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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

Gene

Plcg2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling (By similarity).By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei327PROSITE-ProRule annotation1
Active sitei372PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • activation of store-operated calcium channel activity Source: MGI
  • B cell differentiation Source: UniProtKB
  • B cell receptor signaling pathway Source: UniProtKB
  • follicular B cell differentiation Source: MGI
  • inositol trisphosphate biosynthetic process Source: MGI
  • intracellular signal transduction Source: InterPro
  • negative regulation of programmed cell death Source: MGI
  • phosphatidylinositol biosynthetic process Source: UniProtKB
  • phospholipid catabolic process Source: InterPro
  • positive regulation of receptor internalization Source: CACAO
  • positive regulation of type I interferon production Source: CACAO
  • regulation of gene expression Source: MGI
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • response to lipopolysaccharide Source: MGI
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.1.4.11. 3474.
ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-5607764. CLEC7A (Dectin-1) 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-2 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-gamma-2
Phospholipase C-gamma-2
Short name:
PLC-gamma-2
Gene namesi
Name:Plcg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:97616. Plcg2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3608199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003423641 – 12651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2Add BLAST1265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei753Phosphotyrosine; by BTKCombined sources1
Modified residuei759Phosphotyrosine; by BTKBy similarity1
Modified residuei1197Phosphotyrosine; by BTKBy similarity1
Modified residuei1217PhosphotyrosineCombined sources1
Modified residuei1245PhosphotyrosineCombined sources1

Post-translational modificationi

Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-induced activation of a variety of growth factor receptors and immune system receptors. Phosphorylation leads to increased phospholipase activity (By similarity). Phosphorylated on tyrosine residues by CSF1R.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CIH5.
MaxQBiQ8CIH5.
PaxDbiQ8CIH5.
PeptideAtlasiQ8CIH5.
PRIDEiQ8CIH5.

PTM databases

iPTMnetiQ8CIH5.
PhosphoSitePlusiQ8CIH5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000034330.
GenevisibleiQ8CIH5. MM.

Interactioni

Subunit structurei

Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EporP147532EBI-617954,EBI-617901
Fhl2O704333EBI-617954,EBI-299379
FlnaQ8BTM83EBI-617954,EBI-641991
Fn1P112766EBI-617954,EBI-641955
Inpp5dQ9ES523EBI-617954,EBI-300210
LynP259112EBI-617954,EBI-643537
Pdcd6ipQ9WU787EBI-617954,EBI-641897
Trim27Q621584EBI-617954,EBI-642025
Zbtb7bQ643213EBI-617954,EBI-642868

Protein-protein interaction databases

DIPiDIP-33368N.
IntActiQ8CIH5. 32 interactors.
MINTiMINT-1348529.
STRINGi10090.ENSMUSP00000079991.

Structurei

Secondary structure

11265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi523 – 525Combined sources3
Helixi540 – 551Combined sources12
Turni552 – 555Combined sources4
Beta strandi561 – 565Combined sources5
Beta strandi567 – 569Combined sources3
Beta strandi573 – 579Combined sources7
Beta strandi582 – 593Combined sources12
Beta strandi596 – 602Combined sources7
Beta strandi607 – 609Combined sources3
Helixi610 – 616Combined sources7
Turni617 – 619Combined sources3
Helixi625 – 627Combined sources3
Beta strandi773 – 778Combined sources6
Beta strandi784 – 786Combined sources3
Beta strandi795 – 798Combined sources4
Beta strandi803 – 805Combined sources3
Beta strandi807 – 811Combined sources5
Beta strandi814 – 819Combined sources6
Helixi821 – 823Combined sources3
Beta strandi824 – 826Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DX0X-ray2.50A/B516-640[»]
2EQINMR-A772-827[»]
ProteinModelPortaliQ8CIH5.
SMRiQ8CIH5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CIH5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 131PHPROSITE-ProRule annotationAdd BLAST131
Domaini312 – 456PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini532 – 635SH2 1PROSITE-ProRule annotationAdd BLAST104
Domaini646 – 735SH2 2PROSITE-ProRule annotationAdd BLAST90
Domaini769 – 829SH3PROSITE-ProRule annotationAdd BLAST61
Domaini930 – 1044PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST115
Domaini1048 – 1152C2PROSITE-ProRule annotationAdd BLAST105

