P08487
Gene name |
PLCG1 |
Protein name |
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 |
Names |
PLC-148, Phosphoinositide phospholipase C-gamma-1, Phospholipase C-II, PLC-II, Phospholipase C-gamma-1, PLC-gamma-1 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:281987 |
EC number |
3.1.4.11: Phosphoric diester hydrolases |
Protein Class |
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN (PTHR10336) |
Descriptions
Phosphoinositide-specific phospholipase C-gamma1 (PLC-gamma1) mediates the production of secondary messenger molecules, diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), and is involved in the regulation of intracellular signal transduction. The N-terminal SH2 (SH2N) of PLC-gamma1 is involved in NFAT activation and this activation is autoinhibited by C-terminal SH2 (SH2C) domain of PLC-gamma1 protein. Deletion of sPHN domain substantially increased the ability of PLC-gamma1 to bind LAT protein mediated by SH2C domain. In rat, PLC-gamma1 is a substrate of ITK that recognizes the SH2C domain of PLC-gamma1. The linker downstream of SH2C adopts an intramolecular complex with the SHC2 domain, which prevents the recognition of SH2C by ITK.
Autoinhibitory domains (AIDs)
Target domain |
668-756 (C-terminal SH2 domain) |
Relief mechanism |
Ligand binding |
Assay |
Deletion assay, Mutagenesis experiment |
Target domain |
791-851 (SH3 domain) |
Relief mechanism |
Partner binding |
Assay |
Mutagenesis experiment, Deletion assay, Structural analysis |
Target domain |
666-756 (C-terminal SH2 domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Devkota S et al. (2015) "Scaffold Protein SLP-76 Primes PLCγ1 for Activation by ITK-Mediated Phosphorylation", Journal of molecular biology, 427, 2734-47
- Kunze K et al. (2014) "A recurrent activating PLCG1 mutation in cardiac angiosarcomas increases apoptosis resistance and invasiveness of endothelial cells", Cancer research, 74, 6173-83
- DeBell K et al. (2007) "Intramolecular regulation of phospholipase C-gamma1 by its C-terminal Src homology 2 domain", Molecular and cellular biology, 27, 854-63
- Xie Q et al. (2013) "Substrate recognition of PLCγ1 via a specific docking surface on Itk", Journal of molecular biology, 425, 683-96
Autoinhibited structure
Activated structure
8 structures for P08487
No variants for P08487
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P08487 | |||||
No associated diseases with P08487
14 regional properties for P08487
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1071 - 1194 | IPR000008 |
| domain | Phosphatidylinositol-specific phospholipase C, X domain | 320 - 465 | IPR000909 |
| domain | SH2 domain | 548 - 657 | IPR000980-1 |
| domain | SH2 domain | 666 - 756 | IPR000980-2 |
| domain | SH3 domain | 791 - 851 | IPR001452 |
| domain | Phospholipase C, phosphatidylinositol-specific, Y domain | 953 - 1070 | IPR001711 |
| domain | Pleckstrin homology domain | 27 - 144 | IPR001849-1 |
| domain | Pleckstrin homology domain | 489 - 680 | IPR001849-2 |
| domain | Pleckstrin homology domain | 804 - 933 | IPR001849-3 |
| domain | EF-hand domain | 152 - 187 | IPR002048 |
| binding_site | EF-Hand 1, calcium-binding site | 165 - 177 | IPR018247 |
| domain | PLC-gamma, C-terminal SH2 domain | 663 - 765 | IPR035023 |
| domain | PLC-gamma, N-terminal SH2 domain | 545 - 649 | IPR035024 |
| domain | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1, SH3 domain | 791 - 850 | IPR035724 |
Functions
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| COP9 signalosome | A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| lamellipodium | A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent phospholipase C activity | Catalysis of the reaction: a phosphatidylcholine + H2O = 1,2-diacylglycerol + choline phosphate. This reaction requires Ca2+. |
| phosphatidylinositol phospholipase C activity | Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1,2-diacylglycerol + 1D-myo-inositol 1,4,5-trisphosphate + H(+). |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to epidermal growth factor stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an epidermal growth factor stimulus. |
| cellular response to vascular endothelial growth factor stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vascular endothelial growth factor stimulus. |
| epidermal growth factor receptor signaling pathway | The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. |
| in utero embryonic development | The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| phosphatidylinositol metabolic process | The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. |
