EzCatDB: M00183
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DB codeM00183
RLCP classification1.15.72000.565 : Hydrolysis
CATH domainDomain 12.30.29.30 : PH-domain like
Domain 21.10.238.10 : Recoverin; domain 1
Domain 31.10.238.10 : Recoverin; domain 1
Domain 43.20.20.190 : TIM BarrelCatalytic domain
Domain 52.30.29.30 : PH-domain like
Domain 63.30.505.10 : SHC Adaptor Protein
Domain 73.30.505.10 : SHC Adaptor Protein
Domain 82.30.30.40 : SH3 type barrels.
Domain 92.60.40.150 : Immunoglobulin-like
Domain 10-.-.-.-
E.C.3.1.4.11

CATH domainRelated DB codes (homologues)
1.10.238.10 : Recoverin; domain 1M00198,D00151,M00118
2.30.29.30 : PH-domain likeM00125,M00344,M00118
2.30.30.40 : SH3 type barrels.M00043,M00130,T00256,M00304,M00335
2.60.40.150 : Immunoglobulin-likeM00221,M00043,M00118
3.20.20.190 : TIM BarrelS00236,M00118
3.30.505.10 : SHC Adaptor ProteinM00043,M00130,M00148,T00256,M00304,M00333,M00339,M00344,T00221

Enzyme Name
UniProtKBKEGG

Q9X0A5P08487P19174
Protein name
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1phosphoinositide phospholipase C
triphosphoinositide phosphodiesterase
phosphoinositidase C
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
monophosphatidylinositol phosphodiesterase
phosphatidylinositol phospholipase C
PI-PLC
1-phosphatidyl-D-myo-inositol-4,5-bisphosphateinositoltrisphosphohydrolase
SynonymsPutative uncharacterized protein
EC 3.1.4.11
Phosphoinositide phospholipase C
Phospholipase C-gamma-1
PLC-gamma-1
PLC-II
PLC-148
EC 3.1.4.11
Phosphoinositide phospholipase C
Phospholipase C-gamma-1
PLC-gamma-1
PLC-II
PLC-148
RefSeqNP_228818.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
NP_776850.1 (Protein)
NM_174425.3 (DNA/RNA sequence)
NP_002651.2 (Protein)
NM_002660.2 (DNA/RNA sequence)
NP_877963.1 (Protein)
NM_182811.1 (DNA/RNA sequence)
Pfam
PF00168 (C2)
PF09279 (efhand_like)
PF00388 (PI-PLC-X)
PF00387 (PI-PLC-Y)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical view]
PF00168 (C2)
PF09279 (efhand_like)
PF00388 (PI-PLC-X)
PF00387 (PI-PLC-Y)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00562Inositol phosphate metabolism
MAP04070Phosphatidylinositol signaling system

UniProtKB:Accession NumberQ9X0A5P08487P19174
Entry nameQ9X0A5_THEMAPLCG1_BOVINPLCG1_HUMAN
Activity
1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Subunit
Interacts with CENTG1 via its SH3 domain. Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro- rich domain of TNK1 via its SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells, which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1 and MIST (By similarity). Interacts with RALGPS1 (By similarity).Interacts with CENTG1 via its SH3 domain (By similarity). Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro-rich domain of TNK1 via its SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor- dependent fashion. Interacts with CBLB in activated T-cells, which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1 and MIST (By similarity). Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein.
Subcellular location


Cofactor
Calcium.Calcium.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00076C00001C04021C04637C00165C00641C01245
CompoundCalciumH2OPhosphatidylinositol phosphate1-Phosphatidyl-D-myo-inositol 4,5-bisphosphateDiacylglycerol1,2-Diacyl-sn-glycerolD-myo-Inositol 1,4,5-trisphosphate
Typedivalent metal (Ca2+, Mg2+)H2Ocarbohydrate,phosphate group/phosphate ioncarbohydrate,lipid,phosphate group/phosphate ioncarbohydrate,lipidcarbohydrate,lipidcarbohydrate,phosphate group/phosphate ion
ChEBI29108
15377




16595
PubChem271
962
22247451




439456
               
2fclAUnbound UnboundUnboundUnboundUnboundUnbound
2pldAUnbound UnboundUnboundUnboundUnboundUnbound
2pleAUnbound UnboundUnboundUnboundUnboundUnbound
1hspAUnbound UnboundUnboundUnboundUnboundUnbound
1hsqAUnbound UnboundUnboundUnboundUnboundUnbound
2hspAUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdb
        
