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P07379

- PCKGC_RAT

UniProt

P07379 - PCKGC_RAT

Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

Pck1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of oxaloacetate (OAA) 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.

    Catalytic activityi

    GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

    Cofactori

    Binds 1 manganese ion per subunit.2 Publications

    Enzyme regulationi

    Enzyme activity is enhanced by acetylation.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei87 – 871Substrate2 Publications
    Binding sitei237 – 2371Substrate; via amide nitrogen2 Publications
    Metal bindingi244 – 2441Manganese2 Publications
    Binding sitei244 – 2441Substrate2 Publications
    Metal bindingi264 – 2641Manganese; via tele nitrogen2 Publications
    Binding sitei286 – 2861Substrate2 Publications
    Active sitei288 – 28811 Publication
    Metal bindingi311 – 3111Manganese2 Publications
    Binding sitei405 – 4051GTP2 Publications
    Binding sitei436 – 4361GTP2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi287 – 2926GTP2 Publications
    Nucleotide bindingi530 – 5334GTP2 Publications

    GO - Molecular functioni

    1. carboxylic acid binding Source: BHF-UCL
    2. GDP binding Source: RGD
    3. GTP binding Source: BHF-UCL
    4. magnesium ion binding Source: BHF-UCL
    5. manganese ion binding Source: BHF-UCL
    6. phosphoenolpyruvate carboxykinase (GTP) activity Source: BHF-UCL
    7. phosphoenolpyruvate carboxykinase activity Source: RGD

    GO - Biological processi

    1. gluconeogenesis Source: BHF-UCL
    2. glucose homeostasis Source: BHF-UCL
    3. glucose metabolic process Source: BHF-UCL
    4. glycerol biosynthetic process from pyruvate Source: BHF-UCL
    5. internal protein amino acid acetylation Source: UniProtKB
    6. oxaloacetate metabolic process Source: RGD
    7. response to activity Source: RGD
    8. response to insulin Source: BHF-UCL

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

    GTP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198824. Abacavir metabolism.
    REACT_217998. Gluconeogenesis.
    SABIO-RKP07379.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC:4.1.1.32)
    Short name:
    PEPCK-C
    Gene namesi
    Name:Pck1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi3267. Pck1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]PRO_0000103630Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine; by p300/EP300By similarity
    Modified residuei71 – 711N6-acetyllysine; by p300/EP300By similarity
    Modified residuei594 – 5941N6-acetyllysine; by p300/EP300By similarity

    Post-translational modificationi

    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 By similarity.By similarity
    Ubiquitination by UBR5 leads to proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    PaxDbiP07379.
    PRIDEiP07379.

    PTM databases

    PhosphoSiteiP07379.

    Expressioni

    Inductioni

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

    Gene expression databases

    GenevestigatoriP07379.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    MINTiMINT-4576726.
    STRINGi10116.ENSRNOP00000030913.