| phospholipid catabolic process | The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester. |
| positive regulation of epithelial cell migration | Any process that activates or increases the frequency, rate or extent of epithelial cell migration. |
15 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q1RML2 | PLCZ1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 | Bos taurus (Bovine) | PR |
| P10894 | PLCB1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 | Bos taurus (Bovine) | SS |
| P10895 | PLCD1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 | Bos taurus (Bovine) | SS |
| P16885 | PLCG2 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 | Homo sapiens (Human) | SS |
| P19174 | PLCG1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 | Homo sapiens (Human) | EV |
| Q62077 | Plcg1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 | Mus musculus (Mouse) | SS |
| P24135 | Plcg2 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 | Rattus norvegicus (Rat) | SS |
| P10686 | Plcg1 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 | Rattus norvegicus (Rat) | EV |
| Q39032 | PLC1 | Phosphoinositide phospholipase C 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q56W08 | PLC3 | Phosphoinositide phospholipase C 3 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q6NMA7 | PLC9 | Phosphoinositide phospholipase C 9 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q8GV43 | PLC6 | Phosphoinositide phospholipase C 6 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q944C2 | PLC5 | Phosphoinositide phospholipase C 5 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9STZ3 | PLC8 | Phosphoinositide phospholipase C 8 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q944C1 | PLC4 | Phosphoinositide phospholipase C 4 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGAASPCAN | GCGPSAPSDA | EVVHLCRSLE | VGTVMTLFYS | KKSQRPERKT | FQVKLETRQI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TWSRGADKIE | GAIDIREIKE | IRPGKTSRDF | DRYQEDPAFR | PDQSHCFVIL | YGMEFRLKTL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLQATSEDEV | NMWIRGLTWL | MEDTLQAATP | LQIERWLRKQ | FYSVDRNRED | RISAKDLKNM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LSQVNYRVPN | MRFLRERLTD | LEQRTSDITY | GQFAQLYRSL | MYSAQKTMDL | PFLEASALRA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GERPELCRVS | LPEFQQFLLE | YQGELWAVDR | LQVQEFMLSF | LRDPLREIEE | PYFFLDEFVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FLFSKENSIW | NSQLDEVCPD | TMNNPLSHYW | ISSSHNTYLT | GDQFSSESSL | EAYARCLRMG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| CRCIELDCWD | GPDGMPVIYH | GHTLTTKIKF | SDVLHTIKEH | AFVASEYPVI | LSIEDHCSIA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QQRNMAQYFK | KVLGDTLLTK | PVDIAADGLP | SPNQLKRKIL | IKHKKLAEGS | AYEEVPTSVM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YSENDISNSI | KNGILYLEDP | VNHEWYPHYF | VLTSSKIYYS | EETSSDQGNE | DEEEPKEASG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| STELHSNEKW | FHGKLGAGRD | GRHIAERLLT | EYCIETGAPD | GSFLVRESET | FVGDYTLSFW |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RNGKVQHCRI | HSRQDAGTPK | FFLTDNLVFD | SLYDLITHYQ | QVPLRCNEFE | MRLSEPVPQT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NAHESKEWYH | ASLTRAQAEH | MLMRVPRDGA | FLVRKRNEPN | SYAISFRAEG | KIKHCRVQQE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GQTVMLGNSE | FDSLVDLISY | YEKHPLYRKM | KLRYPINEEA | LEKIGTAEPD | YGALYEGRNP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GFYVEANPMP | TFKCAVKALF | DYKAQREDEL | TFTKSAIIQN | VEKQEGGWWR | GDYGGKKQLW |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FPSNYVEEMV | SPAALEPERE | HLDENSPLGD | LLRGVLDVPA | CQIAVRPEGK | NNRLFVFSIS |
| 910 | 920 | 930 | 940 | 950 | 960 |
| MASVAHWSLD | VAADSQEELQ | DWVKKIREVA | QTADARLTEG | KMMERRKKIA | LELSELVVYC |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| RPVPFDEEKI | GTERACYRDM | SSFPETKAEK | YVNKAKGKKF | LQYNRLQLSR | IYPKGQRLDS |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SNYDPLPMWI | CGSQLVALNF | QTPDKPMQMN | QALFLAGGHC | GYVLQPSVMR | DEAFDPFDKS |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| SLRGLEPCAI | CIEVLGARHL | PKNGRGIVCP | FVEIEVAGAE | YDSIKQKTEF | VVDNGLNPVW |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| PAKPFHFQIS | NPEFAFLRFV | VYEEDMFSDQ | NFLAQATFPV | KGLKTGYRAV | PLKNNYSEGL |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| ELASLLVKID | VFPAKQENGD | LSPFGGASLR | ERSCDASGPL | FHGRAREGSF | EARYQQPFED |
| 1270 | 1280 | 1290 | |||
| FRISQEHLAD | HFDGRDRRTP | RRTRVNGDNR | L |