ID A0A093IXN6_EURHL Unreviewed; 1434 AA.
AC A0A093IXN6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
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;
GN ORFNames=N326_02281 {ECO:0000313|EMBL:KFW03504.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW03504.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW03504.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW03504.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK564565; KFW03504.1; -; Genomic_DNA.
DR Proteomes; UP000054232; Unassembled WGS sequence.
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; cd16221; EFh_PI-PLCeta2; 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; IPR046971; PLC-eta2_EFh.
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:SF166; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-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; 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; 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:UP000054232};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 155..190
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 191..227
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 619..732
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 733..862
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 463..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW03504.1"
FT NON_TER 1434
FT /evidence="ECO:0000313|EMBL:KFW03504.1"
SQ SEQUENCE 1434 AA; 160609 MW; B9FE0DB8CB0BA766 CRC64;
SVARLAEEFF WVGGSIVASP RWKIGHIVER CMTSMQAGTQ MIKLRGSSKG LVRFYYLDEH
KSCIRWRPSR KNEKAKISID SIQEVCEGKQ SEIFQRYADG SFDPNCCFSI YYGDHMESLD
LVSSSGDEAR TWITGLKYLM AGISDEDSLS KRQRTRDQYP SYTFDEADKN GDGSLSISEV
LQLMHKLNVN LPRQKVKQMF KEADTDDNQG TLGFDEFCAF YKMMSTRRDL YLLMLTYSNH
KDYLDTDDLR RFLETEQKMT NVTKEHCLEI VSKFEPCLEN KKEGALGIDG FTNYMRSPSG
DIFNPEHYQV NQDMSYPLSH YFITSSHNTY LMGDQLMSQS RVDMYAWVLQ SGCRCVEVDC
WDGPDGEPIV HHGYTLTSKI LFKDVIETIN KYAFIKNEYP VILSIENHCS VIQQKKMAQY
LLEILGDKLD LSSVHNDDST KLPSPESLKG KILVKGKKLP ANISDDAEEG EVSDEDSADE
IDDDCKLMNG DASSNRKRVE NIAKKKLDSL IKESKIRDCE DPNNFTVTTL PSSGKAALKS
ESKKDDVESG EDFSTSKRQS RSLMGSFSKR KKKGSKLKKA TSLEEGEDDL DSQGNLARSS
VHTSRMTRQK KTMKLSRALS DLVKYTKSVG IHDVEAEISS SWQVSSFSET KAHQILQQKP
AQYLRFNQHQ LSRIYPSSYR VDSSNYNPQP FWNAGCQLVA LNYQSEGRML QLNRAKFSAN
GNCGYVLKPN CMCQGVFNPN SEDPLPGQLK KQLVLRIISG QQLPKPRDSM LGDRGEIIDP
FVEVEVIGLP VDCFKEQTRV VDDNGFNPMW EETLVFTVHM PEIALIRFLV WDHDPIGRDF
IGQRTIAFSS MMPGYRHVYL EGIEEASIFV HVAINDICGK AKQALGLKGL FLRNPKQASL
DSHAAGQLHR KHSFSSHILR RTASAPTKSQ KKNKKGFPEI AFDTKDNSSE GAGEDREVEA
ASQPRFEQEP ESASLSPAPR DGASGVVHGK GLKDVCHFSI KRSVTSLCSL ETITEEPVIA
SENHHASLFF PLPITPYSQE DERTSTAGCV KEEDGWTQAC SKAEDPYGLA VHPQKAWLKV
AADKGAGQPA ENCQKQSDQP AAQALPVSVS QMSSYMLVRR SKSEGLKTSD SSALIRIPSS
LSPAAEVYFD ATVNDRIWSK LDCSSHRDSM SSSSSMSSND TVIDLSLPNL ARKSLPDLGI
RPENFEPLAV RKGMRPRSAT TSGNEMPLVS KSKSNPNLRS GQLPADELCP RPLARSPQDA
FSSIPRRHTW SRLYIESLRQ SSNKSKAQDM VGNNQAKSKS LGDLTSDDIV CTFESKYRSI
SRSFVTRSMR EQRRSSGLRS SVRSQDELTE QLKKLTAFQI SLDPTESEEE GESLGLLRRS
SSRSQSRVRY IANRAKQAQE RQRLQSLGQL SGSPIEERGN PEGACSVAKA VCMD
//
