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Entry version 209 (18 Sep 2019)
Sequence version 1 (01 Jul 1989)
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Protein

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

Gene

Plcg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by phosphorylation on tyrosine residues.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei335PROSITE-ProRule annotation1
Active sitei380PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi165 – 176PROSITE-ProRule annotationAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Transducer
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.11 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1169408 ISG15 antiviral mechanism
R-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol
R-RNO-186763 Downstream signal transduction
R-RNO-202433 Generation of second messenger molecules
R-RNO-2029485 Role of phospholipids in phagocytosis
R-RNO-212718 EGFR interacts with phospholipase C-gamma
R-RNO-2424491 DAP12 signaling
R-RNO-2871796 FCERI mediated MAPK activation
R-RNO-2871809 FCERI mediated Ca+2 mobilization
R-RNO-5218921 VEGFR2 mediated cell proliferation
R-RNO-5654219 Phospholipase C-mediated cascade: FGFR1
R-RNO-5654221 Phospholipase C-mediated cascade, FGFR2
R-RNO-5654227 Phospholipase C-mediated cascade, FGFR3
R-RNO-5654228 Phospholipase C-mediated cascade, FGFR4
R-RNO-8853659 RET signaling
R-RNO-9026527 Activated NTRK2 signals through PLCG1
R-RNO-9034793 Activated NTRK3 signals through PLCG1

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000960

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Plcg1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3347 Plcg1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi842P → L: Inhibits interaction with AGAP2. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5188

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000885002 – 12901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1Add BLAST1289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei506PhosphotyrosineBy similarity1
Modified residuei771Phosphotyrosine; by SYKBy similarity1
Modified residuei775PhosphotyrosineBy similarity1
Modified residuei783Phosphotyrosine; by ITK, SYK and TXKBy similarity1
Modified residuei977PhosphotyrosineBy similarity1
Modified residuei1221PhosphoserineCombined sources1
Modified residuei1227PhosphoserineBy similarity1
Modified residuei1233PhosphoserineBy similarity1
Modified residuei1248PhosphoserineCombined sources1
Modified residuei1253PhosphotyrosineBy similarity1
Modified residuei1263PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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, KIT and PDGFRB. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells (By similarity).By similarity
Ubiquitinated by CBLB in activated T-cells.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P10686

PRoteomics IDEntifications database

More...
PRIDEi
P10686

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10686

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P10686

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P10686

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites).

Interacts (via SH2 domain) with RET (By similarity).

Interacts with FLT1 (tyrosine-phosphorylated).

Interacts with AXL, FLT4 and KIT.

Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated) (By similarity).

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).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247766, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P10686

Database of interacting proteins

More...
DIPi
DIP-2863N

Protein interaction database and analysis system

More...
IntActi
P10686, 14 interactors

Molecular INTeraction database

More...
MINTi
P10686

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000022276

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P10686

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P10686

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10686

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 142PH 1PROSITE-ProRule annotationAdd BLAST116
Domaini152 – 187EF-handPROSITE-ProRule annotationAdd BLAST36
Domaini320 – 464PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini489 – 523PH 2; first partPROSITE-ProRule annotationAdd BLAST35
Domaini550 – 657SH2 1PROSITE-ProRule annotationAdd BLAST108
Domaini668 – 756SH2 2PROSITE-ProRule annotationAdd BLAST89
Domaini791 – 851SH3PROSITE-ProRule annotationAdd BLAST61
Domaini895 – 931PH 2; second partPROSITE-ProRule annotationAdd BLAST37
Domaini953 – 1070PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST118
Domaini1075 – 1177C2PROSITE-ProRule annotationAdd BLAST103

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1264 Eukaryota
ENOG410XPXE LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230864

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10686

KEGG Orthology (KO)

More...
KOi
K01116

Database of Orthologous Groups

More...
OrthoDBi
368239at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10686

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09932 SH2_C-SH2_PLC_gamma_like, 1 hit
cd10341 SH2_N-SH2_PLC_gamma_like, 1 hit
cd11970 SH3_PLCgamma1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 1 hit
2.60.40.150, 1 hit
3.20.20.190, 2 hits
3.30.505.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR001192 PI-PLC_fam
IPR016279 PLC-gamma
IPR028380 PLC-gamma1
IPR035023 PLC-gamma_C-SH2
IPR035024 PLC-gamma_N-SH2
IPR017946 PLC-like_Pdiesterase_TIM-brl
IPR035724 PLCgamma1_SH3
IPR000909 PLipase_C_PInositol-sp_X_dom
IPR001711 PLipase_C_Pinositol-sp_Y
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

