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P08487

- PLCG1_BOVIN

UniProt

P08487 - PLCG1_BOVIN

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Protein
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Gene
PLCG1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - 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 By similarity.

Catalytic activityi

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

Cofactori

Calcium.

Enzyme regulationi

Activated by phosphorylation on tyrosine residues By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei335 – 3351 By similarity
Active sitei380 – 3801 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi165 – 17612 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
  4. signal transducer activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. cellular response to epidermal growth factor stimulus Source: UniProtKB
  2. in utero embryonic development Source: AgBase
  3. intracellular signal transduction Source: InterPro
  4. phospholipid catabolic process Source: InterPro
  5. positive regulation of epithelial cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PLCG1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

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.

GO - Cellular componenti

  1. COP9 signalosome Source: UniProtKB
  2. lamellipodium Source: UniProtKB
  3. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 129112901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
PRO_0000088497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei506 – 5061Phosphotyrosine By similarity
Modified residuei771 – 7711Phosphotyrosine; by SYK2 Publications
Modified residuei775 – 7751Phosphotyrosine By similarity
Modified residuei783 – 7831Phosphotyrosine; alternate3 Publications
Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK; alternate By similarity
Modified residuei977 – 9771Phosphotyrosine By similarity
Modified residuei1222 – 12221Phosphoserine By similarity
Modified residuei1249 – 12491Phosphoserine By similarity
Modified residuei1254 – 12541Phosphotyrosine3 Publications

Post-translational modificationi

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.3 Publications
Ubiquitinated by CBLB in activated T-cells By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP08487.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

DIPiDIP-42760N.
IntActiP08487. 8 interactions.
MINTiMINT-2837008.
STRINGi9913.ENSBTAP00000023383.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi664 – 6663
Beta strandi667 – 6704
Beta strandi671 – 6733
Helixi676 – 6849
Beta strandi685 – 6884
Beta strandi691 – 6955
Beta strandi697 – 7004
Beta strandi702 – 7087
Beta strandi711 – 7133
Beta strandi716 – 7183
Beta strandi721 – 7255
Beta strandi727 – 7326
Helixi735 – 7439
Beta strandi746 – 7494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCINMR-A663-759[»]
2PLDNMR-A663-759[»]
2PLENMR-A663-759[»]
ProteinModelPortaliP08487.
SMRiP08487. Positions 489-658, 663-759, 790-933.

Miscellaneous databases

EvolutionaryTraceiP08487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 142116PH 1
Add
BLAST
Domaini152 – 18736EF-hand
Add
BLAST
Domaini320 – 464145PI-PLC X-box
Add
BLAST
Domaini489 – 52335PH 2; first part
Add
BLAST
Domaini550 – 657108SH2 1
Add
BLAST
Domaini668 – 75689SH2 2
Add
BLAST
Domaini791 – 85161SH3
Add
BLAST
Domaini895 – 93137PH 2; second part
Add
BLAST
Domaini953 – 1070118PI-PLC Y-box
Add
BLAST
Domaini1075 – 1177103C2
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 EF-hand domain.
Contains 2 PH domains.
Contains 2 SH2 domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP08487.
KOiK01116.

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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
PfamiPF00168. 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]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00239. 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]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. 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]

Sequencei

Sequence statusi: Complete.

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

P08487-1 [UniParc]FASTAAdd to Basket

« Hide

MAGAASPCAN GCGPSAPSDA EVVHLCRSLE VGTVMTLFYS KKSQRPERKT     50
FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIRGLTWL MEDTLQAATP 150
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
LEQRTSDITY GQFAQLYRSL MYSAQKTMDL PFLEASALRA GERPELCRVS 250
LPEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 300
FLFSKENSIW NSQLDEVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVDIAADGLP 450
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP 500
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSNEKW 550
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 600
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE 650
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN 700
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM 750
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF 800
DYKAQREDEL TFTKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV 850
SPAALEPERE HLDENSPLGD LLRGVLDVPA CQIAVRPEGK NNRLFVFSIS 900
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA 950
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF 1000
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN 1050
QALFLAGGHC GYVLQPSVMR DEAFDPFDKS SLRGLEPCAI CIEVLGARHL 1100
PKNGRGIVCP FVEIEVAGAE YDSIKQKTEF VVDNGLNPVW PAKPFHFQIS 1150
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEGL 1200
ELASLLVKID VFPAKQENGD LSPFGGASLR ERSCDASGPL FHGRAREGSF 1250
EARYQQPFED FRISQEHLAD HFDGRDRRTP RRTRVNGDNR L 1291
Length:1,291
Mass (Da):148,313
Last modified:August 1, 1988 - v1
Checksum:i9F31C7DAA3F8EA77
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00301 mRNA. Translation: CAA68406.1.
PIRiS00666.
RefSeqiNP_776850.1. NM_174425.3.
UniGeneiBt.307.

Genome annotation databases

GeneIDi281987.
KEGGibta:281987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00301 mRNA. Translation: CAA68406.1 .
PIRi S00666.
RefSeqi NP_776850.1. NM_174425.3.
UniGenei Bt.307.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FCI NMR - A 663-759 [» ]
2PLD NMR - A 663-759 [» ]
2PLE NMR - A 663-759 [» ]
ProteinModelPortali P08487.
SMRi P08487. Positions 489-658, 663-759, 790-933.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-42760N.
IntActi P08487. 8 interactions.
MINTi MINT-2837008.
STRINGi 9913.ENSBTAP00000023383.

Chemistry

BindingDBi P08487.
ChEMBLi CHEMBL5566.

Proteomic databases

PRIDEi P08487.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281987.
KEGGi bta:281987.

Organism-specific databases

CTDi 5335.

Phylogenomic databases

eggNOGi NOG268751.
HOGENOMi HOG000230864.
HOVERGENi HBG053611.
InParanoidi P08487.
KOi K01116.

Miscellaneous databases

EvolutionaryTracei P08487.
NextBioi 20805855.

Family and domain databases

Gene3Di 2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProi IPR000008. C2_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
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 ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
Pfami PF00168. 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 ]
PIRSFi PIRSF000952. PLC-gamma. 1 hit.
PRINTSi PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi SM00239. 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 ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPLCG1_BOVIN
AccessioniPrimary (citable) accession number: P08487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 159 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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