Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Gene

Plcg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Enzyme regulationi

Activated by phosphorylation on tyrosine residues.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei335PROSITE-ProRule annotation1
Active sitei380PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi165 – 176PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Transducer
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.11 3474
ReactomeiR-MMU-1169408 ISG15 antiviral mechanism
R-MMU-170968 Frs2-mediated activation
R-MMU-1855204 Synthesis of IP3 and IP4 in the cytosol
R-MMU-186763 Downstream signal transduction
R-MMU-202433 Generation of second messenger molecules
R-MMU-2029485 Role of phospholipids in phagocytosis
R-MMU-212718 EGFR interacts with phospholipase C-gamma
R-MMU-2424491 DAP12 signaling
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-2871809 FCERI mediated Ca+2 mobilization
R-MMU-5218921 VEGFR2 mediated cell proliferation
R-MMU-5654219 Phospholipase C-mediated cascade: FGFR1
R-MMU-5654221 Phospholipase C-mediated cascade, FGFR2
R-MMU-5654227 Phospholipase C-mediated cascade, FGFR3
R-MMU-5654228 Phospholipase C-mediated cascade, FGFR4
R-MMU-8853659 RET signaling
R-MMU-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:Plcg1
Synonyms:Plcg-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97615 Plcg1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000884992 – 13021-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1Add BLAST1301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei506PhosphotyrosineCombined sources1
Modified residuei771Phosphotyrosine; by SYKCombined sources1
Modified residuei775PhosphotyrosineCombined sources1
Modified residuei783Phosphotyrosine; by ITK, SYK and TXKBy similarity1
Modified residuei977PhosphotyrosineCombined sources1
Modified residuei1221PhosphoserineBy similarity1
Modified residuei1227PhosphoserineBy similarity1
Modified residuei1233PhosphoserineBy similarity1
Modified residuei1248PhosphoserineBy similarity1
Modified residuei1253PhosphotyrosineBy similarity1
Modified residuei1263PhosphoserineBy similarity1

Post-translational modificationi

Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ (By similarity).By similarity
Ubiquitinated by CBLB in activated T-cells.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ62077
MaxQBiQ62077
PaxDbiQ62077
PRIDEiQ62077

PTM databases

iPTMnetiQ62077
PhosphoSitePlusiQ62077

Expressioni

Gene expression databases

BgeeiENSMUSG00000016933
CleanExiMM_PLCG1
ExpressionAtlasiQ62077 baseline and differential

Interactioni

Subunit structurei

Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. 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 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, THEMIS and CLNK. Interacts with FLT4 and KIT. Interacts with AXL (By similarity). Interacts with SYK; activates PLCG1 (By similarity). Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with TESPA1 (By similarity). Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1.By similarity14 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • glutamate receptor binding Source: MGI
  • neurotrophin TRKA receptor binding Source: MGI
  • protein kinase binding Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi20223811 interactors.
CORUMiQ62077
DIPiDIP-29284N
IntActiQ62077 23 interactors.
MINTiQ62077
STRINGi10090.ENSMUSP00000099404

Structurei

3D structure databases

ProteinModelPortaliQ62077
SMRiQ62077
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 142PH 1PROSITE-ProRule annotationAdd BLAST116
Domaini152 – 187EF-handPROSITE-ProRule annotationAdd BLAST36
Domaini320 – 464PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini489 – 523PH 2; first partPROSITE-ProRule annotationAdd BLAST35
Domaini550 – 657SH2 1PROSITE-ProRule annotationAdd BLAST108
Domaini668 – 756SH2 2PROSITE-ProRule annotationAdd BLAST89
Domaini791 – 851SH3PROSITE-ProRule annotationAdd BLAST61
Domaini895 – 931PH 2; second partPROSITE-ProRule annotationAdd BLAST37
Domaini953 – 1070PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST118
Domaini1075 – 1177C2PROSITE-ProRule annotationAdd BLAST103

Domaini

The SH3 domain mediates interaction with RALGPS1 (By similarity). The SH3 domain also mediates interaction with CLNK.By similarity1 Publication

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG1264 Eukaryota
ENOG410XPXE LUCA
GeneTreeiENSGT00730000110782
HOGENOMiHOG000230864
HOVERGENiHBG053611
InParanoidiQ62077
KOiK01116
OMAiPMPTFKC
OrthoDBiEOG091G07R3
PhylomeDBiQ62077
TreeFamiTF313216

Family and domain databases

CDDicd09932 SH2_C-SH2_PLC_gamma_like, 1 hit
cd10341 SH2_N-SH2_PLC_gamma_like, 1 hit
cd11970 SH3_PLCgamma1, 1 hit
Gene3Di2.30.29.301 hit
2.60.40.1501 hit
3.20.20.1902 hits
3.30.505.102 hits
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR001192 PI-PLC_fam
IPR016279 PLC-gamma
IPR028380 PLC-gamma1
IPR035023 PLC-gamma_C-SH2
IPR035024 PLC-gamma_N-SH2
IPR017946 PLC-like_Pdiesterase_TIM-brl
IPR035724 PLCgamma1_SH3
IPR000909 PLipase_C_PInositol-sp_X_dom
IPR001711 PLipase_C_Pinositol-sp_Y
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PANTHERiPTHR10336 PTHR10336, 1 hit
PTHR10336:SF52 PTHR10336:SF52, 1 hit
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF00388 PI-PLC-X, 1 hit
PF00387 PI-PLC-Y, 1 hit
PF00017 SH2, 2 hits
PF00018 SH3_1, 1 hit
PIRSFiPIRSF000952 PLC-gamma, 1 hit
PRINTSiPR00390 PHPHLIPASEC
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00239 C2, 1 hit
SM00233 PH, 3 hits
SM00148 PLCXc, 1 hit
SM00149 PLCYc, 1 hit
SM00252 SH2, 2 hits
SM00326 SH3, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
SSF51695 SSF51695, 2 hits
SSF55550 SSF55550, 2 hits
PROSITEiView protein in PROSITE
PS50004 C2, 1 hit
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS50003 PH_DOMAIN, 2 hits
PS50007 PIPLC_X_DOMAIN, 1 hit
PS50008 PIPLC_Y_DOMAIN, 1 hit
PS50001 SH2, 2 hits
PS50002 SH3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT GERPEHCQVS
260 270 280 290 300
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS STELHSSEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI
860 870 880 890 900
NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE
1260 1270 1280 1290 1300
ARYQQPFEDF RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC

SL
Length:1,302
Mass (Da):149,668
Last modified:January 24, 2006 - v2
Checksum:i5D123C508D425EB2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti966D → A in CAA64639 (PubMed:8687404).Curated1
Sequence conflicti984P → R in CAA64639 (PubMed:8687404).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC065091 mRNA Translation: AAH65091.1
X95346 mRNA Translation: CAA64639.1
CCDSiCCDS16996.1
RefSeqiNP_067255.2, NM_021280.3
UniGeneiMm.44463

Genome annotation databases

EnsembliENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933
GeneIDi18803
KEGGimmu:18803
UCSCiuc008nra.1 mouse

Similar proteinsi

Entry informationi

Entry nameiPLCG1_MOUSE
AccessioniPrimary (citable) accession number: Q62077
Secondary accession number(s): Q6P1G1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 24, 2006
Last modified: March 28, 2018
This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome