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P08487 (PLCG1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

EC=3.1.4.11
Alternative name(s):
PLC-148
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-II
Short name=PLC-II
Phospholipase C-gamma-1
Short name=PLC-gamma-1
Gene names
Name:PLCG1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Cofactor

Calcium.

Enzyme regulation

Activated by phosphorylation on tyrosine residues By similarity.

Subunit structure

Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. 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 By similarity. Interacts with RALGPS1. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated) By similarity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT By similarity. Interacts (via SH2 domain) with RET. Interacts (via SH2 domain) with PDGFRA (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding) By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity. Ref.4 Ref.6

Subcellular location

Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment By similarity.

Domain

The SH3 domain mediates interaction with CLNK and RALGPS1 By similarity.

Post-translational modification

May be dephosphorylated by PTPRJ By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine phosphorylated in response to signaling via activated FLT1, FLT3, PDGFRA, PDGFRB and KIT. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells By similarity. Ref.2 Ref.3 Ref.5

Ubiquitinated by CBLB in activated T-cells By similarity.

Sequence similarities

Contains 1 C2 domain.

Contains 1 EF-hand domain.

Contains 2 PH domains.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell projection
   DomainRepeat
SH2 domain
SH3 domain
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Transducer
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from sequence or structural similarity. Source: AgBase

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCOP9 signalosome

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 16410013PubMed 16467851PubMed 7876130Ref.7PubMed 8555205. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBLP226813EBI-8013886,EBI-518228From a different organism.
LATO43561-24EBI-8013886,EBI-8070286From a different organism.
LCP2Q130945EBI-8013886,EBI-346946From a different organism.
PDGFRBP096193EBI-8013886,EBI-641237From a different organism.
SykP480254EBI-8013886,EBI-300116From a different organism.
VAV1P154984EBI-8013886,EBI-625518From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 129112901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
PRO_0000088497

Regions

Domain27 – 142116PH 1
Domain152 – 18736EF-hand
Domain320 – 464145PI-PLC X-box
Domain489 – 52335PH 2; first part
Domain550 – 657108SH2 1
Domain668 – 75689SH2 2
Domain791 – 85161SH3
Domain895 – 93137PH 2; second part
Domain953 – 1070118PI-PLC Y-box
Domain1075 – 1177103C2
Calcium binding165 – 17612 Potential

Sites

Active site3351 By similarity
Active site3801 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue5061Phosphotyrosine By similarity
Modified residue7711Phosphotyrosine; by SYK Ref.2 Ref.3
Modified residue7751Phosphotyrosine By similarity
Modified residue7831Phosphotyrosine; alternate Ref.2 Ref.3 Ref.5
Modified residue7831Phosphotyrosine; by ITK, SYK and TXK; alternate By similarity
Modified residue9771Phosphotyrosine By similarity
Modified residue12221Phosphoserine By similarity
Modified residue12491Phosphoserine By similarity
Modified residue12541Phosphotyrosine Ref.2 Ref.3 Ref.5

Secondary structure

.......................... 1291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08487 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 9F31C7DAA3F8EA77

FASTA1,291148,313
        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 

« Hide

References

[1]"Sequence similarity of phospholipase C with the non-catalytic region of src."
Stahl M.L., Ferenz C.R., Kelleher K.L., Kriz R.W., Knopf J.L.
Nature 332:269-272(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro."
Kim J.W., Sim S.S., Kim U.H., Nishibe S., Whal M.I., Carpenter G., Rhee S.G.
J. Biol. Chem. 265:3940-3943(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
[3]"Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells."
Whal M.I., Nishibe S., Kim J.W., Kim H.K., Rhee S.G., Carpenter G.
J. Biol. Chem. 265:3944-3948(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
[4]"Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors."
Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.
Science 250:979-982(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA.
[5]"PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254."
Kim H.K., Kim J.W., Zilberstein A., Margolis B., Kim J.G., Schlessinger J., Rhee S.G.
Cell 65:435-441(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254.
[6]"Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7."
Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M.
J. Biol. Chem. 271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RET.
[7]"Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide."
Pascal S.M., Singer A.U., Gish G., Yamazaki T., Shoelson S.E., Pawson T., Kay L.E., Forman-Kay J.D.
Cell 77:461-472(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 663-759.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00301 mRNA. Translation: CAA68406.1.
PIRS00666.
RefSeqNP_776850.1. NM_174425.3.
UniGeneBt.307.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCINMR-A663-759[»]
2PLDNMR-A663-759[»]
2PLENMR-A663-759[»]
ProteinModelPortalP08487.
SMRP08487. Positions 489-658, 663-759, 790-933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-42760N.
IntActP08487. 8 interactions.
MINTMINT-2837008.
STRING9913.ENSBTAP00000023383.

Chemistry

BindingDBP08487.
ChEMBLCHEMBL5566.

Proteomic databases

PRIDEP08487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281987.
KEGGbta:281987.

Organism-specific databases

CTD5335.

Phylogenomic databases

eggNOGNOG268751.
HOGENOMHOG000230864.
HOVERGENHBG053611.
InParanoidP08487.
KOK01116.

Family and domain databases

Gene3D2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProIPR000008. C2_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 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]
PIRSFPIRSF000952. PLC-gamma. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50004. 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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08487.
NextBio20805855.

Entry information

Entry namePLCG1_BOVIN
AccessionPrimary (citable) accession number: P08487
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references