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UniProtKB - P07379 (PCKGC_RAT)

Entry version 176 (07 Apr 2021)
Sequence version 1 (01 Apr 1988)
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Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

Pck1

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

Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:4186849, PubMed:30193097, PubMed:26322521, PubMed:26709450, PubMed:28345895, PubMed:31461616). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:30193097). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a regulator of formation and maintenance of memory CD8+ T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8+ T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity).By similarity6 Publications

Miscellaneous

In eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one.Curated

<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

Mn2+9 PublicationsNote: Binds 1 Mn2+ ion per subunit.9 Publications

<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

Phosphoenolpyruvate carboxykinase activity is regulated by acetylation and glucose levels (PubMed:30193097). The anaplerotic conversion of phosphoenolpyruvate to oxaloacetate is improved by PCK1 acetylation on Lys-91 (K91ac), Lys-473 (K473ac) and Lys-521 (K521ac) (PubMed:30193097). High glucose concentrations favor PCK1 anaplerotic activity by triggering acetylation on Lys-91 (K91ac). At low glucose levels, SIRT1-mediated deacetylation of Lys-91 promotes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (By similarity). Phosphoenolpyruvate carboxykinase activity is inhibited by 3-mercaptopicolinate (PubMed:26322521). Phosphoenolpyruvate carboxykinase activity is inhibited by 3-[(carboxymethyl)thio]picolinate (CMP), which acts as a competitive inhibitor at the oxaloacetate/phosphoenolpyruvate-binding site (PubMed:31461616). Phosphorylation at Ser-90 reduces the binding affinity to oxaloacetate and converts the enzyme into an atypical protein kinase using GTP as donor (By similarity).By similarity3 Publications

<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

Kcat is 76 sec(-1) with oxaloacetate as substrate (PubMed:30193097). Kcat is 27 sec(-1) with phosphoenolpyruvate as substrate (PubMed:30193097). Kcat is 65 sec(-1) with GTP as substrate (PubMed:30193097). Kcat is 25 sec(-1) with GDP as substrate (PubMed:30193097). Kcat is 52 sec(-1) with phosphoenolpyruvate carboxykinase in the forward reaction (PubMed:26709450). Kcat is 19 sec(-1) with phosphoenolpyruvate carboxykinase in the backward forward reaction (PubMed:26709450).2 Publications
  1. KM=39 µM for oxaloacetate1 Publication
  2. KM=161 µM for GTP1 Publication
  3. KM=301 µM for phosphoenolpyruvate1 Publication
  4. KM=79 µM for GDP1 Publication
  5. KM=475 µM for phosphoenolpyruvate (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
  6. KM=207 µM for GDP (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
  7. KM=435 µM for CO2 (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
  8. KM=51 µM for oxaloacetate (for phosphoenolpyruvate carboxykinase in the forward reaction)1 Publication
  9. KM=55 µM for GTP (for phosphoenolpyruvate carboxykinase in the forward reaction)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei87Substrate5 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi244ManganeseCombined sources10 Publications1
    Metal bindingi264Manganese; via tele nitrogenCombined sources10 Publications1
    Binding sitei286Substrate6 Publications1
    <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 sitei2882 Publications1
    Metal bindingi311ManganeseCombined sources10 Publications1
    Binding sitei405GTPCombined sources7 Publications1
    Binding sitei436GTPCombined sources8 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi287 – 292GTPCombined sources8 Publications6
    Nucleotide bindingi530 – 533GTPCombined sources8 Publications4

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionDecarboxylase, Kinase, Lyase, Transferase
    Biological processGluconeogenesis
    LigandGTP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.1.1.32, 5301

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-RNO-70263, Gluconeogenesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P07379

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00138

    <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:
    Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Curated (EC:4.1.1.325 Publications)
    Short name:
    PEPCK-C
    Alternative name(s):
    Serine-protein kinase PCK1Curated (EC:2.7.11.-By similarity)
    <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:Pck11 PublicationImported
    <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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
    <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: Chromosome 3

    Organism-specific databases

    Rat genome database

    More...    RGDi    		3267, Pck1

    <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

    Cytoplasm, Endoplasmic reticulum

    <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>Mutagenesisi89E → A, D or Q: Abolished phosphoenolpyruvate carboxykinase activity; decreased affinity for oxaloacetate. 1 Publication1
    Mutagenesisi90S → A: Decreased phosphorylation and increased acetylation levels. 1 Publication1
    Mutagenesisi91K → Q: 3-fold decrease of affinity for phosphoenolpyruvate. 1 Publication1
    Mutagenesisi477H → R: Destabilization of the closed state of the omega-loop, resulting in decreased capture rates for the weaker binding substrates associated with catalysis in the phosphoenolpyruvate to oxaloacetate direction. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL1075234

    <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 '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_00001036301 – 622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Add BLAST622