    Structurei

    Secondary structure

    1
    622
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi12 – 143
    Beta strandi15 – 184
    Helixi20 – 223
    Helixi25 – 3814
    Beta strandi40 – 456
    Helixi50 – 6213
    Beta strandi65 – 695
    Beta strandi72 – 743
    Beta strandi76 – 783
    Beta strandi84 – 863
    Helixi89 – 913
    Beta strandi92 – 954
    Helixi99 – 1024
    Beta strandi107 – 1093
    Helixi119 – 1279
    Turni131 – 1344
    Beta strandi137 – 14812
    Beta strandi155 – 1628
    Helixi164 – 17310
    Beta strandi174 – 1774
    Helixi178 – 1847
    Beta strandi190 – 1956
    Helixi214 – 2163
    Beta strandi218 – 2225
    Helixi223 – 2253
    Beta strandi227 – 2326
    Helixi236 – 2394
    Helixi242 – 2487
    Helixi249 – 25810
    Beta strandi261 – 2644
    Beta strandi266 – 2716
    Beta strandi277 – 2837
    Beta strandi286 – 2894
    Helixi290 – 2945
    Beta strandi304 – 3118
    Beta strandi313 – 3175
    Beta strandi323 – 3264
    Beta strandi330 – 3356
    Turni341 – 3433
    Helixi345 – 3506
    Beta strandi356 – 3594
    Beta strandi361 – 3633
    Beta strandi388 – 3914
    Beta strandi395 – 3973
    Beta strandi405 – 4095
    Helixi410 – 4123
    Turni418 – 4214
    Beta strandi426 – 4349
    Beta strandi438 – 4403
    Beta strandi443 – 4464
    Helixi450 – 4589
    Beta strandi461 – 4633
    Beta strandi466 – 4694
    Beta strandi475 – 4773
    Helixi479 – 4813
    Turni483 – 4853
    Helixi490 – 49910
    Helixi500 – 5023
    Beta strandi510 – 5145
    Beta strandi521 – 5233
    Beta strandi525 – 5273
    Helixi530 – 5334
    Helixi534 – 54411
    Beta strandi550 – 5534
    Beta strandi556 – 5594
    Turni561 – 5633
    Turni567 – 5693
    Helixi574 – 5785
    Helixi582 – 59918
    Helixi601 – 6033
    Helixi606 – 62015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP07379.
    SMRiP07379. Positions 1-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07379.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 4053Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1274.
    GeneTreeiENSGT00390000001912.
    HOGENOMiHOG000191700.
    HOVERGENiHBG053651.
    InParanoidiP07379.
    KOiK01596.
    OMAiPDHIHIC.
    OrthoDBiEOG7KSX81.
    PhylomeDBiP07379.
    TreeFamiTF314402.

    Family and domain databases

    Gene3Di3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPiMF_00452. PEPCK_GTP.
    InterProiIPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view]
    PANTHERiPTHR11561. PTHR11561. 1 hit.
    PfamiPF00821. PEPCK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMiSSF68923. SSF68923. 1 hit.
    PROSITEiPS00505. PEPCK_GTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07379-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPQLHNGLD FSAKVIQGSL DSLPQEVRKF VEGNAQLCQP EYIHICDGSE    50
    EEYGRLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR 100
    DTVPIPKSGQ SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG 150
    SPLAKIGIEL TDSPYVVASM RIMTRMGTSV LEALGDGEFI KCLHSVGCPL 200
    PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI 250
    ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPTL 300
    PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT 350
    IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDEEPCA 400
    HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW 450
    QHGVFVGAAM RSEATAAAEH KGKVIMHDPF AMRPFFGYNF GKYLAHWLSM 500
    AHRPAAKLPK IFHVNWFRKD KNGKFLWPGF GENSRVLEWM FGRIEGEDSA 550
    KLTPIGYVPK EDALNLKGLG DVNVEELFGI SKEFWEKEVE EIDKYLEDQV 600
    NADLPYEIER ELRALKQRIS QM 622
    Length:622
    Mass (Da):69,416
    Last modified:April 1, 1988 - v1
    Checksum:iF800F73F8F127B04
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03248
    , K03243, K03244, K03245, K03246, K03247 Genomic DNA. Translation: AAC98698.1.
    BC081900 mRNA. Translation: AAH81900.1.
    PIRiA23927. QYRTGP.
    RefSeqiNP_942075.1. NM_198780.3.
    UniGeneiRn.104376.

