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
//