PCKGC_CHICK
ID PCKGC_CHICK Reviewed; 622 AA.
AC P05153;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphoenolpyruvate carboxykinase, cytosolic [GTP] {ECO:0000305};
DE Short=PEPCK-C;
DE EC=4.1.1.32 {ECO:0000250|UniProtKB:P35558};
DE AltName: Full=Serine-protein kinase PCK1 {ECO:0000305};
DE EC=2.7.11.- {ECO:0000250|UniProtKB:P35558};
GN Name=PCK1 {ECO:0000250|UniProtKB:P35558};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3094011; DOI=10.1073/pnas.83.20.7583;
RA Cook J.S., Weldon S.L., Garcia-Ruiz J.P., Hod Y., Hanson R.W.;
RT "Nucleotide sequence of the mRNA encoding the cytosolic form of
RT phosphoenolpyruvate carboxykinase (GTP) from the chicken.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7583-7587(1986).
CC -!- FUNCTION: Regulates cataplerosis and anaplerosis, the processes that
CC control the levels of metabolic intermediates in the citric acid cycle.
CC At low glucose levels, it catalyzes the cataplerotic conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step
CC in the metabolic pathway that produces glucose from lactate and other
CC precursors derived from the citric acid cycle. At high glucose levels,
CC it catalyzes the anaplerotic conversion of phosphoenolpyruvate to
CC oxaloacetate. In addition to the phosphoenolpyruvate carboxykinase
CC activity, also acts as a protein kinase when phosphorylated at Ser-90:
CC phosphorylation at Ser-90 reduces the binding affinity to oxaloacetate
CC and promotes an atypical serine protein kinase activity using GTP as
CC donor. {ECO:0000250|UniProtKB:P35558}.
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:0000250|UniProtKB:P35558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389;
CC Evidence={ECO:0000250|UniProtKB:P35558};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390;
CC Evidence={ECO:0000250|UniProtKB:P35558};
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 glucose levels (By similarity). Phosphorylation at Ser-90
CC reduces the binding affinity to oxaloacetate and converts the enzyme
CC into an atypical protein kinase using GTP as donor (By similarity).
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P35558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35558}.
CC -!- PTM: Phosphorylation at Ser-90 reduces the binding affinity to
CC oxaloacetate and promotes the protein kinase activity.
CC {ECO:0000250|UniProtKB:P35558}.
CC -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic one
CC and a mitochondrial one. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000305}.
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DR EMBL; M14229; AAA49005.1; -; mRNA.
DR PIR; A26494; QYCHGC.
DR RefSeq; NP_990802.1; NM_205471.1.
DR AlphaFoldDB; P05153; -.
DR SMR; P05153; -.
DR STRING; 9031.ENSGALP00000041760; -.
DR PaxDb; P05153; -.
DR GeneID; 396458; -.
DR KEGG; gga:396458; -.
DR CTD; 5105; -.
DR VEuPathDB; HostDB:geneid_396458; -.
DR eggNOG; KOG3749; Eukaryota.
DR InParanoid; P05153; -.
DR OrthoDB; 286671at2759; -.
DR PhylomeDB; P05153; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR SABIO-RK; P05153; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:P05153; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0051379; F:epinephrine binding; IDA:AgBase.
DR GO; GO:0005525; F:GTP binding; ISA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:AgBase.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; ISA:AgBase.
DR GO; GO:0106264; F:protein serine kinase activity (using GTP as donor); ISS:UniProtKB.
DR GO; GO:0008343; P:adult feeding behavior; IMP:AgBase.
DR GO; GO:0007568; P:aging; ISA:AgBase.
DR GO; GO:0006522; P:alanine metabolic process; IDA:AgBase.
DR GO; GO:0006531; P:aspartate metabolic process; IDA:AgBase.
DR GO; GO:0071320; P:cellular response to cAMP; ISA:AgBase.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:AgBase.
DR GO; GO:0071361; P:cellular response to ethanol; IDA:AgBase.
DR GO; GO:0071332; P:cellular response to fructose stimulus; ISA:AgBase.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; ISA:AgBase.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:AgBase.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:AgBase.