The PANTHER Classification System

More...
PANTHERi
PTHR10336 PTHR10336, 1 hit
PTHR10336:SF173 PTHR10336:SF173, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00168 C2, 1 hit
PF00388 PI-PLC-X, 1 hit
PF00387 PI-PLC-Y, 1 hit
PF00017 SH2, 2 hits
PF00018 SH3_1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000952 PLC-gamma, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00390 PHPHLIPASEC
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in 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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
SSF51695 SSF51695, 1 hit
SSF55550 SSF55550, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P10686-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT GERPELCQVS
260 270 280 290 300
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSSEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI
860 870 880 890 900
NPAILEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGTSLRE RASDASSQLF HVRAREGSFE
1260 1270 1280 1290
ARYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
Length:1,290
Mass (Da):148,548
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBB3240C27972CE3B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V845G3V845_RAT
1-phosphatidylinositol 4,5-bisphosp...
Plcg1 rCG_32419
1,290Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J03806 mRNA Translation: AAA41921.1
L14476 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

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PIRi
A31317

NCBI Reference Sequences

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RefSeqi
NP_037319.1, NM_013187.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
25738

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25738

UCSC genome browser

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UCSCi
RGD:3347 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03806 mRNA Translation: AAA41921.1
L14476 Genomic DNA No translation available.
PIRiA31317
RefSeqiNP_037319.1, NM_013187.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y0MX-ray1.20A791-851[»]
1YWOX-ray1.81A790-851[»]
1YWPX-ray1.60A790-851[»]
2FJLNMR-A489-547[»]
A851-933[»]
3GQIX-ray2.50B545-770[»]
4K44X-ray1.70A/B664-766[»]
4K45X-ray1.50A664-766[»]
B770-787[»]
5EG3X-ray2.61B661-773[»]
SMRiP10686
ModBaseiSearch...

Protein-protein interaction databases

BioGridi247766, 3 interactors
CORUMiP10686
DIPiDIP-2863N
IntActiP10686, 14 interactors
MINTiP10686
STRINGi10116.ENSRNOP00000022276

Chemistry databases

BindingDBiP10686
ChEMBLiCHEMBL5188
SwissLipidsiSLP:000000960

PTM databases

iPTMnetiP10686
PhosphoSitePlusiP10686

Proteomic databases

PaxDbiP10686
PRIDEiP10686

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25738
KEGGirno:25738
UCSCiRGD:3347 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5335
RGDi3347 Plcg1

Phylogenomic databases

eggNOGiKOG1264 Eukaryota
ENOG410XPXE LUCA
HOGENOMiHOG000230864
InParanoidiP10686
KOiK01116
OrthoDBi368239at2759
PhylomeDBiP10686

Enzyme and pathway databases

BRENDAi3.1.4.11 5301
ReactomeiR-RNO-1169408 ISG15 antiviral mechanism
R-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol
R-RNO-186763 Downstream signal transduction
R-RNO-202433 Generation of second messenger molecules
R-RNO-2029485 Role of phospholipids in phagocytosis
R-RNO-212718 EGFR interacts with phospholipase C-gamma
R-RNO-2424491 DAP12 signaling
R-RNO-2871796 FCERI mediated MAPK activation
R-RNO-2871809 FCERI mediated Ca+2 mobilization
R-RNO-5218921 VEGFR2 mediated cell proliferation
R-RNO-5654219 Phospholipase C-mediated cascade: FGFR1
R-RNO-5654221 Phospholipase C-mediated cascade, FGFR2
R-RNO-5654227 Phospholipase C-mediated cascade, FGFR3
R-RNO-5654228 Phospholipase C-mediated cascade, FGFR4
R-RNO-8853659 RET signaling
R-RNO-9026527 Activated NTRK2 signals through PLCG1
R-RNO-9034793 Activated NTRK3 signals through PLCG1

Miscellaneous databases

EvolutionaryTraceiP10686
PMAP-CutDBiP10686

Protein Ontology

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PROi
PR:P10686

Family and domain databases

CDDicd09932 SH2_C-SH2_PLC_gamma_like, 1 hit
cd10341 SH2_N-SH2_PLC_gamma_like, 1 hit
cd11970 SH3_PLCgamma1, 1 hit
Gene3Di2.30.29.30, 1 hit
2.60.40.150, 1 hit
3.20.20.190, 2 hits
3.30.505.10, 2 hits
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR001192 PI-PLC_fam
IPR016279 PLC-gamma
IPR028380 PLC-gamma1
IPR035023 PLC-gamma_C-SH2
IPR035024 PLC-gamma_N-SH2
IPR017946 PLC-like_Pdiesterase_TIM-brl
IPR035724 PLCgamma1_SH3
IPR000909 PLipase_C_PInositol-sp_X_dom
IPR001711 PLipase_C_Pinositol-sp_Y
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PANTHERiPTHR10336 PTHR10336, 1 hit
PTHR10336:SF173 PTHR10336:SF173, 1 hit
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF00388 PI-PLC-X, 1 hit
PF00387 PI-PLC-Y, 1 hit
PF00017 SH2, 2 hits
PF00018 SH3_1, 1 hit
PIRSFiPIRSF000952 PLC-gamma, 1 hit
PRINTSiPR00390 PHPHLIPASEC
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
SMARTiView protein in 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
SUPFAMiSSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
SSF51695 SSF51695, 1 hit
SSF55550 SSF55550, 2 hits
PROSITEiView protein in 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLCG1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10686
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 18, 2019
This is version 209 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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