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0PLCG1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePLCG1
Description1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1 (ec 3.1.4.11) (phosphoinositide phospholipase c) (plc-gamma-1) (phospholipase c-gamma-1) (plc-ii) (plc-148).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004435 phosphoinositide phospholipase C activity (NAS)
0005515 protein binding (IPI)
0005057 receptor signaling protein activity (NAS)
0007165 signal transduction (NAS)

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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
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
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps . Similar sequences were later found in many other intracellular signal-transducing proteins . SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific.H2 domains recognize between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs fromone SH2 domain to another.nd strictly phosphorylation-dependent manner . They are found in a wide variety of protein contexts e.g..n association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules..e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the alpha+beta class.ts overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel beta-sheet.lanked by 2 short alpha-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand.nd is hence designated the phosphate binding loop.he phosphorylated ligand binds perpendicular to the beta-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins .
  IPR000980:SH2 motif
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
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
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:-94.5850296020508 
Location:321-465IPR001711:PLCYc 
Evalue:-69.0043648054025 
Location:953-1070IPR000980:SH2 
Evalue:-31.5686359405518 
Location:550-639IPR000980:SH2 
Evalue:-28.8860569000244 
Location:668-741IPR000008:C2 
Evalue:-20.8239078521729 
Location:1090-1177IPR001452:SH3_1 
Evalue:-20.4559326171875 
Location:794-849IPR011993:PH_type 
Evalue:-13.5228786468506 
Location:17-152IPR011992:EF-Hand_type 
Evalue:0 
Location:156-218IPR001849:PH_DOMAIN 
Evalue:0 
Location:895-931IPR001192:PHPHLIPASEC 
Evalue:0 
Location:1178-1188
SequencesProtein: PLCG1_HUMAN (1290 aa)
mRNA: NM_002660 NM_182811
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 assignmentK05859
  Level 3 annotation:
    phospholipase C, gamma
  Level 2 annotation:
    Inositol phosphate metabolism
    Calcium signaling pathway
    Phosphatidylinositol signaling system
    Natural killer cell mediated cytotoxicity
    Fc epsilon RI signaling pathway
    Leukocyte transendothelial migration
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 113 residues, 39199574-39199912Exon2: 53 residues, 39221659-39221812Exon3: 33 residues, 39221923-39222017Exon4: 18 residues, 39222159-39222207Exon5: 30 residues, 39224505-39224590Exon6: 30 residues, 39224695-39224779Exon7: 13 residues, 39225011-39225046Exon8: 26 residues, 39225256-39225329Exon9: 36 residues, 39225431-39225533Exon10: 41 residues, 39225768-39225887Exon11: 30 residues, 39225974-39226060Exon12: 42 residues, 39226134-39226255Exon13: 58 residues, 39226986-39227155Exon14: 43 residues, 39227298-39227421Exon15: 36 residues, 39227503-39227605Exon16: 64 residues, 39227692-39227880Exon17: 69 residues, 39228247-39228448Exon18: 42 residues, 39228529-39228649Exon19: 62 residues, 39228732-39228913Exon20: 28 residues, 39229905-39229983Exon21: 36 residues, 39230820-39230924Exon22: 34 residues, 39231132-39231229Exon23: 25 residues, 39231510-39231580Exon24: 54 residues, 39232165-39232323Exon25: 34 residues, 39234246-39234343Exon26: 77 residues, 39234474-39234699Exon27: 51 residues, 39234782-39234931Exon28: 40 residues, 39235473-39235588Exon29: 56 residues, 39235705-39235867Exon30: 31 residues, 39235976-39236065Exon31: 64 residues, 39236177-39236365Exon32: 419 residues, 39236520-39237771Exon33: 2 residues, -Jump to PLCG1_HUMANExon1: 113 residues, 39199574-39199912Exon2: 53 residues, 39221659-39221812Exon3: 33 residues, 39221923-39222017Exon4: 18 residues, 39222159-39222207Exon5: 30 residues, 39224505-39224590Exon6: 30 residues, 39224695-39224779Exon7: 13 residues, 39225011-39225046Exon8: 26 residues, 39225256-39225329Exon9: 36 residues, 39225431-39225533Exon10: 41 residues, 39225768-39225887Exon11: 30 residues, 39225974-39226060Exon12: 42 residues, 39226134-39226255Exon13: 58 residues, 39226986-39227155Exon14: 43 residues, 39227298-39227421Exon15: 36 residues, 39227503-39227605Exon16: 64 residues, 39227692-39227880Exon17: 69 residues, 39228247-39228448Exon18: 42 residues, 39228529-39228649Exon19: 62 residues, 39228732-39228913Exon20: 28 residues, 39229905-39229983Exon21: 36 residues, 39230820-39230924Exon22: 34 residues, 39231132-39231229Exon23: 25 residues, 39231510-39231580Exon24: 54 residues, 39232165-39232323Exon25: 34 residues, 39234246-39234343Exon26: 77 residues, 39234474-39234699Exon27: 51 residues, 39234782-39234931Exon28: 40 residues, 39235473-39235588Exon29: 56 residues, 39235705-39235867Exon30: 31 residues, 39235976-39236065Exon31: 63 residues, 39236180-39236365Exon32: 419 residues, 39236520-39237771Exon33: 2 residues, -Jump to PLCG1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4522 39464583-39680547 ~-216K 23108(CHD6)(-)Loci: 3256 39199574-39237771 ~-38K 23100(PLCG1)(+)Link out to UCSC