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
GeneTreeiENSGT00730000110782.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiQ8CIH5.
KOiK05859.
OMAiMLMRIPR.
OrthoDBiEOG091G07R3.
PhylomeDBiQ8CIH5.
TreeFamiTF313216.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 2 hits.
PTHR10336:SF25. PTHR10336:SF25. 2 hits.
PfamiPF00168. C2. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 2 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CIH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTMVNVDTL PEYEKSQIKR ALELGTVMTV FNARKSTPER RTVQMIMETR
60 70 80 90 100
QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRH KAECCFTILY
110 120 130 140 150
GTQFVLSTLS LATDSKEDAV KWLSGLKILH QEAMSASTPT MIESWLRKQI
160 170 180 190 200
YSVDQTRRNS ISLRELKTIL PLVNFKVSGI KFLKDKLVEI GAQKDELSFE
210 220 230 240 250
QFHLFYKKLM FDQQKSILDE FKKDSSVFIL GNTDRPDASA VYLQDFQRFL
260 270 280 290 300
LHEQQELWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS
310 320 330 340 350
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR
360 370 380 390 400
AGCRCIELDC WDGPDGKPII YHGWTRTTKI KFDDVVQAIR DHAFVTSSFP
410 420 430 440 450
VILSIEEHCS VEQQRHMAKV FKEVLGDMLL TKPTEASADQ LPSPSQLREK
460 470 480 490 500
IIIKHKKLGP KGDVDVNVED KKDEHKPQGE LYMWDSIDQK WTRHYCAIAD
510 520 530 540 550
AKLSFGDDIE QAVEEEPVQD TPPTELHFGE KWFHKKVESR TSAEKLLQEY
560 570 580 590 600
CAETGAKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMENGVMKYY
610 620 630 640 650
LTDNLTFNSI YALIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDS
660 670 680 690 700
LSRGEAEDML MRIPRDGAFL IRKREGTNSY AITFRARGKV KHCRINRDGR
710 720 730 740 750
HFVLGTSAYF ESLVELVSYY EKHALYRKMR LRYPVTPELL ERYNMERDIN
760 770 780 790 800
SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELTF CRGALIHNVS
810 820 830 840 850
KEPGGWWKGD YGTRIQQYFP SNYVEDISAG DAEEMEKQII EDNPLGSLCK
860 870 880 890 900
GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF
910 920 930 940 950
QSIREITWKM DTKENNMKYW ERNQSIAIEL SDLVVYCKPT SKTKDHLENP
960 970 980 990 1000
DFREIRSFVE TKADSIVRQK PVDLLRYNQK GLTRVYPKGQ RVDSSNYDPF
1010 1020 1030 1040 1050
RLWLCGSQMV ALNFQTPDKY MQMNHALFSL NGRTGYVLQP ESMRSEKYDP
1060 1070 1080 1090 1100
MPLESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDSNKFK
1110 1120 1130 1140 1150
TTVVNDNGLS PVWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH
1160 1170 1180 1190 1200
ATYPIKGIKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC
1210 1220 1230 1240 1250
RQLRRRQEEL NNQLFLYDTH QNLRGANRDA LVKEFNVNEN QLQLYQEKCN
1260
RRLREKRVSN SRFYS
Length:1,265
Mass (Da):147,592
Last modified:March 1, 2003 - v1
Checksum:iE4A2A6AD6F05160E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti787E → G in BAE24959 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK142173 mRNA. Translation: BAE24959.1.
AK151039 mRNA. Translation: BAE30056.1.
BC019654 mRNA. Translation: AAH19654.1.
BC023877 mRNA. Translation: AAH23877.1.
CCDSiCCDS22700.1.
RefSeqiNP_758489.1. NM_172285.2.
UniGeneiMm.192699.

Genome annotation databases

EnsembliENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
GeneIDi234779.
KEGGimmu:234779.
UCSCiuc009npc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK142173 mRNA. Translation: BAE24959.1.
AK151039 mRNA. Translation: BAE30056.1.
BC019654 mRNA. Translation: AAH19654.1.
BC023877 mRNA. Translation: AAH23877.1.
CCDSiCCDS22700.1.
RefSeqiNP_758489.1. NM_172285.2.
UniGeneiMm.192699.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DX0X-ray2.50A/B516-640[»]
2EQINMR-A772-827[»]
ProteinModelPortaliQ8CIH5.
SMRiQ8CIH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-33368N.
IntActiQ8CIH5. 32 interactors.
MINTiMINT-1348529.
STRINGi10090.ENSMUSP00000079991.

Chemistry databases

ChEMBLiCHEMBL3608199.

PTM databases

iPTMnetiQ8CIH5.
PhosphoSitePlusiQ8CIH5.

Proteomic databases

EPDiQ8CIH5.
MaxQBiQ8CIH5.
PaxDbiQ8CIH5.
PeptideAtlasiQ8CIH5.
PRIDEiQ8CIH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
GeneIDi234779.
KEGGimmu:234779.
UCSCiuc009npc.1. mouse.

Organism-specific databases

CTDi5336.
MGIiMGI:97616. Plcg2.

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
GeneTreeiENSGT00730000110782.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiQ8CIH5.
KOiK05859.
OMAiMLMRIPR.
OrthoDBiEOG091G07R3.
PhylomeDBiQ8CIH5.
TreeFamiTF313216.

Enzyme and pathway databases

BRENDAi3.1.4.11. 3474.
ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiQ8CIH5.
PROiQ8CIH5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034330.
GenevisibleiQ8CIH5. MM.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 2 hits.
PTHR10336:SF25. PTHR10336:SF25. 2 hits.
PfamiPF00168. C2. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 2 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCG2_MOUSE
AccessioniPrimary (citable) accession number: Q8CIH5
Secondary accession number(s): Q3UBA8, Q3UQT0, Q8VE69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: March 1, 2003
Last modified: November 30, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.