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Database: UniProt
Entry: A0A3Q3RXY4_9TELE
LinkDB: A0A3Q3RXY4_9TELE
Original site: A0A3Q3RXY4_9TELE 
ID   A0A3Q3RXY4_9TELE        Unreviewed;      1259 AA.
AC   A0A3Q3RXY4;
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=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE            EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000012995.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000012995.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC       by activated phosphatidylinositol-specific phospholipase C enzymes.
CC       {ECO:0000256|PIRNR:PIRNR000956}.
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   AlphaFoldDB; A0A3Q3RXY4; -.
DR   STRING; 205130.ENSMAMP00000012995; -.
DR   Ensembl; ENSMAMT00000013347.2; ENSMAMP00000012995.1; ENSMAMG00000008785.2.
DR   GeneTree; ENSGT00940000160539; -.
DR   InParanoid; A0A3Q3RXY4; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
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; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08591; PI-PLCc_beta; 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   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 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; IPR014815; PLC-beta_C.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR037862; PLC-beta_PH.
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:SF11; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-3; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF06631; DUF1154; 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   Pfam; PF08703; PLC-beta_C; 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; SSF69989; C-terminal domain of PLC-beta; 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.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000956, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR000956,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW   ECO:0000256|RuleBase:RU361133};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT   DOMAIN          567..683
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          686..810
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          466..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1191..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          933..960
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1007..1114
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        516..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         362
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         413
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ   SEQUENCE   1259 AA;  143637 MW;  5CA7312EE0FCFFE3 CRC64;
     MAGAKPGVHA LQLKPVSVHE ALKSGGKFIK WDEEPSSGNP TQVTLKVDPG GFFLYWNVGS
     GQEVEVLDIS TIRDTRIGKY AKQPKDPKVR EIVSGKGDNG EGKLVSIVHG NDLVNISFLN
     LYATQEDTAK FFTDELFTLA TNILSQNASR NTFLLKAYTK LKLQVSQDGK IPVKNILKMF
     SDKKRVETAL EQCGLVNNRS EGIKPDDFTW EAFQKFLDNL CLRPEIQSIF EESGSKRKPF
     ISLDQLTDFI NRKQRDSRLN EVLYPPLKRE QVRLIMEKYE TNTSQLERDQ ISLQAFSRYL
     GGEENGIVPP ERLDVLDDMN QPLSHYFINS SHNTYLTVGQ LTGLSSVEMY RQVLLTGCRC
     IELDCWKGRP TDEEPYITHG FTMTTEISFK EVIEAIAESA FKTSPYPVIL SFENHVDSAK
     QQAKMAEYCR TIFGDALLID PLDKYPLVPG QPLPSPQELM GKILIKNKKK HHHHRPSSGG
     SIRRRELGEQ SSPNNECLLA ESEGSQLLSN GEEKLAERMV KDSGPRKSIG GEGESEEEEE
     DEPVPELKKP NTDEGTASSE VNATEEMSTL VNYIEPVKFK SFEVATKRKK YFEMSSFVET
     KGMDTLKSSP IEFVEYNKNQ LSRIYPKGTR VDSSNYMPQL FWNVGCQMVA LNFQTLDLPM
     QLNMGVFEYN GRSGYLLKPE FMRRTDKHFD PFTENIVDGI VANTIKIRVI SGQFLTDKKV
     GVYVEVDIFG LPVDTKRKYR TKTSNGNSLD PVWDDEMFVF NKIVLPTLAS LRIAVFEENG
     KFIGHRILPV SAIRPGYHYI NLKNELNQPL LLPSLLVYTE AQDYIPNEHQ EYAEALTNPI
     KHISQLDKRE TQLAVLIEDN SEHVPIQPKE GDTKKENEVI PGGRLPPTFY NVPPCPMDES
     PDIIKLPAPA PSQKEDLIAT VLTDVQVHSV EELRQQKSYL KLLKKQSQEL KELRKKHLKK
     VWNLSKEQKN RSSQLQSDSK RRRSQMEKHL KRSIKKNEPQ EPVERELTAL NQELEKQTVQ
     LREWQMQELL KLRQELHSLE REKKKAHLLE ALEKLKDTAH ECQTAQLKKL RETCEKEKKE
     LQKILDRKRQ NSITEAKTRE KEKAETELNE INRKHIQDSV ASIRRLEEAQ SRRQDKLILR
     HREVVQHIDE ELPMLQSQLE KELEEEYQRL PEEICQHLQV ELQNKGLGKD ALFSPFSNHS
     SPSPSSGSGP PSNCSTPSNP STPNRSTWNR SMDNSITSLA DSSSSSTTPV LSEPEMSFS
//
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