    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 residuei19PhosphoserineCombined sources1
    Modified residuei70N6-acetyllysine; by p300/EP300By similarity1
    Modified residuei71N6-acetyllysine; by p300/EP300By similarity1
    Modified residuei90PhosphoserineBy similarity1
    Modified residuei91N6-acetyllysine; by p300/EP300By similarity1 Publication1
    Modified residuei118PhosphoserineCombined sources1
    Modified residuei178PhosphothreonineBy similarity1
    Modified residuei286PhosphoserineBy similarity1
    Modified residuei473N6-acetyllysine1 Publication1
    Modified residuei521N6-acetyllysine1 Publication1
    Modified residuei524N6-acetyllysine1 Publication1
    Modified residuei594N6-acetyllysine; by p300/EP300By 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

    Acetylated (PubMed:30193097). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5; acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels (By similarity).By similarity1 Publication
    Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation (PubMed:30193097). Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2 (By similarity).By similarity1 Publication
    Ubiquitination by UBR5 leads to proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P07379

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

    More...    PaxDbi    		P07379

    PRoteomics IDEntifications database

    More...    PRIDEi    		P07379

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P07379

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

    More...    PhosphoSitePlusi    		P07379

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Regulated by cAMP, dexamethasone, glucagon and by insulin. Dexamthasone, glucagon and cAMP increase levels, insulin decreases levels.2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSRNOG00000028616, Expressed in kidney and 21 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P07379, RN

    <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

    Monomer.

    8 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		263330, 1 interactor

    STRING: functional protein association networks

    More...    STRINGi    		10116.ENSRNOP00000030913

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P07379

    <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

    1622
    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    		P07379

    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    		P07379

    <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

    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>Regioni235 – 237Substrate binding5 Publications3
    Regioni403 – 405Substrate binding5 Publications3
    Regioni457 – 487Omega-loop1 PublicationAdd BLAST31

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG3749, Eukaryota

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00390000001912

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_028872_1_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P07379

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		GPTNNWV

    Database of Orthologous Groups

    More...    OrthoDBi    		286671at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P07379

    TreeFam database of animal gene trees

    More...    TreeFami    		TF314402

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00819, PEPCK_GTP, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.449.10, 1 hit
    3.90.228.20, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00452, PEPCK_GTP, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR018091, PEP_carboxykin_GTP_CS
    IPR013035, PEP_carboxykinase_C
    IPR008209, PEP_carboxykinase_GTP
    IPR035077, PEP_carboxykinase_GTP_C
    IPR035078, PEP_carboxykinase_GTP_N
    IPR008210, PEP_carboxykinase_N

    The PANTHER Classification System

    More...    PANTHERi    		PTHR11561, PTHR11561, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00821, PEPCK_GTP, 1 hit
    PF17297, PEPCK_N, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001348, PEP_carboxykinase_GTP, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF68923, SSF68923, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00505, PEPCK_GTP, 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>Sequencei

    <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.

    P07379-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPPQLHNGLD FSAKVIQGSL DSLPQEVRKF VEGNAQLCQP EYIHICDGSE 
            60         70         80         90        100
    EEYGRLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR 
           110        120        130        140        150
    DTVPIPKSGQ SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG 
           160        170        180        190        200
    SPLAKIGIEL TDSPYVVASM RIMTRMGTSV LEALGDGEFI KCLHSVGCPL 
           210        220        230        240        250
    PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI 
           260        270        280        290        300
    ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPTL 
           310        320        330        340        350
    PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT 
           360        370        380        390        400
    IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDEEPCA 
           410        420        430        440        450
    HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW 
           460        470        480        490        500
    QHGVFVGAAM RSEATAAAEH KGKVIMHDPF AMRPFFGYNF GKYLAHWLSM 
           510        520        530        540        550
    AHRPAAKLPK IFHVNWFRKD KNGKFLWPGF GENSRVLEWM FGRIEGEDSA 
           560        570        580        590        600
    KLTPIGYVPK EDALNLKGLG DVNVEELFGI SKEFWEKEVE EIDKYLEDQV 
           610        620 
    NADLPYEIER ELRALKQRIS QM
    Length:622
    Mass (Da):69,416
    Last modified:April 1, 1988 - 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:iF800F73F8F127B04
    GO

    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
    		K03248 K03247 Genomic DNA Translation: AAC98698.1
    BC081900 mRNA Translation: AAH81900.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A23927, QYRTGP

    NCBI Reference Sequences

    More...    RefSeqi    		NP_942075.1, NM_198780.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		362282

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		rno:362282

    <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
    		K03248 K03247 Genomic DNA Translation: AAC98698.1
    BC081900 mRNA Translation: AAH81900.1
    PIRiA23927, QYRTGP
    RefSeqiNP_942075.1, NM_198780.3

