PCKGC_MOUSE
ID PCKGC_MOUSE Reviewed; 622 AA.
AC Q9Z2V4; Q3UEH3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphoenolpyruvate carboxykinase, cytosolic [GTP] {ECO:0000305};
DE Short=PEPCK-C;
DE EC=4.1.1.32 {ECO:0000269|PubMed:11792850, ECO:0000269|PubMed:29230018, ECO:0000269|PubMed:30193097};
DE AltName: Full=Serine-protein kinase PCK1 {ECO:0000305};
DE EC=2.7.11.- {ECO:0000250|UniProtKB:P35558};
GN Name=Pck1 {ECO:0000312|MGI:MGI:97501};
GN Synonyms=Pepck {ECO:0000303|PubMed:10938127};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10221772; DOI=10.1016/s0303-7207(98)00234-2;
RA Williams C.P., Postic C., Robin D., Robin P., Parrinello J., Shelton K.,
RA Printz R.L., Magnuson M.A., Granner D.K., Forest C., Chalkley R.;
RT "Isolation and characterization of the mouse cytosolic phosphoenolpyruvate
RT carboxykinase (GTP) gene: evidence for tissue-specific hypersensitive
RT sites.";
RL Mol. Cell. Endocrinol. 148:67-77(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10938127; DOI=10.1128/mcb.20.17.6508-6517.2000;
RA She P., Shiota M., Shelton K.D., Chalkley R., Postic C., Magnuson M.A.;
RT "Phosphoenolpyruvate carboxykinase is necessary for the integration of
RT hepatic energy metabolism.";
RL Mol. Cell. Biol. 20:6508-6517(2000).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=11916968; DOI=10.1074/jbc.m200727200;
RA Allen-Jennings A.E., Hartman M.G., Kociba G.J., Hai T.;
RT "The roles of ATF3 in liver dysfunction and the regulation of
RT phosphoenolpyruvate carboxykinase gene expression.";
RL J. Biol. Chem. 277:20020-20025(2002).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11792850; DOI=10.1073/pnas.022616299;
RA Olswang Y., Cohen H., Papo O., Cassuto H., Croniger C.M., Hakimi P.,
RA Tilghman S.M., Hanson R.W., Reshef L.;
RT "A mutation in the peroxisome proliferator-activated receptor gamma-binding
RT site in the gene for the cytosolic form of phosphoenolpyruvate
RT carboxykinase reduces adipose tissue size and fat content in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:625-630(2002).
RN [6]
RP INDUCTION.
RX PubMed=16100117; DOI=10.1074/jbc.m504119200;
RA Cassuto H., Kochan K., Chakravarty K., Cohen H., Blum B., Olswang Y.,
RA Hakimi P., Xu C., Massillon D., Hanson R.W., Reshef L.;
RT "Glucocorticoids regulate transcription of the gene for phosphoenolpyruvate
RT carboxykinase in the liver via an extended glucocorticoid regulatory
RT unit.";
RL J. Biol. Chem. 280:33873-33884(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, ACETYLATION,
RP AND DEACETYLATION BY SIRT1.
RX PubMed=30193097; DOI=10.1016/j.molcel.2018.07.031;
RA Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F.,
RA Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.;
RT "Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme
RT activity between gluconeogenic and anaplerotic reactions.";
RL Mol. Cell 71:718-732(2018).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=29230018; DOI=10.1038/s41556-017-0002-2;
RA Ma R., Ji T., Zhang H., Dong W., Chen X., Xu P., Chen D., Liang X., Yin X.,
RA Liu Y., Ma J., Tang K., Zhang Y., Peng Y., Lu J., Zhang Y., Qin X., Cao X.,
RA Wan Y., Huang B.;
RT "A Pck1-directed glycogen metabolic program regulates formation and
RT maintenance of memory CD8+ T cells.";
RL Nat. Cell Biol. 20:21-27(2018).
CC -!- FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes
CC the reversible decarboxylation and phosphorylation of oxaloacetate
CC (OAA) and acts as the rate-limiting enzyme in gluconeogenesis
CC (PubMed:11916968, PubMed:11792850, PubMed:30193097, PubMed:29230018).
