PCKGC_RAT
ID PCKGC_RAT Reviewed; 622 AA.
AC P07379;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phosphoenolpyruvate carboxykinase, cytosolic [GTP] {ECO:0000305};
DE Short=PEPCK-C;
DE EC=4.1.1.32 {ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:31461616};
DE AltName: Full=Serine-protein kinase PCK1 {ECO:0000305};
DE EC=2.7.11.- {ECO:0000250|UniProtKB:P35558};
GN Name=Pck1 {ECO:0000303|PubMed:24863970, ECO:0000312|RGD:3267};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2993287; DOI=10.1016/s0021-9258(19)85145-1;
RA Beale E.G., Chrapkiewicz N.B., Scoble H.A., Metz R.J., Quick D.P.,
RA Noble R.L., Donelson J.E., Biemann K., Granner D.K.;
RT "Rat hepatic cytosolic phosphoenolpyruvate carboxykinase (GTP). Structures
RT of the protein, messenger RNA, and gene.";
RL J. Biol. Chem. 260:10748-10760(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 279-290, AND ACTIVE SITE.
RC TISSUE=Liver;
RX PubMed=2909519; DOI=10.1016/s0021-9258(17)31219-x;
RA Lewis C.T., Seyer J.M., Carlson G.M.;
RT "Cysteine 288: an essential hyperreactive thiol of cytosolic
RT phosphoenolpyruvate carboxykinase (GTP).";
RL J. Biol. Chem. 264:27-33(1989).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=4186849; DOI=10.1016/s0021-9258(18)63606-3;
RA Ballard F.J., Hanson R.W.;
RT "Purification of phosphoenolpyruvate carboxykinase from the cytosol
RT fraction of rat liver and the immunochemical demonstration of differences
RT between this enzyme and the mitochondrial phosphoenolpyruvate
RT carboxykinase.";
RL J. Biol. Chem. 244:5625-5630(1969).
RN [5]
RP INDUCTION.
RX PubMed=6096365; DOI=10.1016/s0021-9258(17)42541-5;
RA Sasaki K., Cripe T.P., Koch S.R., Andreone T.L., Petersen D.D., Beale E.G.,
RA Granner D.K.;
RT "Multihormonal regulation of phosphoenolpyruvate carboxykinase gene
RT transcription. The dominant role of insulin.";
RL J. Biol. Chem. 259:15242-15251(1984).
RN [6]
RP INDUCTION.
RX PubMed=18335579; DOI=10.1055/s-2007-1004526;
RA Christ B.;
RT "Inhibition of glucagon-signaling and downstream actions by interleukin
RT 1beta and tumor necrosis factor alpha in cultured primary rat
RT hepatocytes.";
RL Horm. Metab. Res. 40:18-23(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524,
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-90 AND LYS-91.
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 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=17685635; DOI=10.1021/bi701038x;
RA Sullivan S.M., Holyoak T.;
RT "Structures of rat cytosolic PEPCK: insight into the mechanism of
RT phosphorylation and decarboxylation of oxaloacetic acid.";
RL Biochemistry 46:10078-10088(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP SUBSTRATE ANALOG, COFACTOR, AND SUBUNIT.
RX PubMed=18197707; DOI=10.1021/bi7020662;
RA Stiffin R.M., Sullivan S.M., Carlson G.M., Holyoak T.;
RT "Differential inhibition of cytosolic PEPCK by substrate analogues. Kinetic
RT and structural characterization of inhibitor recognition.";
RL Biochemistry 47:2099-2109(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=18772387; DOI=10.1073/pnas.0805364105;
RA Sullivan S.M., Holyoak T.;
RT "Enzymes with lid-gated active sites must operate by an induced fit
RT mechanism instead of conformational selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13829-13834(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND
RP SUBSTRATES, COFACTOR, AND SUBUNIT.
RX PubMed=20476774; DOI=10.1021/bi100399e;
RA Johnson T.A., Holyoak T.;
RT "Increasing the conformational entropy of the Omega-loop lid domain in
RT phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic
RT fidelity.";
RL Biochemistry 49:5176-5187(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 1-463 AND 475-622 IN COMPLEX WITH
RP MANGANESE; GTP AND SUBSTRATES, COFACTOR, AND ACTIVE SITE.
RX PubMed=23127136; DOI=10.1021/bi301278t;
RA Johnson T.A., Holyoak T.;
RT "The Omega-loop lid domain of phosphoenolpyruvate carboxykinase is
RT essential for catalytic function.";
RL Biochemistry 51:9547-9559(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND
RP SUBSTRATE, COFACTOR, AND SUBUNIT.