DR GO; GO:0071456; P:cellular response to hypoxia; ISA:AgBase.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:AgBase.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISA:AgBase.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IDA:AgBase.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISA:AgBase.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISA:AgBase.
DR GO; GO:0048589; P:developmental growth; IDA:AgBase.
DR GO; GO:0007586; P:digestion; TAS:AgBase.
DR GO; GO:0030703; P:eggshell formation; IMP:AgBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:AgBase.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IEP:AgBase.
DR GO; GO:0006094; P:gluconeogenesis; TAS:AgBase.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:AgBase.
DR GO; GO:0006541; P:glutamine metabolic process; IDA:AgBase.
DR GO; GO:0019563; P:glycerol catabolic process; IDA:AgBase.
DR GO; GO:0006544; P:glycine metabolic process; IDA:AgBase.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:AgBase.
DR GO; GO:0050892; P:intestinal absorption; TAS:AgBase.
DR GO; GO:0006089; P:lactate metabolic process; IDA:AgBase.
DR GO; GO:0006735; P:NADH regeneration; TAS:AgBase.
DR GO; GO:0045912; P:negative regulation of carbohydrate metabolic process; IDA:AgBase.
DR GO; GO:0018991; P:oviposition; IMP:AgBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045913; P:positive regulation of carbohydrate metabolic process; IDA:AgBase.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; TAS:AgBase.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0006560; P:proline metabolic process; IDA:AgBase.
DR GO; GO:0019543; P:propionate catabolic process; IDA:AgBase.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:AgBase.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:AgBase.
DR GO; GO:0006111; P:regulation of gluconeogenesis; TAS:AgBase.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046015; P:regulation of transcription by glucose; TAS:AgBase.
DR GO; GO:0051591; P:response to cAMP; IDA:AgBase.
DR GO; GO:0046898; P:response to cycloheximide; TAS:AgBase.
DR GO; GO:0051384; P:response to glucocorticoid; TAS:AgBase.
DR GO; GO:0070741; P:response to interleukin-6; ISA:AgBase.
DR GO; GO:0033993; P:response to lipid; ISA:AgBase.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISA:AgBase.
DR GO; GO:1904640; P:response to methionine; ISA:AgBase.
DR GO; GO:0042594; P:response to starvation; IDA:AgBase.
DR GO; GO:0009069; P:serine family amino acid metabolic process; IDA:AgBase.
DR GO; GO:0019953; P:sexual reproduction; IMP:AgBase.
DR GO; GO:0007296; P:vitellogenesis; IMP:AgBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Kinase; Lyase;
KW Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..622
FT /note="Phosphoenolpyruvate carboxykinase, cytosolic [GTP]"
FT /id="PRO_0000103631"
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 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35558"
SQ SEQUENCE 622 AA; 69528 MW; 1BB1E708A3D5E722 CRC64;
MAPELKTEVN IISKVIQGDL ESLPPQVREF IESNAKLCQP ESIHICDGSE EENKKILDIM
VEQGMIKKLS KYENCWLALT NPRDVARIES KTVIITQEQR DTIPIPKTGS SQLGRWMSEE
DFEKAFNTRF PGCMQGRTMY VIPFSMGPIG SPLAKIGIEL TDSPYVVASM RMMTRMGTAA
LKALGNGEFV KCLHSVGCPL PLKEPLINNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL
LGKKCFALRI ASRIAKEEGW LAEHMLILGI TNPEGEKKYF AAAFPSACGK TNLAMMNPSR
PGWKIECVGD DIAWMKFDEL GNLRAINPEN GFFGVAPGTS IKTNPNAIKT IFKNTIFTNV
AETSDGGVYW EGIDEPLPPG VTLTSWKNKD WTPDNGEPCA HPNSRFCTPA SQCPIMDPAW
ESPEGVPIEG IIFGGRRPAG VPLVYEAFNW QHGVFIGAAM RSEATAAAEH KGKIIMHDPF
AMRPFFGYNF GKYLAHWLSM AHRPAAKLPR IFHVNWFRKD SQGKFLWPGY GENSRVLEWM
FNRIQGKASA KSTAIGYIPA DTALNLKGLE DINLTELFNI SKEFWEKEVE EIKQYFEGQV
NADLPYEIER ELLALEMRIK QL
