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P07379

- PCKGC_RAT

UniProt

P07379 - PCKGC_RAT

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Protein
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Gene
Pck1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.UniRule annotation

Cofactori

Binds 1 manganese ion per subunit.2 Publications

Enzyme regulationi

Enzyme activity is enhanced by acetylation By similarity.UniRule annotation

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi287 – 2926GTPUniRule annotation
Nucleotide bindingi530 – 5334GTPUniRule annotation

GO - Molecular functioni

  1. GDP binding Source: RGD
  2. GTP binding Source: BHF-UCL
  3. carboxylic acid 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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; by p300/EP300 By similarity
Modified residuei71 – 711N6-acetyllysine; by p300/EP300 By similarity
Modified residuei594 – 5941N6-acetyllysine; by p300/EP300 By 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.UniRule annotation
Ubiquitination by UBR5 leads to proteasomal degradation By similarity.UniRule annotation

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.

Protein-protein interaction databases

MINTiMINT-4576726.
STRINGi10116.ENSRNOP00000030913.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP07379.

Family & Domainsi

Region

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 127 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

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