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0PLCB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePLCB2
Description1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2 (ec 3.1.4.11) (phosphoinositide phospholipase c) (plc-beta-2) (phospholipase c-beta-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004435 phosphoinositide phospholipase C activity (TAS)
0007202 phospholipase C activation (TAS)
0006644 phospholipid metabolism (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Phosphoinositide-specific phospholipase C (PLC) mediates the cellular actions of avariety of hormones.eurotransmitters and growth factors . Agonist-dependent activation of PLC causes hydrolysis of membrane phosphatidylinositol4.-bisphosphate (PIP2).enerating the second messengers inositol 1..-trisphosphate(IP3) and diacylglycerol (DAG). IP3 binds specific intracellular receptors to triggerCa2+ mobilisation.hile DAG mediates activation of a family of protein kinase C isozymes.Based on molecular size.mmunoreactivity and amino acid sequence.everalsubtypes have been classified. Overall.equence identity between sub-types is low.et all isoforms share two conserved domains.esignated X and Y.In PLC-beta subtypes. and Y domains are separated by a stretch of 70-120 amino acidsrich in Ser.hr and acidic residues. Their C terminus is rich in basic residues. In PLC-gammas.here is an insert of more than 400 residues containing an SH3 and two SH2 domains. PLCs show little similarity in the 300-residue N-terminal region preceding the X-domain.This entry represents a PLC region found towards the C-terminus which contains the X and Y boxes and the Ca2+-dependent membrane-targeting module of these proteins.
  IPR001192:Phosphoinositide-specific phospholipase C, C-terminal (PLC)
InterPro domains unassigned to SynO:
Phosphatidylinositol-specific phospholipase C (). eukaryotic intracellular enzyme.lays an important role in signal transduction processes . It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins . In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC. All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as the X-box and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distancebetween these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd one SH3 domain are inserted between the two PLC-specific domains. The two conserved regions have been shown to be important for the catalytic activity. By profile analysis.e could show that sequences with significant similarity to the X-box domain occur also in prokaryotic and trypanosome PI-specific phospholipases C. Apart from this region.he prokaryotic enzymes show no similarity to their eukaryotic counterparts.
  IPR000909:Phosphatidylinositol-specific phospholipase C, X region
Phosphatidylinositol-specific phospholipase C ().n eukaryotic intracellular enzyme.lays an important role in signal transduction processes (see ). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins .In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as X-box (see ) and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distance between these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd one SH3 domain are inserted between the two PLC-specific domains. The two conserved regions have been shown to be important for the catalytic activity. At the C-terminal of the Y-box.here is a C2 domain (see ) possibly involved in Ca-dependent membrane attachment.
  IPR001711:Phosphatidylinositol-specific phospholipase C, Y domain
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
This domain consists of a duplication of two EF-hand units.here each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain . These include: calbindin D9K.100 proteins such as calcyclin.olcalcin phl p 7 (a calcium-binding pollen allergen).steonectin.arvalbumin.almodulin family of proteins (troponin C.altractin.dc4p.yosin essential chain.alcineurin.ecoverin.eurocalcin).lasmodial-specific CaII-binding protein Cbp40.enta-EF-Hand proteins (sorcin.rancalcin.alpain).s well as multidomain proteins such as phosphoinositide-specific phospholipase C.ystrophin.b1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
  IPR011992:EF-Hand type
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
Phosphatidylinositol-specific phospholipase C ().n eukaryotic intracellular enzyme.lays an important role in signal transduction processes (see ). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3..-triphosphate into the second messenger molecules diacylglycerol and inositol-1..-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins .In mammals.here are at least 6 different isoforms of PI-PLC.hey differ in their domain structure.heir regulation.nd their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.All eukaryotic PI-PLCs contain two regions of homology.ometimes referred to as X-box (see ) and Y-box. The order of these two regions is always the same (NH2-X-Y-COOH).ut the spacing is variable. In most isoforms.he distance between these two regions is only 50-100 residues but in the gamma isoforms one PH domain.wo SH2 domains.nd one SH3 domain are inserted between the two PLC-specific domains. The two conserved regions have been shown to be important for the catalytic activity. At the C-terminal of the Y-box.here is a C2 domain (see ) possibly involved in Ca-dependent membrane attachment.This entry represents the X and Y box regions of phosphatidylinositol-specific phospholipase C.