2fclA
2pldA
2pleA
1hspA
1hsqA
2hspA


references
[1]
CommentsPHOSPHORYLATION SITES.
Medline ID90154080
PubMed ID1689310
JournalJ Biol Chem
Year1990
Volume265
Pages3940-3
AuthorsKim JW, Sim SS, Kim UH, Nishibe S, Wahl MI, Carpenter G, Rhee SG
TitleTyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro.
Related UniProtKBP08487
[2]
CommentsPHOSPHORYLATION SITES.
Medline ID90154081
PubMed ID1689311
JournalJ Biol Chem
Year1990
Volume265
Pages3944-8
AuthorsWahl MI, Nishibe S, Kim JW, Kim H, Rhee SG, Carpenter G
TitleIdentification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells.
Related UniProtKBP08487
[3]
CommentsPHOSPHORYLATION SITES.
Medline ID91208680
PubMed ID1708307
JournalCell
Year1991
Volume65
Pages435-41
AuthorsKim HK, Kim JW, Zilberstein A, Margolis B, Kim JG, Schlessinger J, Rhee SG
TitlePDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.
Related UniProtKBP08487
[4]
CommentsSTRUCTURE BY NMR OF SH3 DOMAIN.
Medline ID93208890
PubMed ID7681365
JournalCell
Year1993
Volume72
Pages953-60
AuthorsKohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J, Inagaki F
TitleSolution structure of the SH3 domain of phospholipase C-gamma.
Related PDB1hsp,1hsq,2hsp
Related UniProtKBP19174
[5]
PubMed ID7993895
JournalBiochemistry
Year1994
Volume33
Pages14671-8
AuthorsGergel JR, McNamara DJ, Dobrusin EM, Zhu G, Saltiel AR, Miller WT
TitleIdentification of amino acids in the N-terminal SH2 domain of phospholipase C gamma 1 important in the interaction with epidermal growth factor receptor.
[6]
CommentsSTRUCTURE BY NMR OF 663-759.
Medline ID94236690
PubMed ID8181064
JournalCell
Year1994
Volume77
Pages461-72
AuthorsPascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD
TitleNuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide.
Related PDB2pld,2ple
Related UniProtKBP08487
[7]
PubMed ID7843417
JournalFEBS Lett
Year1995
Volume358
Pages287-92
AuthorsHuang PS, Davis L, Huber H, Goodhart PJ, Wegrzyn RE, Oliff A, Heimbrook DC
TitleAn SH3 domain is required for the mitogenic activity of microinjected phospholipase C-gamma 1.
[8]
PubMed ID8524815
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages11618-22
AuthorsHuang X, Li Y, Tanaka K, Moore KG, Hayashi JI
TitleCloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase C gamma 1, Grb2, and phosphatidylinositol 3-kinase.
[9]
PubMed ID7773170
JournalProtein Sci
Year1995
Volume4
Pages13-20
AuthorsMacLean D, Sefler AM, Zhu G, Decker SJ, Saltiel AR, Singh J, McNamara D, Dobrusin EM, Sawyer TK
TitleDifferentiation of peptide molecular recognition by phospholipase C gamma-1 Src homology-2 domain and a mutant Tyr phosphatase PTP1bC215S.
[10]
PubMed ID8660853
JournalCell Immunol
Year1996
Volume171
Pages164-9
AuthorsKanner SB
TitleFocal adhesion kinase-related fakB is regulated by the integrin LFA-1 and interacts with the SH3 domain of phospholipase C gamma 1.
[11]
PubMed ID8941357
JournalBiochem Biophys Res Commun
Year1996
Volume228
Pages802-6
AuthorsPei Z, Yang L, Williamson JR
TitlePhospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro.
[12]
PubMed ID8630067
JournalBiochem Biophys Res Commun
Year1996
Volume222
Pages186-93
AuthorsSmith MR, Liu YL, Kim SR, Bae YS, Kim CG, Kwon KS, Rhee SG, Kung HF
TitlePLC gamma 1 Src homology domain induces mitogenesis in quiescent NIH 3T3 fibroblasts.
[13]
PubMed ID8598208
JournalEMBO J
Year1996
Volume15
Pages73-82
AuthorsObermeier A, Tinhofer I, Grunicke HH, Ullrich A
TitleTransforming potentials of epidermal growth factor and nerve growth factor receptors inversely correlate with their phospholipase C gamma affinity and signal activation.
