ID A0A3Q3FLD3_9LABR Unreviewed; 1569 AA.
AC A0A3Q3FLD3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000021286.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000021286.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSLBET00000022424.1; ENSLBEP00000021286.1; ENSLBEG00000016344.1.
DR GeneTree; ENSGT00940000158374; -.
DR Proteomes; UP000261660; Unplaced.
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; 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:UP000261660};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 57..165
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 179..214
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 215..251
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 645..758
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 759..888
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 483..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1569 AA; 174343 MW; EC05F113C3402A53 CRC64;
MESVAARMAM VTDSPNPSLR SRATVTSDGD SFVSTASLPC NHFLSANVIN VVEKCMSSMQ
SGTQMVKLRG GSKGLVRFFF LDEHKSCIRW RPSRKNEKAK ISIDSIREVC EGKQSEIFQR
YAEGSFDPNC CFSLYYGEHM ESLDLVSGTG EEARTWITGL KYLMAGISDE DSLAKRQRTR
DQWLKQTFTE ADKNGDGSLS IGEVLQLLHK LNVNLPRQKV KQMFKEADTD DNQGTLGFEE
FCSFYKMMST RRDLYLLMLT YSNHKDHLDV DDLVRFMETE QKMTKVSKEH CLEIINKFEP
CSENQKQGVL GIDGLTNYTR SPEGDIFNPA HYEVNQDMNQ PLCNYFIASS HNTYLMGDQL
MSQSRVDMYA WVLQAGCRCV EVDCWDGQDG EPIVHHGYTL TSKILFKDVI ETINKYAFVK
NDYPVILSIE NHCSVPQQKK MAQYLIEILG DKLDVSNIKA EESGRLPSPD LLKGKILVKG
KKLPPNIDED AEEGDVSDED SADEMEDDCK LMNGDTSANR KQVENMAKKK LDNLMKESKI
RDREDPDSFT IAALPPAGKA TDKTSSKGKS EDGTDTADES NPSCNKRTGR SFIGSFSKRK
KKTTKLKKTS SFEDTDTDQE STSSASRAPL HHSKKKKTMK LSRALSDLVK YTCSVGLYDI
EAQANCSWQV SSLSETKAHQ VMQQKATSFI QFNQKQLSRI YPSSYRVDSS NFNPQPFWSA
GCQLVALNYQ SEGRVLQLNR AKFYSNGNCG YILKPACMCE GAFNPSLEDP LPGQMKKQLV
LKIISGQQLP KPKDSMLGDR GEIIDPFVEV EVIGLPIDCC KEQTRVVDDN GFNPMWEETL
VFTVHMPELA LVRFLVWDHD PIGQDFIGQR TIAFNSMMPG YRHVYLEGME EASIFVHVAV
NDITGKARAV SGIKGLFHRN PKQASLDSHA AAQHSRKHPF GAHLLRRTAS APTKGQPKIK
KGFPEIDTKD YSSEGASEER ESEDRDKASA AASHQTTTPQ HRSRDSLASH QAKGPWDRPD
TNGAFHPEEG KDSSSVQEPA PSPPFLALNS EEARKPRFIR SVSTPEESLS PHHSSSSPPS
SSSSAIKSDS PLALPSNGVA DKVIRDFKEP SILSRTTDSP LKNPTEKTVP SQCSQEAQAN
RSPPSLMEHT QNQSEDREAL TEKKNDPAEL KSSSRTEPPA AAAKTAQARR ALFSNLPTHI
PVRRTKSEGQ VLVAVASDHQ VQSAVPEVCM DATMNDRLWS KLEPDSHRDS MSSSSSISSS
DTVIDLSLPN LARKSLPAAA SGAFDPPWVN CRHSALVSYD TLRVSKSKSN PNLQQSECDE
DELKPRPLQP PQEASLDSPG RLTQRRHTWS RLYMEGLKQS ASSRPSTAAA AVQTSAASMS
KSLGDLTSDD ISCNFDSKYR SISRSFIVRP ARDQLRRGSP RKPRPPSDLT EQLRRLTDVE
PLTASDFNKT RAAEPQEEPE EETLVRRTSS RSQSRVRYIA NRAKKAQERQ RLQGLVQGRS
ASFSLSGSGS VGSPIEERGN PEGACCVARS PCSSQDLLSQ LAPHDAPSPR QSHSSPDPEN
SEVFFMLKL
//
