AiPD: Autoinhibited Protein Database

G3QXU1

Gene name	PLCG1
Protein name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
Names
Species	Gorilla gorilla gorilla (Western lowland gorilla)
KEGG Pathway
EC number
Protein Class

Descriptions

Phosphoinositide-specific phospholipase C-gamma1 (PLC-gamma1) mediates the production of seondary messenger molecules, diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), and is involved in the regulation of intracellular signal transduction. The C-terminal SH2 (SH2C) domain (second SH2 domain) is involved in the autoinhibition of PLC-gamma1 protein. The N-terminal portion of PH domain regulates the binding of SH2C. In rat, Plcg1 is a substrate of Itk that recognizes the SH2C domain of PLC-gamma1. The linker downstream of SH2C adopts an intramolecular complex with SHC2 domain, which prevents the recognition of SH2C by Itk.

Autoinhibitory domains (AIDs)

668-790 (C-terminal SH2 domain) SS

Target domain	320-465 (Catalytic PLC X domain)
Relief mechanism	PTM, Partner binding
Assay

AID

668-790 (C-terminal SH2 domain)

Target domain

320-465 (Catalytic PLC X domain)

Relief mechanism

PTM (Phosphorylation of Y783. This phosphorylated region directly interacts with cSH2 domain.), Partner binding(Interactions with scaffold proteins such as SLP-76)

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

0 structures for G3QXU1

Entry ID	Method	Resolution	Chain	Position	Source

No variants for G3QXU1

Variant ID(s)	Position	Change	Description	Diseaes Association	Provenance
No variants for G3QXU1

No associated diseases with G3QXU1

8 regional properties for G3QXU1

Type	Name	Position	InterPro Accession
domain	C2 domain	1071 - 1194	IPR000008
domain	SH2 domain	548 - 657	IPR000980-1
domain	SH2 domain	666 - 756	IPR000980-2
domain	Phospholipase C, phosphatidylinositol-specific, Y domain	953 - 1070	IPR001711
domain	EF-hand domain	152 - 187	IPR002048
binding_site	EF-Hand 1, calcium-binding site	165 - 177	IPR018247
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

		Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category	No pathway information available

3 GO annotations of cellular component

Name	Definition
cell-cell junction	A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects.
glutamatergic synapse	A synapse that uses glutamate as a neurotransmitter.
Schaffer collateral - CA1 synapse	A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.

4 GO annotations of molecular function

Name	Definition
calcium ion binding	Binding to a calcium ion (Ca2+).
glutamate receptor binding	Binding to a glutamate receptor.
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(+).
receptor tyrosine kinase binding	Binding to a receptor that possesses protein tyrosine kinase activity.

7 GO annotations of biological process

Name	Definition
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.
inositol phosphate metabolic process	The chemical reactions and pathways involving inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
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.
modulation of chemical synaptic transmission	Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission.
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.
T cell receptor signaling pathway	The series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.

No homologous proteins in AiPD

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
No homologous proteins

10	20	30	40	50	60
MAGAASPCAN	GCGPGAPSDA	EVLHLCRSLE	VGTVMTLFYS	KKSQRPERKT	FQVKLETRQI
70	80	90	100	110	120
TWSRGADKIE	GAIDIREIKE	IRPGKTSRDF	DRYQEDPAFR	PDQSHCFVIL	YGMEFRLKTL
130	140	150	160	170	180
SLQATSEDEV	NMWIKGLTWL	MEDTLQAPTP	LQIERWLRKQ	FYSVDRNRED	RISAKDLKNM
190	200	210	220	230	240
LSQVNYRVPN	MRFLRERLTD	LEQRSGDITY	GQFAQLYRSL	MYSAQKTMDL	PFLEASTLRA
250	260	270	280	290	300
GERPELCRVS	LPEFQQFLLD	YQGELWAVDR	LQVQEFMLSF	LRDPLREIEE	PYFFLDEFVT
310	320	330	340	350	360
FLFSKENSVW	NSQLDAVCPD	TMNNPLSHYW	ISSSHNTYLT	GDQFSSESSL	EAYARCLRMG
370	380	390	400	410	420
CRCIELDCWD	GPDGMPVIYH	GHTLTTKIKF	SDVLHTIKEH	AFVASEYPVI	LSIEDHCSIA
430	440	450	460	470	480
QQRNMAQYFK	KVLGDTLLTK	PVEISADGLP	SPNQLKRKIL	IKHKKLAEGS	AYEEVPTSMM
490	500	510	520	530	540
YSENDISNSI	KNGILYLEDP	VNHEWYPHYF	VLTSSKIYYS	EETSSDQGNE	DEEEPKEVSS
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	NPVALEPERE	HLDENSPLGD	LLRGVLDVPA	CQIAIRPEGK	NNRLFVFSIS
910	920	930	940	950	960
MASVAHWSLD	VAADSQEELQ	DWVKKIREVA	QTADARLTEG	KIMERRKKIA	LELSELVVYC
970	980	990	1000	1010	1020
RPVPFDEEKI	GTERACYRDM	SSFPETKAEK	YVNKAKGKKF	LQYNRLQLSR	IYPKGQRLDS
1030	1040	1050	1060	1070	1080
SNYDPLPMWI	CGSQLVALNF	QTPDKPMQMN	QALFMTGRHC	GYVLQPSTMR	DEAFDPFDKS
1090	1100	1110	1120	1130	1140
SLRGLEPCAI	SIEVLGARHL	PKNGRGIVCP	FVEIEVAGAE	YDSTKQKTEF	VVDNGLNPVW
1150	1160	1170	1180	1190	1200
PAKPFHFQIS	NPEFAFLRFV	VYEEDMFSDQ	NFLAQATFPV	KGLKTGYRAV	PLKNNYSEDL
1210	1220	1230	1240	1250	1260
ELASLLIKID	IFPAKENGDL	SPFSGTSLRE	RGSDASGQLF	HGRAREGSFE	SRYQQPFEDF
1270	1280
RISQEHLADH	FDSRERRAPR	RTRVNGDNRL