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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.

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

Cofactori

Mn2+2 PublicationsNote: Binds 1 Mn(2+) 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
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.
REACT_260360. Transcriptional regulation of white adipocyte differentiation.
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
  3. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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
Checksum:iF800F73F8F127B04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi P07379.
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.
REACT_260360. Transcriptional regulation of white adipocyte differentiation.
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: November 26, 2014
This is version 130 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