CC Regulates cataplerosis and anaplerosis, the processes that control the
CC levels of metabolic intermediates in the citric acid cycle
CC (PubMed:30193097). At low glucose levels, it catalyzes the cataplerotic
CC conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-
CC limiting step in the metabolic pathway that produces glucose from
CC lactate and other precursors derived from the citric acid cycle
CC (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic
CC conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097).
CC Acts as a regulator of formation and maintenance of memory CD8(+) T-
CC cells: up-regulated in these cells, where it generates
CC phosphoenolpyruvate, via gluconeogenesis (PubMed:29230018). The
CC resultant phosphoenolpyruvate flows to glycogen and pentose phosphate
CC pathway, which is essential for memory CD8(+) T-cells homeostasis
CC (PubMed:29230018). In addition to the phosphoenolpyruvate carboxykinase
CC activity, also acts as a protein kinase when phosphorylated at Ser-90:
CC phosphorylation at Ser-90 by AKT1 reduces the binding affinity to
CC oxaloacetate and promotes an atypical serine protein kinase activity
CC using GTP as donor (By similarity). The protein kinase activity
CC regulates lipogenesis: upon phosphorylation at Ser-90, translocates to
CC the endoplasmic reticulum and catalyzes phosphorylation of INSIG
CC proteins (INSIG1 and INSIG2), thereby disrupting the interaction
CC between INSIG proteins and SCAP and promoting nuclear translocation of
CC SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent
CC transcription of downstream lipogenesis-related genes (By similarity).
CC {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:11792850,
CC ECO:0000269|PubMed:11916968, ECO:0000269|PubMed:29230018,
CC ECO:0000269|PubMed:30193097}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC Evidence={ECO:0000269|PubMed:11792850, ECO:0000269|PubMed:29230018,
CC ECO:0000269|PubMed:30193097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389;
CC Evidence={ECO:0000269|PubMed:29230018, ECO:0000269|PubMed:30193097};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390;
CC Evidence={ECO:0000269|PubMed:30193097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-seryl-[protein] = GDP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:83421;
CC Evidence={ECO:0000250|UniProtKB:P35558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021;
CC Evidence={ECO:0000250|UniProtKB:P35558};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P35558};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P35558};
CC -!- ACTIVITY REGULATION: Phosphoenolpyruvate carboxykinase activity is
CC regulated by acetylation and glucose levels (PubMed:30193097). The
CC anaplerotic conversion of phosphoenolpyruvate to oxaloacetate is
CC improved by PCK1 acetylation on Lys-91 (K91ac), Lys-473 (K473ac) and
CC Lys-521 (K521ac) (By similarity). High glucose concentrations favor
CC PCK1 anaplerotic activity by triggering acetylation on Lys-91 (K91ac).
CC At low glucose levels, SIRT1-mediated deacetylation of Lys-91 promotes
CC the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (By
CC similarity). Phosphorylation at Ser-90 reduces the binding affinity to
CC oxaloacetate and converts the enzyme into an atypical protein kinase
CC using GTP as donor (By similarity). {ECO:0000250|UniProtKB:P07379,
CC ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000269|PubMed:30193097}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P35558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes
CC translocation to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- INDUCTION: Expression is repressed by ATF3 (PubMed:11916968).
CC Expression is regulated by glucocortinoids and insulin
CC (PubMed:16100117). Up-regulated in CD8(+) memory T-cells
CC (PubMed:29230018). {ECO:0000269|PubMed:11916968,
CC ECO:0000269|PubMed:16100117, ECO:0000269|PubMed:29230018}.
CC -!- PTM: Acetylated (PubMed:30193097). Lysine acetylation by p300/EP300 is
CC increased on high glucose conditions and promotes ubiquitination by
CC UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by
CC SIRT2 (By similarity). Deacetylated by SIRT1 (PubMed:30193097).
CC {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.
CC -!- PTM: Ubiquitination by UBR5 leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation
CC affects the efficiency of SIRT1-mediated deacetylation, and regulates
CC PCK1 ubiquitination and degradation. Phosphorylation at Ser-90 by AKT1
CC reduces the binding affinity to oxaloacetate and promotes the protein
CC kinase activity: phosphorylated PCK1 translocates to the endoplasmic
CC reticulum, where it phosphorylates INSIG1 and INSIG2.
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- DISRUPTION PHENOTYPE: Mice do not survive beyond 2 to 3 days after
CC birth. {ECO:0000269|PubMed:10938127}.