    Genome annotation databases

    EnsembliENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616.
    GeneIDi362282.
    KEGGirno:362282.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03248
    , K03243 , K03244 , K03245 , K03246 , K03247 Genomic DNA. Translation: AAC98698.1 .
    BC081900 mRNA. Translation: AAH81900.1 .
    PIRi A23927. QYRTGP.
    RefSeqi NP_942075.1. NM_198780.3.
    UniGenei Rn.104376.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QEW X-ray 1.80 A 1-622 [» ]
    2QEY X-ray 1.90 A 1-622 [» ]
    2QF1 X-ray 1.80 A 1-622 [» ]
    2QF2 X-ray 1.65 A/B 1-622 [» ]
    2RK7 X-ray 1.90 A/B 1-622 [» ]
    2RK8 X-ray 2.00 A/B 1-622 [» ]
    2RKA X-ray 1.95 A/C 1-622 [» ]
    2RKD X-ray 1.90 A 1-622 [» ]
    2RKE X-ray 1.80 A 1-622 [» ]
    3DT2 X-ray 1.50 A 1-622 [» ]
    3DT4 X-ray 1.45 A/C 1-622 [» ]
    3DT7 X-ray 1.50 A/B 1-622 [» ]
    3DTB X-ray 1.30 A/B 1-622 [» ]
    3MOE X-ray 1.25 A 1-622 [» ]
    3MOF X-ray 1.75 A/B 1-622 [» ]
    3MOH X-ray 2.10 A/B 1-622 [» ]
    4GMM X-ray 1.74 A 1-463 [» ]
    A 475-622 [» ]
    4GMU X-ray 1.20 A 1-463 [» ]
    A 475-622 [» ]
    4GMW X-ray 1.75 A 1-463 [» ]
    A 475-622 [» ]
    4GMZ X-ray 2.05 A 1-463 [» ]
    A 475-622 [» ]
    4GNL X-ray 1.70 A 1-463 [» ]
    A 475-622 [» ]
    4GNM X-ray 1.50 A 1-463 [» ]
    A 475-622 [» ]
    4GNO X-ray 1.50 A 1-463 [» ]
    A 475-622 [» ]
    4GNP X-ray 1.74 A 1-463 [» ]
    A 475-622 [» ]
    4GNQ X-ray 1.40 A 1-463 [» ]
    A 475-622 [» ]
    4OX2 X-ray 2.00 A/B 1-622 [» ]
    ProteinModelPortali P07379.
    SMRi P07379. Positions 1-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4576726.
    STRINGi 10116.ENSRNOP00000030913.

    Chemistry

    ChEMBLi CHEMBL1075234.

    PTM databases

    PhosphoSitei P07379.

    Proteomic databases

    PaxDbi P07379.
    PRIDEi P07379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000031586 ; ENSRNOP00000030913 ; ENSRNOG00000028616 .
    GeneIDi 362282.
    KEGGi rno:362282.

    Organism-specific databases

    CTDi 5105.
    RGDi 3267. Pck1.

    Phylogenomic databases

    eggNOGi COG1274.
    GeneTreei ENSGT00390000001912.
    HOGENOMi HOG000191700.
    HOVERGENi HBG053651.
    InParanoidi P07379.
    KOi K01596.
    OMAi PDHIHIC.
    OrthoDBi EOG7KSX81.
    PhylomeDBi P07379.
    TreeFami TF314402.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    Reactomei REACT_198824. Abacavir metabolism.
    REACT_217998. Gluconeogenesis.
    SABIO-RK P07379.

    Miscellaneous databases

    EvolutionaryTracei P07379.
    NextBioi 679329.
    PROi P07379.

    Gene expression databases

    Genevestigatori P07379.

    Family and domain databases

    Gene3Di 3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPi MF_00452. PEPCK_GTP.
    InterProi IPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view ]
    PANTHERi PTHR11561. PTHR11561. 1 hit.
    Pfami PF00821. PEPCK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMi SSF68923. SSF68923. 1 hit.
    PROSITEi PS00505. PEPCK_GTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rat hepatic cytosolic phosphoenolpyruvate carboxykinase (GTP). Structures of the protein, messenger RNA, and gene."
      Beale E.G., Chrapkiewicz N.B., Scoble H.A., Metz R.J., Quick D.P., Noble R.L., Donelson J.E., Biemann K., Granner D.K.
      J. Biol. Chem. 260:10748-10760(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. "Cysteine 288: an essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP)."
      Lewis C.T., Seyer J.M., Carlson G.M.
      J. Biol. Chem. 264:27-33(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 279-290, ACTIVE SITE CYS-288.
      Tissue: Liver.
    4. "Multihormonal regulation of phosphoenolpyruvate carboxykinase gene transcription. The dominant role of insulin."
      Sasaki K., Cripe T.P., Koch S.R., Andreone T.L., Petersen D.D., Beale E.G., Granner D.K.
      J. Biol. Chem. 259:15242-15251(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
      Christ B.
      Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
      Sullivan S.M., Holyoak T.
      Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, REACTION MECHANISM.
    7. "Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection."
      Sullivan S.M., Holyoak T.
      Proc. Natl. Acad. Sci. U.S.A. 105:13829-13834(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, REACTION MECHANISM.

    Entry informationi

    Entry nameiPCKGC_RAT
    AccessioniPrimary (citable) accession number: P07379
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    External Data

    Dasty 3