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Entry version 220 (02 Jun 2021)
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) (PubMed:7531435).

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, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:7531435).

Plays a role in actin reorganization and cell migration (By similarity).

By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

    1. Vmax=13.8 µmol/min/mg enzyme toward phosphatidylinositol1 Publication
    2. Vmax=0.6 µmol/min/mg enzyme toward 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate)1 Publication

    pH dependencei

    Optimum pH is 5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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-1Curated (EC:3.1.4.111 Publication)
    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%5Fand%5Ftaxonomy%5Fsection">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:Plcg1Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    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%5Fand%5Fbiotech%5Fsection">'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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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

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

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with AGAP2 via its SH3 domain.

    Interacts (via SH2 domain) with RET.

    Interacts with FLT1 (tyrosine-phosphorylated) (By similarity).

    Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated).

    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 AXL, FLT4 and KIT.

    Interacts with RALGPS1.

    Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites).

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

    Interacts with PIP5K1C (By similarity).

    Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding).

    Interacts with SYK; activates PLCG1.

    Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By similarity).

    Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome (By similarity).

    By similarity

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    247766, 5 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, 27 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

    More...
    SMRi
    P10686

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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%5Fand%5Fdomains%5Fsection">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
    Domaini1071 – 1194C2PROSITE-ProRule annotationAdd BLAST124

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni522 – 546DisorderedSequence analysisAdd BLAST25
    Regioni1271 – 1290DisorderedSequence analysisAdd BLAST20

    <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 (By similarity). The SH3 domain also mediates interaction with RALGPS1 (By similarity).By similarity

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1264, Eukaryota

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P10686

    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

    Database of protein disorder

    More...
    DisProti
    DP01851

    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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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: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>

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A31317

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_037319.1, NM_013187.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    25738

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:25738

    UCSC genome browser

    More...
    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

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    6PBCX-ray2.46A21-200[»]
    A791-1215[»]
    SMRiP10686
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi247766, 5 interactors
    CORUMiP10686
    DIPiDIP-2863N
    IntActiP10686, 27 interactors
    MINTiP10686
    STRINGi10116.ENSRNOP00000022276

    Chemistry databases

    BindingDBiP10686
    ChEMBLiCHEMBL5188
    SwissLipidsiSLP:000000960

    PTM databases

    iPTMnetiP10686
    PhosphoSitePlusiP10686

    Proteomic databases

    PaxDbiP10686
    PRIDEiP10686

    Genome annotation databases

    GeneIDi25738
    KEGGirno:25738
    UCSCiRGD:3347, rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5335
    RGDi3347, Plcg1

    Phylogenomic databases

    eggNOGiKOG1264, Eukaryota
    InParanoidiP10686
    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

    Protein Ontology

    More...
    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
    DisProtiDP01851
    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

    MobiDB: a database of protein disorder and mobility annotations

    More...
    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%5Fand%5Fisoforms">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: June 2, 2021
    This is version 220 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, Reference proteome

    Documents

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