ID A0A0K3AS74_CAEEL Unreviewed; 1346 AA.
AC A0A0K3AS74;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN Name=egl-8 {ECO:0000313|EMBL:CTQ86719.1,
GN ECO:0000313|WormBase:B0348.4j};
GN ORFNames=B0348.4 {ECO:0000313|WormBase:B0348.4j}, CELE_B0348.4
GN {ECO:0000313|EMBL:CTQ86719.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CTQ86719.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CTQ86719.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86719.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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-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|PIRNR:PIRNR000956,
CC ECO:0000256|RuleBase:RU361133};
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 EMBL; BX284605; CTQ86719.1; -; Genomic_DNA.
DR RefSeq; NP_001300020.1; NM_001313091.1.
DR SMR; A0A0K3AS74; -.
DR EnsemblMetazoa; B0348.4j.1; B0348.4j.1; WBGene00001177.
DR GeneID; 178537; -.
DR AGR; WB:WBGene00001177; -.
DR WormBase; B0348.4j; CE50563; WBGene00001177; egl-8.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001177; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; A0A0K3AS74; baseline and differential.
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; cd16200; EFh_PI-PLCbeta; 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; 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:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 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 PIRSF; PIRSF000956; PLC-beta; 2.
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 1: Evidence at protein level;
KW Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000956};
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 Proteomics identification {ECO:0007829|EPD:A0A0K3AS74,
KW ECO:0007829|PeptideAtlas:A0A0K3AS74};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 673..789
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 792..917
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 510..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1346 AA; 152896 MW; 773F2B80C0832269 CRC64;
MAKEFQFNWK PTIIPELLHG SVFDRYDDES TCLELNAQVR IDENGFFLRW LIEGKDAVVL
DMGQIWEART GGLPKDGRIM FELEQRGASE TIAERTIWIT HGQDLVNVQS FFLVAESVEL
AKTCRAGIND ILKSSRIRHV CPTTQLMKYH TWLTMNVNER RKIPIKLIIK TFSSGKPEKM
VQKCLNDLGL GGDKYTPARV INRSMGKKFR NFYKCSRGRK RKEREELDVD ILTFEKFQRL
YNKICPRTEV QELFVKLSGQ KEYLTKERLI NFLNEEQRDP RLNEILFPFF DSQRIVALLK
KHENDIKYQE DGKMSGDGFL RFLMSDENPP VFLDRIEMFM DMDQPLCHYY INSSHNTYLT
GRQYGGKSSS EIYRQVLLSG CRCIELDCWD GTGENKGEPI ITHGKAMCTD VFFKDVLVQI
RDTAFARSDF PVVLSFENHC SKSNQLKMAK YCMDIFGDML LSKPFEDAPL DPGVSLPSPN
RLRKKILIKN KRLKTDIERH QLDQFLREGK LDEEDELNET PEVVGEDSVS PREMPAKEND
EAHPELKQNF IAKNLKGFGF SKKQPDSSTS LLTASPTPSS SSMAMSNANN PFSSSTLNSP
QPMERSRSEK RSFRQKKGGV FGDELHSDSA ALIDFMRTAS SRKKKPVLTK EEEERIFAEY
HYTGATTNIH PLLSSLVNYT HPVKFSGFDV AEANNLHFHM SSFSESTGLG YLKQSAPEFV
NYNKRQSSRI YPKGARVDSS NFLPQIFWNA GCQMVSLNFQ TPDVYMQLNM GKFEYNGGSG
YLLKPDFLRR PDRTFDPFSE SPVDGVIAAH CSVRVISGQF LSDRKIGTYV EVEMYGLPTD
TIRKEHKTKV IPGNGLNPVY NEDPFVFRKV VLPELAVLRF AVYDENGKQL GQRILPLDGL
QAGYRHISLR SDTNQSFILS PVLFVQIVIK TYVPDELSGL VDALADPRAF LSEQKKRQEA
LAHMGVDDSD IPDVPNTRNM ALRHVKQPPR QNGSSADLLA NNGQTGSARG DQTSSMASST
IRSPNEQPQP VAVDKFKVDP IEVDDLRRDK AFAKLLKRFQ KELDDLRKKH QKQRDSIQKQ
QPARRRNSSI AWIQTNVDKL ITNNRRSTKK EKGSRRSLTA SVSSGCGSAS GTVTVSVCSP
SGASCSGYST GGPSTPVACN SDGTGSPATI GSPVPQDLVN NDRVRSLVNT QTGEWSAMVR
RHDEEEFELK KVQLKEQFDL LRKLMSEAQK NQMLALKLRL EAEGKDLKQT QTKKSMEDAK
VIQLDKGIKT KAERDRRVKE LNEKNLKMFV EERKRLAMKA QKHEEQLTKR HLDQLEQLDK
DFHKALDAEV GNYKEEQLAA QPTSVV
//
