THRHFPLKNF
     T
//