[14]
PubMed ID8657103
JournalMol Cell Biol
Year1996
Volume16
Pages1305-15
AuthorsLaw CL, Chandran KA, Sidorenko SP, Clark EA
TitlePhospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.
[15]
PubMed ID8649391
JournalMol Cell Biol
Year1996
Volume16
Pages2823-9
AuthorsMotto DG, Musci MA, Ross SE, Koretzky GA
TitleTyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C gamma 1 activation in T cells.
[16]
PubMed ID9712732
JournalBiochem Biophys Res Commun
Year1998
Volume249
Pages537-41
AuthorsGraham LJ, Stoica BA, Shapiro M, DeBell KE, Rellahan B, Laborda J, Bonvini E
TitleSequences surrounding the Src-homology 3 domain of phospholipase Cgamma-1 increase the domain's association with Cbl.
[17]
PubMed ID9514887
JournalBiochem Biophys Res Commun
Year1998
Volume244
Pages62-7
AuthorsAhn SJ, Han SJ, Mo HJ, Chung JK, Hong SH, Park TK, Kim CG
TitleInteraction of phospholipase C gamma 1 via its COOH-terminal SRC homology 2 domain with synaptojanin.
[18]
PubMed ID9468499
JournalJ Biol Chem
Year1998
Volume273
Pages4465-9
AuthorsBae YS, Cantley LG, Chen CS, Kim SR, Kwon KS, Rhee SG
TitleActivation of phospholipase C-gamma by phosphatidylinositol 3,4,5-trisphosphate.
[19]
PubMed ID9570517
JournalJ Immunol
Year1998
Volume160
Pages1059-66
AuthorsStoica B, DeBell KE, Graham L, Rellahan BL, Alava MA, Laborda J, Bonvini E
TitleThe amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1.
[20]
PubMed ID9882440
JournalArch Biochem Biophys
Year1999
Volume361
Pages149-55
AuthorsHorstman DA, Chattopadhyay A, Carpenter G
TitleThe influence of deletion mutations on phospholipase C-gamma 1 activity.
[21]
PubMed ID10360750
JournalBioorg Med Chem Lett
Year1999
Volume9
Pages1429-32
AuthorsLee JS, Yang MY, Yeo H, Kim J, Lee HS, Ahn JS
TitleUncarinic acids: phospholipase Cgamma1 inhibitors from hooks of Uncaria rhynchophylla.
[22]
PubMed ID10202147
JournalEMBO J
Year1999
Volume18
Pages1832-44
AuthorsWilliams BL, Irvin BJ, Sutor SL, Chini CC, Yacyshyn E, Bubeck Wardenburg J, Dalton M, Chan AC, Abraham RT
TitlePhosphorylation of Tyr319 in ZAP-70 is required for T-cell antigen receptor-dependent phospholipase C-gamma1 and Ras activation.
[23]
PubMed ID10350061
JournalFEBS Lett
Year1999
Volume450
Pages77-83
AuthorsPumphrey NJ, Taylor V, Freeman S, Douglas MR, Bradfield PF, Young SP, Lord JM, Wakelam MJ, Bird IN, Salmon M, Buckley CD
TitleDifferential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31.
[24]
PubMed ID10586033
JournalJ Immunol
Year1999
Volume163
Pages6435-41
AuthorsPerez-Villar JJ, Kanner SB
TitleRegulated association between the tyrosine kinase Emt/Itk/Tsk and phospholipase-C gamma 1 in human T lymphocytes.
[25]
PubMed ID10672930
JournalMol Cells
Year1999
Volume9
Pages631-7
AuthorsKim MJ, Si F, Kim SJ, Hong SB, Hwang JI, Lee HJ, Lee SJ, Chang JS, Lee YH, Ryu SH, Suh PG
TitleThe SH2-SH2-SH3 domain of phospholipase C-gamma1 directly binds to translational elongation factor-1alpha.
[26]
PubMed ID10438904
JournalJ Immunol
Year1999
Volume163
Pages1746-9
AuthorsIshiai M, Sugawara H, Kurosaki M, Kurosaki T
TitleCutting edge: association of phospholipase C-gamma 2 Src homology 2 domains with BLNK is critical for B cell antigen receptor signaling.
[27]
PubMed ID10873601
JournalBiochem Biophys Res Commun
Year2000
Volume273
Pages294-301
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TitleCharacterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1.
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PubMed ID11094067
