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

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P08487 (PLCG1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 148. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

PLCG1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1291 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › lamellipodium By similarity. Cell projection › ruffle 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 process	Lipid degradation Lipid metabolism
Cellular component	Cell projection
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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_component	lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from sequence or structural similarity. Source: UniProtKB signalosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1291

1291

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

PRO_0000088497

Regions

Domain

27 – 142

116

PH 1

Domain

152 – 187

EF-hand

Domain

320 – 464

145

PI-PLC X-box

Domain

489 – 523

PH 2; first part

Domain

550 – 657

108

SH2 1

Domain

668 – 756

SH2 2

Domain

791 – 851

SH3

Domain

895 – 931

PH 2; second part

Domain

953 – 1070

118

PI-PLC Y-box

Domain

1075 – 1177

103

Calcium binding

165 – 176

Potential

Sites

Active site

335

By similarity

Active site

380

By similarity

Amino acid modifications

Modified residue

379

Phosphotyrosine By similarity

Modified residue

481

Phosphotyrosine By similarity

Modified residue

506

Phosphotyrosine By similarity

Modified residue

771

Phosphotyrosine; by SYK Ref.2 Ref.3

Modified residue

775

Phosphotyrosine By similarity

Modified residue

783

Phosphotyrosine; alternate Ref.2 Ref.3 Ref.5

Modified residue

783

Phosphotyrosine; by ITK, SYK and TXK; alternate By similarity

Modified residue

977

Phosphotyrosine By similarity

Modified residue

1222

Phosphoserine By similarity

Modified residue

1249

Phosphoserine By similarity

Modified residue

1254

Phosphotyrosine Ref.2 Ref.3 Ref.5

Modified residue

1264

Phosphoserine By similarity

Secondary structure

1291

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08487 [UniParc].

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

FASTA

1,291

148,313

        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.

IPI

IPI00717084.

PIR

S00666.

RefSeq

NP_776850.1. NM_174425.3.

UniGene

Bt.307.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FCI	NMR	-	A	663-759	[»]
2PLD	NMR	-	A	663-759	[»]
2PLE	NMR	-	A	663-759	[»]

ProteinModelPortal

P08487.

SMR

P08487. Positions 489-658, 663-759, 790-933.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42760N.

MINT

MINT-2837008.

STRING

9913.ENSBTAP00000023383.

Proteomic databases

PRIDE

P08487.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

281987.

KEGG

bta:281987.

Organism-specific databases

CTD

5335.

Phylogenomic databases

eggNOG

NOG268751.

HOGENOM

HOG000230864.

HOVERGEN

HBG053611.

InParanoid

P08487.

K01116.

OrthoDB

EOG4320X7.

Family and domain databases

Gene3D

2.30.29.30. 3 hits.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
IPR001192. Pinositol_PLipase_C.
IPR016279. PLC-gamma.
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]

PANTHER

PTHR10336. PTHR10336. 1 hit.

Pfam

PF00168. C2. 1 hit.
PF09279. efhand_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]

PIRSF

PIRSF000952. PLC-gamma. 1 hit.

PRINTS

PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.

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.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
SSF50044. SH3. 1 hit.

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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08487.

ChEMBL

CHEMBL5566.

EvolutionaryTrace

P08487.

NextBio

20805855.

Entry information

Entry name

PLCG1_BOVIN

Accession

Primary (citable) accession number: P08487

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents