ID K7FQ96_PELSI Unreviewed; 1073 AA.
AC K7FQ96;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=PLCB1 {ECO:0000313|Ensembl:ENSPSIP00000010206.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000010206.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000010206.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGCU01171819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FQ96; -.
DR STRING; 13735.ENSPSIP00000010206; -.
DR Ensembl; ENSPSIT00000010258.1; ENSPSIP00000010206.1; ENSPSIG00000008760.1.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000155428; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR OMA; GKVNHKP; -.
DR TreeFam; TF313216; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0005521; F:lamin binding; IEA:Ensembl.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:AgBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:2000438; P:negative regulation of monocyte extravasation; IEA:Ensembl.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:Ensembl.
DR GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
DR GO; GO:2000560; P:positive regulation of CD24 production; IEA:Ensembl.
DR GO; GO:0048639; P:positive regulation of developmental growth; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0080154; P:regulation of fertilization; IEA:Ensembl.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IEA:Ensembl.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16208; EFh_PI-PLCbeta1; 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; IPR028400; PLC-beta1_EF.
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:SF12; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-1; 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|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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 461..577
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 577..705
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 387..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..942
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 400..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1073 AA; 122877 MW; F421A3A611F63552 CRC64;
QDPKLREQLD AGNIGGRLEN RMITVVYGPD LVNISYLNLV AFQEEIAKEW TDEVFSLATN
LLAHNMSRDA FLEKAYTKLK LQVTHEGRIP LKSIYRLFSA DRKRVETALE ACNLPSARND
SIPQEDFTPE AYRVFLNNLC PRPEIDNIFS EFGAKSRPYL AVDQMMEFIN YKQRDPRLNE
ILYPPMKQEQ VQQLIEKYEP NNSLAKKGQI SVDGFMRYLS GEENGVVPPE KLDLNEDMSQ
PLSHYFINSS HNTYLTAGQL AGSSSVEMYR QVLLSGCRCV ELDCWKGRTA EEEPVITHGF
TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMDP
LEKYPLESGV PLPSPMDLMH KILVKNKKKS QKSADGSSKK KVAEQASNTC SDASSGFEPS
SPGAGEAEIE SDDDDDDDDD CKKSSMDEGT AGREAMATEE MSNLVNYVQP VKFESFEISN
KRNKSFEMSS FVETKGLEQL TKSPVEFVEY NKRQLSRIYP KGTRVDSSNY MPQVFWNAGC
QLVALNFQTV DLSMQINMGM YEYNGKSGYR LKPEFMRRPD KHFDPFTESI VDGIVANTLS
VKIISGQFLS EKKIGTYVEV DMFGLPVDTR RKALKTKTSQ GNAINPVWEE EPIVFKKVVL
PSLACLRIAV YEEGGKFIGH RILPVSAIRP GYHYICLRNE RNQPLMLPAV FVYIDVKDYV
PDTYADVIEA LSNPIRYVNL MEQRAKQLAA LTLEDEEEVK KEAEQGDPPS EANHEPRPTP
AENGLSHSTS LTTKPATQVV HSQPAPGSVK APAKTEDLIQ SVLTEVEAQT IEELKQQKSF
VKLQKKHYKE MKDLVKRHHK KTTDLIKEHT AKYNEIQNDY LRRRAVLEKS TKRDSKKRCE
TGSPDHSSTI EQELAALDSE MTQKLIELKE KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ
KLTDVAEECQ SSQLKKLKET CEKEKKELKK KMDKKRQEKI TEAKTKDKNQ MDEEKTEMIR
SYIQEVVQYI KRLEDAQSKR QEKLVEKHKE IRQQILDEKP KSIEEQEVEE QKK
//