    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
    2QEWX-ray1.80A1-622[»]
    2QEYX-ray1.90A1-622[»]
    2QF1X-ray1.80A1-622[»]
    2QF2X-ray1.65A/B1-622[»]
    2RK7X-ray1.90A/B1-622[»]
    2RK8X-ray2.00A/B1-622[»]
    2RKAX-ray1.95A/C1-622[»]
    2RKDX-ray1.90A1-622[»]
    2RKEX-ray1.80A1-622[»]
    3DT2X-ray1.50A1-622[»]
    3DT4X-ray1.45A/C1-622[»]
    3DT7X-ray1.50A/B1-622[»]
    3DTBX-ray1.30A/B1-622[»]
    3MOEX-ray1.25A1-622[»]
    3MOFX-ray1.75A/B1-622[»]
    3MOHX-ray2.10A/B1-622[»]
    4GMMX-ray1.74A1-463[»]
    A475-622[»]
    4GMUX-ray1.20A1-463[»]
    A475-622[»]
    4GMWX-ray1.75A1-463[»]
    A475-622[»]
    4GMZX-ray2.05A1-463[»]
    A475-622[»]
    4GNLX-ray1.70A1-463[»]
    A475-622[»]
    4GNMX-ray1.50A1-463[»]
    A475-622[»]
    4GNOX-ray1.50A1-463[»]
    A475-622[»]
    4GNPX-ray1.74A1-463[»]
    A475-622[»]
    4GNQX-ray1.40A1-463[»]
    A475-622[»]
    4OX2X-ray2.00A/B1-622[»]
    4YW8X-ray1.55A1-622[»]
    4YW9X-ray1.40A1-622[»]
    4YWBX-ray1.50A/C1-622[»]
    4YWDX-ray2.10A1-622[»]
    5FH0X-ray1.60A1-622[»]
    5FH1X-ray1.55A1-622[»]
    5FH2X-ray1.49A1-622[»]
    5FH3X-ray1.60A1-622[»]
    5FH4X-ray1.49A1-622[»]
    5FH5X-ray1.55A1-622[»]
    5V95X-ray2.30A1-622[»]
    5V97X-ray1.80A1-622[»]
    5V9FX-ray2.05A1-622[»]
    5V9GX-ray1.95A1-622[»]
    5V9HX-ray2.15A/B1-622[»]
    6P5OX-ray1.49A1-622[»]
    6YI9X-ray1.75A1-622[»]
    SMRiP07379
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi263330, 1 interactor
    STRINGi10116.ENSRNOP00000030913

    Chemistry databases

    BindingDBiP07379
    ChEMBLiCHEMBL1075234

    PTM databases

    iPTMnetiP07379
    PhosphoSitePlusiP07379

    Proteomic databases

    jPOSTiP07379
    PaxDbiP07379
    PRIDEiP07379

    Genome annotation databases

    EnsembliENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616
    GeneIDi362282
    KEGGirno:362282

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		5105
    RGDi3267, Pck1

    Phylogenomic databases

    eggNOGiKOG3749, Eukaryota
    GeneTreeiENSGT00390000001912
    HOGENOMiCLU_028872_1_0_1
    InParanoidiP07379
    OMAiGPTNNWV
    OrthoDBi286671at2759
    PhylomeDBiP07379
    TreeFamiTF314402

    Enzyme and pathway databases

    UniPathwayiUPA00138
    BRENDAi4.1.1.32, 5301
    ReactomeiR-RNO-70263, Gluconeogenesis
    SABIO-RKiP07379

    Miscellaneous databases

    EvolutionaryTraceiP07379

    Protein Ontology

    More...    PROi    		PR:P07379

    Gene expression databases

    BgeeiENSRNOG00000028616, Expressed in kidney and 21 other tissues
    GenevisibleiP07379, RN

    Family and domain databases

    CDDicd00819, PEPCK_GTP, 1 hit
    Gene3Di3.40.449.10, 1 hit
    3.90.228.20, 1 hit
    HAMAPiMF_00452, PEPCK_GTP, 1 hit
    InterProiView protein in InterPro
    IPR018091, PEP_carboxykin_GTP_CS
    IPR013035, PEP_carboxykinase_C
    IPR008209, PEP_carboxykinase_GTP
    IPR035077, PEP_carboxykinase_GTP_C
    IPR035078, PEP_carboxykinase_GTP_N
    IPR008210, PEP_carboxykinase_N
    PANTHERiPTHR11561, PTHR11561, 1 hit
    PfamiView protein in Pfam
    PF00821, PEPCK_GTP, 1 hit
    PF17297, PEPCK_N, 1 hit
    PIRSFiPIRSF001348, PEP_carboxykinase_GTP, 1 hit
    SUPFAMiSSF68923, SSF68923, 1 hit
    PROSITEiView protein in PROSITE
    PS00505, PEPCK_GTP, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    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 nameiPCKGC_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: P07379
    <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: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: April 7, 2021
    This is version 176 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, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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