CC -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic one
CC and a mitochondrial one.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000305}.
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DR EMBL; AF009605; AAD01427.1; -; Genomic_DNA.
DR EMBL; AK028046; BAC25718.1; -; mRNA.
DR EMBL; AK133496; BAE21687.1; -; mRNA.
DR EMBL; AK149525; BAE28938.1; -; mRNA.
DR CCDS; CCDS17141.1; -.
DR RefSeq; NP_035174.1; NM_011044.2.
DR AlphaFoldDB; Q9Z2V4; -.
DR SMR; Q9Z2V4; -.
DR BioGRID; 202046; 1.
DR IntAct; Q9Z2V4; 1.
DR STRING; 10090.ENSMUSP00000029017; -.
DR iPTMnet; Q9Z2V4; -.
DR PhosphoSitePlus; Q9Z2V4; -.
DR SwissPalm; Q9Z2V4; -.
DR jPOST; Q9Z2V4; -.
DR MaxQB; Q9Z2V4; -.
DR PaxDb; Q9Z2V4; -.
DR PRIDE; Q9Z2V4; -.
DR ProteomicsDB; 287891; -.
DR Antibodypedia; 1643; 613 antibodies from 40 providers.
DR DNASU; 18534; -.
DR Ensembl; ENSMUST00000029017; ENSMUSP00000029017; ENSMUSG00000027513.
DR GeneID; 18534; -.
DR KEGG; mmu:18534; -.
DR UCSC; uc008odm.1; mouse.
DR CTD; 5105; -.
DR MGI; MGI:97501; Pck1.
DR VEuPathDB; HostDB:ENSMUSG00000027513; -.
DR eggNOG; KOG3749; Eukaryota.
DR GeneTree; ENSGT00390000001912; -.
DR HOGENOM; CLU_028872_1_1_1; -.
DR InParanoid; Q9Z2V4; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 286671at2759; -.
DR PhylomeDB; Q9Z2V4; -.
DR TreeFam; TF314402; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; Q9Z2V4; -.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 18534; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Pck1; mouse.
DR PRO; PR:Q9Z2V4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z2V4; protein.
DR Bgee; ENSMUSG00000027513; Expressed in right kidney and 90 other tissues.
DR Genevisible; Q9Z2V4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISO:MGI.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IMP:UniProtKB.
DR GO; GO:0004611; F:phosphoenolpyruvate carboxykinase activity; IMP:MGI.
DR GO; GO:0106264; F:protein serine kinase activity (using GTP as donor); ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; IEA:Ensembl.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IDA:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IMP:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; IMP:UniProtKB.
DR GO; GO:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; IDA:MGI.
DR GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0070741; P:response to interleukin-6; IEA:Ensembl.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:1904640; P:response to methionine; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Decarboxylase; Endoplasmic reticulum;
KW Gluconeogenesis; GTP-binding; Kinase; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation.
FT CHAIN 1..622
FT /note="Phosphoenolpyruvate carboxykinase, cytosolic [GTP]"
FT /id="PRO_0000103628"
FT REGION 457..487
FT /note="Omega-loop"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT ACT_SITE 288
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 287..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 403..405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MOD_RES 71
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MOD_RES 91
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16822"
FT MOD_RES 473
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT MOD_RES 521
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07379"
SQ SEQUENCE 622 AA; 69355 MW; 9D94738B4A0EE196 CRC64;
MPPQLHNGLD FSAKVIQGSL DSLPQAVRKF VEGNAQLCQP EYIHICDGSE EEYGQLLAHM
QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR DTVPIPKTGL SQLGRWMSEE
DFEKAFNARF PGCMKGRTMY VIPFSMGPLG SPLAKIGIEL TDSPYVVASM RIMTRMGISV
LEALGDGEFI KCLHSVGCPL PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL
LGKKCFALRI ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPSL
PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV
AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDAEPCA HPNSRFCTPA SQCPIIDPAW
ESPEGVPIEG IIFGGRRPEG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKIIMHDPF
AMRPFFGYNF GKYLAHWLSM AHRPAAKLPK IFHVNWFRKD KDGKFLWPGF GENSRVLEWM
FGRIEGEDSA KLTPIGYIPK ENALNLKGLG GVNVEELFGI SKEFWEKEVE EIDRYLEDQV
NTDLPYEIER ELRALKQRIS QM
