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Database: UniProt
Entry: A0A3Q4IE65_NEOBR
LinkDB: A0A3Q4IE65_NEOBR
Original site: A0A3Q4IE65_NEOBR 
ID   A0A3Q4IE65_NEOBR        Unreviewed;       982 AA.
AC   A0A3Q4IE65;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   Name=PLCH1 {ECO:0000313|Ensembl:ENSNBRP00000029772.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000029772.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000029772.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00001913};
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DR   AlphaFoldDB; A0A3Q4IE65; -.
DR   STRING; 32507.ENSNBRP00000029772; -.
DR   Ensembl; ENSNBRT00000030535.1; ENSNBRP00000029772.1; ENSNBRG00000022647.1.
DR   GeneTree; ENSGT00940000157185; -.
DR   OMA; QVVESHI; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000022647; Expressed in brain and 1 other cell type or tissue.
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; cd13364; PH_PLC_eta; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
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; IPR001849; PH_domain.
DR   InterPro; IPR001192; PI-PLC_fam.
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:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-1; 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; PF09279; EF-hand_like; 1.
DR   Pfam; PF16457; PH_12; 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; SM00233; PH; 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; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          76..110
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          112..147
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          148..184
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          570..682
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          684..812
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          533..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   982 AA;  110842 MW;  BAA631EBBBBBAB48 CRC64;
     MSVMQSGTQM VKLKAGSKGL VRLFYLDEHR SCIRWKPSRK SEKAKITIDS LYKVTEGGQS
     DIFHRHADGT FDPACCFTVY HGNHMESLDL VTSNAEEART WITGLRYLMA GISDEDSLQT
     FEEADKNGDG LLNIDEIYQL LHKLNVNLPR RKVKQMFQEA DTDDHQGTLT YEEFSVFYKM
     MSLRRDLYLL MMAYSDRKDH LTAEELVNFL HNEQKMTNVT PEYVAEIIDK FEVSEENKQQ
     CVMGIEGFTN FMRCPTCDIF NPLHHEVNQD MDQPLCNYFI ASSHNTYLTG DQLLSHSKTD
     MYAWVLQSGC RCVEVDCWDG PEGEPMVQHG YTLTSKIPFK SVIETINKYA FINNQYPVIL
     SIENHCSIQQ QKKIAQYLRE IFADKLDIGD VLSGDCKTLP SPHSLQGKIL IKGKRLPAYL
     SADAEEGEVS DDDSADEIED DFKLKSSNGN GHHQVVESHI RKKLDSLLKE SRIGDKEDTD
     SFSIRALLRA THQGLQKNLR QVKPQGEVSV IVCLFTYLCL FTIQRHSKSR LTCQSMDKEE
     DGQERSGREA GGQFNRCGRK RKTMKLSRDL SNLVVFTNSV ASQECLNEGT AGDVLSFSET
     RAQSLVNHRT EEFLAFNQRQ LSRIYPSAYR IDSSNFNPQF YWNVGCQLVA LNYQTEGRMM
     QLNRAKFMVN GGIGYVLKPP PMCKGTFNPF SDDPLPAYPK KQLILKIISG QQLPKPPDSM
     LGDRGEIIDP FVEVEIIGLP VDCCKEQTRV VDDNGFNPVW EETLTFTLHM AEVALVRFLV
     WDHDPIGRDF IGQRTVAFTS LMPGYRHVYL EGLTEASIFV HMSVHDVYGK WSPLVLNPSF
     TIMHFLGSNK SNQLRGIRGF FNRSSKSSVD TNSSGPRKRS ISDHLLRRTA SAPAKGRKKT
     KMMLSESVAS ISDQKNGTGA AAAGGEGVSG KEGGMEKRLQ PRAPLIHRPI SMPLDRLLQG
     QLSICSPDKE QHDMGADTII GG
//
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