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Year2000
Volume20
Pages9149-61
AuthorsIrvin BJ, Williams BL, Nilson AE, Maynor HO, Abraham RT
TitlePleiotropic contributions of phospholipase C-gamma1 (PLC-gamma1) to T-cell antigen receptor-mediated signaling: reconstitution studies of a PLC-gamma1-deficient Jurkat T-cell line.
[29]
PubMed ID11015615
JournalPhysiol Rev
Year2000
Volume80
Pages1291-335
AuthorsRebecchi MJ, Pentyala SN
TitleStructure, function, and control of phosphoinositide-specific phospholipase C.
[30]
PubMed ID11502583
JournalAm J Physiol Cell Physiol
Year2001
Volume281
PagesC1046-58
AuthorsPanebra A, Ma SX, Zhai LW, Wang XT, Rhee SG, Khurana S
TitleRegulation of phospholipase C-gamma(1) by the actin-regulatory protein villin.
[31]
PubMed ID11331309
JournalJ Cell Biol
Year2001
Volume153
Pages599-612
AuthorsMatsuda M, Paterson HF, Rodriguez R, Fensome AC, Ellis MV, Swann K, Katan M
TitleReal time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor.
[32]
PubMed ID11390650
JournalMol Cell Biol
Year2001
Volume21
Pages4208-18
AuthorsYablonski D, Kadlecek T, Weiss A
TitleIdentification of a phospholipase C-gamma1 (PLC-gamma1) SH3 domain-binding site in SLP-76 required for T-cell receptor-mediated activation of PLC-gamma1 and NFAT.
[33]
PubMed ID12061819
JournalExp Cell Res
Year2002
Volume277
Pages86-94
AuthorsTvorogov D, Carpenter G
TitleEGF-dependent association of phospholipase C-gamma1 with c-Cbl.
[34]
PubMed ID12374773
JournalFASEB J
Year2002
Volume16
Pages1504-14
AuthorsShin SY, Ko J, Chang JS, Min do S, Choi C, Bae SS, Kim MJ, Hyun DS, Kim JH, Han MY, Kim YH, Kim YS, Na DS, Suh PG, Lee YH
TitleNegative regulatory role of overexpression of PLC gamma 1 in the expression of early growth response 1 gene in rat 3Y1 fibroblasts.
[35]
PubMed ID11886851
JournalJ Biol Chem
Year2002
Volume277
Pages19697-702
AuthorsChang JS, Seok H, Kwon TK, Min do S, Ahn BH, Lee YH, Suh JW, Kim JW, Iwashita S, Omori A, Ichinose S, Numata O, Seo JK, Oh YS, Suh PG
TitleInteraction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity.
[36]
PubMed ID14993410
JournalMol Interv
Year2002
Volume2
Pages352-5;338
AuthorsWang Z, Moran MF
TitlePhospholipase C-gamma1: a phospholipase and guanine nucleotide exchange factor.
[37]
PubMed ID12226755
JournalOncogene
Year2002
Volume21
Pages6520-9
AuthorsPiccolo E, Innominato PF, Mariggio MA, Maffucci T, Iacobelli S, Falasca M
TitleThe mechanism involved in the regulation of phospholipase Cgamma1 activity in cell migration.
[38]
PubMed ID11796522
JournalEndocrinology
Year2002
Volume143
Pages655-64
AuthorsEichhorn J, Kayali AG, Resor L, Austin DA, Rose DW, Webster NJ
TitlePLC-gamma1 enzyme activity is required for insulin-induced DNA synthesis.

comments
Although this enzyme is partially homologous to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase from rat and human (Swiss-prot;P10688, M00118), the tertiary structure of catalytic domain has not been sulved yet. Comparison of sequence data suggests that this enzyme should have a similar catalytic site.
This enzyme must be composed of the following domains:
the N-terminal PH domain (CATH 2.30.29.30),
two EF-hand domains (CATH 1.10.238.10),
a catalytic domain (CATH 3.20.20.190), which is split into two regions,
another PH domain, which is also split into two regions,
two SH2 domains (CATH 3.30.505.10),
SH3 domain (CATH 2.30.30.40),
C2 domain (CATH 2.60.40.150),
and the C-terminal domain.

createdupdated
2003-08-282009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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