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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-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+6 PublicationsNote: Binds 1 Mn2+ ion per subunit.6 Publications

Enzyme regulationi

Enzyme activity is enhanced by acetylation.By similarity

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
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
Binding sitei87Substrate5 Publications1
Metal bindingi244Manganese6 Publications1
Metal bindingi264Manganese; via tele nitrogen6 Publications1
Binding sitei286Substrate6 Publications1
Active sitei2882 Publications1
Metal bindingi311Manganese6 Publications1
Binding sitei405GTP4 Publications1
Binding sitei436GTP5 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi287 – 292GTP5 Publications6
Nucleotide bindingi530 – 533GTP5 Publications4

GO - Molecular functioni

  • carboxylic acid binding Source: BHF-UCL
  • GDP binding Source: RGD
  • GTP binding Source: BHF-UCL
  • magnesium ion binding Source: BHF-UCL
  • manganese ion binding Source: BHF-UCL
  • nucleoside diphosphate kinase activity Source: Reactome
  • phosphoenolpyruvate carboxykinase (GTP) activity Source: BHF-UCL
  • phosphoenolpyruvate carboxykinase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular response to cAMP Source: RGD
  • cellular response to fructose stimulus Source: RGD
  • cellular response to glucagon stimulus Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to potassium ion starvation Source: Ensembl
  • cellular response to retinoic acid Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • drug metabolic process Source: Reactome
  • gluconeogenesis Source: BHF-UCL
  • glucose homeostasis Source: BHF-UCL
  • glucose metabolic process Source: BHF-UCL
  • glycerol biosynthetic process from pyruvate Source: BHF-UCL
  • internal protein amino acid acetylation Source: UniProtKB
  • oxaloacetate metabolic process Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter in response to acidic pH Source: Ensembl
  • response to activity Source: RGD
  • response to insulin Source: BHF-UCL
  • response to interleukin-6 Source: RGD
  • response to lipid Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to methionine Source: RGD
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

BRENDAi4.1.1.32. 5301.
ReactomeiR-RNO-2161541. Abacavir metabolism.
R-RNO-70263. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi3267. Pck1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • extracellular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001036301 – 622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Add BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19PhosphoserineCombined sources1
Modified residuei70N6-acetyllysine; by p300/EP300By similarity1
Modified residuei71N6-acetyllysine; by p300/EP300By similarity1
Modified residuei118PhosphoserineCombined sources1
Modified residuei178PhosphothreonineBy similarity1
Modified residuei286PhosphoserineBy similarity1
Modified residuei594N6-acetyllysine; by p300/EP300By similarity1

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, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP07379.
PRIDEiP07379.

PTM databases

iPTMnetiP07379.
PhosphoSitePlusiP07379.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSRNOG00000028616.
GenevisibleiP07379. RN.

Interactioni

Subunit structurei

Monomer.5 Publications

Protein-protein interaction databases

MINTiMINT-4576726.
STRINGi10116.ENSRNOP00000030913.

Chemistry databases

BindingDBiP07379.

Structurei

Secondary structure

1622
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi12 – 14Combined sources3
Beta strandi15 – 18Combined sources4
Helixi20 – 22Combined sources3
Helixi25 – 38Combined sources14
Beta strandi40 – 45Combined sources6
Helixi50 – 62Combined sources13
Beta strandi65 – 69Combined sources5
Beta strandi72 – 74Combined sources3
Beta strandi76 – 78Combined sources3
Beta strandi84 – 86Combined sources3
Helixi89 – 91Combined sources3
Beta strandi92 – 95Combined sources4
Helixi99 – 102Combined sources4
Beta strandi107 – 109Combined sources3
Helixi119 – 127Combined sources9
Turni131 – 134Combined sources4
Beta strandi137 – 148Combined sources12
Beta strandi155 – 162Combined sources8
Helixi164 – 173Combined sources10
Beta strandi174 – 177Combined sources4
Helixi178 – 184Combined sources7
Beta strandi190 – 195Combined sources6
Helixi214 – 216Combined sources3
Beta strandi218 – 222Combined sources5
Helixi223 – 225Combined sources3
Beta strandi227 – 232Combined sources6
Helixi236 – 239Combined sources4
Helixi242 – 248Combined sources7
Helixi249 – 258Combined sources10
Beta strandi261 – 264Combined sources4
Beta strandi266 – 271Combined sources6
Beta strandi277 – 283Combined sources7
Beta strandi286 – 289Combined sources4
Helixi290 – 294Combined sources5
Beta strandi304 – 311Combined sources8
Beta strandi313 – 317Combined sources5
Beta strandi323 – 326Combined sources4
Beta strandi330 – 335Combined sources6
Turni341 – 343Combined sources3
Helixi345 – 350Combined sources6
Beta strandi356 – 359Combined sources4
Beta strandi361 – 363Combined sources3
Beta strandi388 – 391Combined sources4
Beta strandi395 – 397Combined sources3
Beta strandi405 – 409Combined sources5
Helixi410 – 412Combined sources3
Turni418 – 421Combined sources4
Beta strandi426 – 434Combined sources9
Beta strandi438 – 440Combined sources3
Beta strandi443 – 446Combined sources4
Helixi450 – 458Combined sources9
Beta strandi461 – 463Combined sources3
Beta strandi466 – 469Combined sources4
Beta strandi475 – 477Combined sources3
Helixi479 – 481Combined sources3
Turni483 – 485Combined sources3
Helixi490 – 499Combined sources10
Helixi500 – 502Combined sources3
Beta strandi510 – 514Combined sources5
Beta strandi521 – 523Combined sources3
Beta strandi525 – 527Combined sources3
Helixi530 – 533Combined sources4
Helixi534 – 544Combined sources11
Beta strandi550 – 553Combined sources4
Beta strandi556 – 559Combined sources4
Turni561 – 563Combined sources3
Turni567 – 569Combined sources3
Helixi574 – 578Combined sources5
Helixi582 – 599Combined sources18
Helixi601 – 603Combined sources3
Helixi606 – 620Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP07379.
SMRiP07379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07379.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni235 – 237Substrate binding5 Publications3
Regioni403 – 405Substrate binding5 Publications3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3749. Eukaryota.
COG1274. LUCA.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiP07379.
KOiK01596.
OMAiWLSMAQH.
OrthoDBiEOG091G02YK.
PhylomeDBiP07379.
TreeFamiTF314402.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP. 1 hit.
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.
PIRiA23927. QYRTGP.
RefSeqiNP_942075.1. NM_198780.3.
UniGeneiRn.104376.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP07379.
SMRiP07379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4576726.
STRINGi10116.ENSRNOP00000030913.

Chemistry databases

BindingDBiP07379.
ChEMBLiCHEMBL1075234.

PTM databases

iPTMnetiP07379.
PhosphoSitePlusiP07379.

Proteomic databases

PaxDbiP07379.
PRIDEiP07379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5105.
RGDi3267. Pck1.

Phylogenomic databases

eggNOGiKOG3749. Eukaryota.
COG1274. LUCA.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiP07379.
KOiK01596.
OMAiWLSMAQH.
OrthoDBiEOG091G02YK.
PhylomeDBiP07379.
TreeFamiTF314402.

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi4.1.1.32. 5301.
ReactomeiR-RNO-2161541. Abacavir metabolism.
R-RNO-70263. Gluconeogenesis.
SABIO-RKP07379.

Miscellaneous databases

EvolutionaryTraceiP07379.
PROiP07379.

Gene expression databases

BgeeiENSRNOG00000028616.
GenevisibleiP07379. RN.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.