  IPR013841:Phosphatidylinositol-specific phospholipase C, X and Y boxes
IPR000909:PI-PLC-X 
Evalue:-92.6197891235352 
Location:313-464IPR001711:PI-PLC-Y 
Evalue:-82.958610534668 
Location:541-658IPR000008:C2 
Evalue:-16.0809211730957 
Location:680-763IPR011992:EF-Hand_type 
Evalue:-15.221848487854 
Location:217-308IPR011993:PH_type 
Evalue:0 
Location:5-145IPR001192:PHPHLIPASEC 
Evalue:0 
Location:764-774
SequencesProtein: PLCB2_HUMAN (1181 aa)
mRNA: NM_004573
Local Annotation
Synapse Ontology
Any process that activates or increases the rate, frequency or extent of synaptic growth at neuromuscular junction.
sdb:0047 positive regulation of synaptic growth at neuromuscular junction  (Evidence:domains)
those channels, like InsP3-gated calcium channels which activated by InsP3 and release calcium into plasma.
sdb:0117 ionotropic receptor on the ER  (Evidence:domains)
protein kinase-catalyzed phosphorylation of specific ion channel subunits lead to cell surface expression of ion channel subunit
sdb:0201 cell surface expression of ion channel subunit  (Evidence:domains)
activation of calmodulin-dependent protein kinases
sdb:0204 activation of calmodulin-dependent protein kinase  (Evidence:domains)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:domains)
intracellular calcium store release to change the concentration of cytosolic calcium.
sdb:0321 intracellular calcium store release  (Evidence:domains)
KO assignmentK05858
  Level 3 annotation:
    phospholipase C, beta
  Level 2 annotation:
    Inositol phosphate metabolism
    Wnt signaling pathway
    Calcium signaling pathway
    Phosphatidylinositol signaling system
    Gap junction
    Long-term potentiation
    Long-term depression
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 337 residues, 38367401-38368411Exon2: 31 residues, 38368764-38368851Exon3: 21 residues, 38369517-38369575Exon4: 34 residues, 38370069-38370165Exon5: 27 residues, 38370253-38370330Exon6: 57 residues, 38370510-38370676Exon7: 76 residues, 38370757-38370980Exon8: 17 residues, 38371098-38371143Exon9: 27 residues, 38371341-38371417Exon10: 33 residues, 38371556-38371651Exon11: 37 residues, 38371831-38371936Exon12: 35 residues, 38372418-38372518Exon13: 57 residues, 38373052-38373217Exon14: 53 residues, 38373758-38373913Exon15: 43 residues, 38374428-38374553Exon16: 30 residues, 38374693-38374778Exon17: 34 residues, 38375788-38375885Exon18: 39 residues, 38376014-38376127Exon19: 52 residues, 38376250-38376401Exon20: 30 residues, 38377013-38377098Exon21: 29 residues, 38377369-38377452Exon22: 54 residues, 38377715-38377873Exon23: 51 residues, 38378054-38378201Exon24: 57 residues, 38378290-38378457Exon25: 35 residues, 38378620-38378721Exon26: 27 residues, 38381449-38381525Exon27: 20 residues, 38381628-38381682Exon28: 28 residues, 38381762-38381842Exon29: 49 residues, 38381961-38382102Exon30: 25 residues, 38382780-38382849Exon31: 28 residues, 38383493-38383571Exon32: 85 residues, 38387081-38387330Exon33: 2 residues, -Jump to PLCB2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2873 38484977-38498355 ~-13K 12090(IVD)(+)Loci: 2874 38550504-38552645 ~-2K 12093(D4ST1)(+)Loci: 2875 38673738-38743829 ~-70K 12099(CASC5)(+)Loci: 2876 38843576-38847203 ~-4K 12107(GCHFR)(+)Loci: 2877 38973919-38983464 ~-10K 12116(VPS18)(+)Loci: 4163 38367401-38387330 ~-20K 12082(PLCB2)(-)Link out to UCSC