Reviewed, UniProtKB/Swiss-Prot P08487 (PLCG1_BOVIN)

Names and origin

Protein names

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
    Phospholipase C-II
      Short name=PLC-II
    PLC-148

Gene names

Name:

PLCG1

Organism

Bos taurus (Bovine)

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.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Subunit structure	Interacts with AGAP2 via its SH3 domain. Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro-rich domain of TNK1 via its SH3 domain. 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 its 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 By similarity.
Domain	The SH3 domain mediates interaction with CLNK and RALGPS1 By similarity.
Post-translational modification	The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. 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
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	in utero embryonic development Inferred from sequence or structural similarity. Source: AgBase intracellular signaling cascade Inferred from electronic annotation. Source: InterPro phospholipid catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from electronic annotation. Source: EC 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 1291

1290

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

PRO_0000088497

Regions

Domain

27 – 142

116

PH 1

Domain

152 – 187

36

EF-hand

Domain

320 – 464

145

PI-PLC X-box

Domain

489 – 523

35

PH 2; first part

Domain

550 – 657

108

SH2 1

Domain

668 – 756

89

SH2 2

Domain

791 – 851

61

SH3

Domain

895 – 931

37

PH 2; second part

Domain

953 – 1070

118

PI-PLC Y-box

Domain

1075 – 1177

103

C2

Calcium binding

165 – 176

12

Potential

Sites

Active site

335

1

By similarity

Active site

380

1

By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

6

1

Phosphoserine By similarity

Modified residue

379

1

Phosphotyrosine By similarity

Modified residue

481

1

Phosphotyrosine By similarity

Modified residue

506

1

Phosphotyrosine By similarity

Modified residue

525

1

Phosphoserine By similarity

Modified residue

771

1

Phosphotyrosine Ref.2 Ref.3

Modified residue

775

1

Phosphotyrosine By similarity

Modified residue

783

1

Phosphotyrosine Ref.2 Ref.3 Ref.4

Modified residue

977

1

Phosphotyrosine By similarity

Modified residue

1222

1

Phosphoserine By similarity

Modified residue

1249

1

Phosphoserine By similarity

Modified residue

1254

1

Phosphotyrosine Ref.2 Ref.3 Ref.4

Modified residue

1264

1

Phosphoserine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1291

Helix Strand Turn

Details...

Beta strand

667 – 670

4

Helix

677 – 684

8

Beta strand

690 – 695

6

Beta strand

697 – 708

12

Beta strand

711 – 713

3

Beta strand

716 – 719

4

Beta strand

721 – 725

5

Beta strand

727 – 732

6

Helix

734 – 741

8

Beta strand

746 – 749

4

Sequences

	Sequence		Length	Mass (Da)
	P08487-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 9F31C7DAA3F8EA77	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

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: 2831461] [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: 1689310] [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: 1689311] [Abstract] Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
[4]	"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: 1708307] [Abstract] Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254.
[5]	"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: 8181064] [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.

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	[»]

SMR

P08487. Positions 489-553, 542-658, 790-855, 851-933.

ModBase

Search...

Protein-protein interaction databases

STRING

P08487.

Proteomic databases

PRIDE

P08487.

Genome annotation databases

Ensembl

ENSBTAT00000023383; ENSBTAP00000023383; ENSBTAG00000017584; Bos taurus. [Genome view]

GeneID

281987.

KEGG

bta:281987.

Organism-specific databases

CTD

281987.

Phylogenomic databases

eggNOG

maNOG14009.

HOVERGEN

P08487.

InParanoid

P08487.

Enzyme and pathway databases

BRENDA

3.1.4.11. 251.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR011993. PH_type.
IPR015359. Phospholipase_C_EF-hand-like.
IPR001192. Phospholipase_C_Pinositol-sp_C.
IPR001711. Phospholipase_C_Pinositol-sp_Y.
IPR016279. PLC-gamma.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 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]

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...

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:	February 9, 2010
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)