RX PubMed=24863970; DOI=10.1016/j.ymgme.2014.04.001;
RA Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C.,
RA Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G., Holloman C.,
RA Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H., Snyder J.P.,
RA Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W., Traynelis S.F.,
RA Kerr D.S., Gahl W.A.;
RT "Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations
RT associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA
RT receptor glutamate insensitivity.";
RL Mol. Genet. Metab. 113:161-170(2014).
RN [15] {ECO:0007744|PDB:4YW8, ECO:0007744|PDB:4YW9, ECO:0007744|PDB:4YWB, ECO:0007744|PDB:4YWD}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH
RP 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=26322521; DOI=10.1021/acs.biochem.5b00822;
RA Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.;
RT "Inhibition and allosteric regulation of monomeric phosphoenolpyruvate
RT carboxykinase by 3-mercaptopicolinic acid.";
RL Biochemistry 54:5878-5887(2015).
RN [16] {ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1, ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3, ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5FH5}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF GLU-89.
RX PubMed=26709450; DOI=10.1021/acs.biochem.5b01215;
RA Johnson T.A., Mcleod M.J., Holyoak T.;
RT "Utilization of substrate intrinsic binding energy for conformational
RT change and catalytic function in phosphoenolpyruvate carboxykinase.";
RL Biochemistry 55:575-587(2016).
RN [17] {ECO:0007744|PDB:5V95, ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G, ECO:0007744|PDB:5V9H}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF HIS-477.
RX PubMed=28345895; DOI=10.1021/acs.biochem.7b00178;
RA Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.;
RT "Asymmetric anchoring is required for efficient omega-loop opening and
RT closing in cytosolic phosphoenolpyruvate carboxykinase.";
RL Biochemistry 56:2106-2115(2017).
RN [18] {ECO:0007744|PDB:6P5O}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH
RP 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
RX PubMed=31461616; DOI=10.1021/acs.biochem.9b00583;
RA Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.;
RT "Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel
RT inhibitor of phosphoenolpyruvate carboxykinase.";
RL Biochemistry 58:3918-3926(2019).
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:4186849, PubMed:30193097, PubMed:26322521, PubMed:26709450,
CC PubMed:28345895, PubMed:31461616). Regulates cataplerosis and
CC anaplerosis, the processes that control the levels of metabolic
CC intermediates in the citric acid cycle (PubMed:30193097). At low
CC glucose levels, it catalyzes the cataplerotic conversion of
CC oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in
CC the metabolic pathway that produces glucose from lactate and other
CC precursors derived from the citric acid cycle (PubMed:30193097). At
CC high glucose levels, it catalyzes the anaplerotic conversion of
CC phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a
CC regulator of formation and maintenance of memory CD8(+) T-cells: up-
CC regulated in these cells, where it generates phosphoenolpyruvate, via
CC gluconeogenesis (By similarity). The resultant phosphoenolpyruvate
CC flows to glycogen and pentose phosphate pathway, which is essential for
CC memory CD8(+) T-cells homeostasis (By similarity). In addition to the
CC phosphoenolpyruvate carboxykinase activity, also acts as a protein
CC kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1
CC reduces the binding affinity to oxaloacetate and promotes an atypical
CC serine protein kinase activity using GTP as donor (By similarity). The
CC protein kinase activity regulates lipogenesis: upon phosphorylation at
CC Ser-90, translocates to the endoplasmic reticulum and catalyzes
CC phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby
CC disrupting the interaction between INSIG proteins and SCAP and
CC promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or
CC SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-
CC related genes (By similarity). {ECO:0000250|UniProtKB:P35558,
CC ECO:0000250|UniProtKB:Q9Z2V4, ECO:0000269|PubMed:26322521,
CC ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895,
CC ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:31461616,
CC ECO:0000269|PubMed:4186849}.
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:26322521, ECO:0000269|PubMed:26709450,
CC ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:30193097,
CC ECO:0000269|PubMed:31461616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389;
CC Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:30193097};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390;
CC Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:28345895,
CC 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:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707,
CC ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
CC ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970,
CC ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450,
CC ECO:0000269|PubMed:28345895};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:17685635,
CC ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
CC ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
CC ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521,
CC ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895};
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) (PubMed:30193097). 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). Phosphoenolpyruvate carboxykinase activity is inhibited by
CC 3-mercaptopicolinate (PubMed:26322521). Phosphoenolpyruvate
CC carboxykinase activity is inhibited by 3-
CC [(carboxymethyl)thio]picolinate (CMP), which acts as a competitive
CC inhibitor at the oxaloacetate/phosphoenolpyruvate-binding site
CC (PubMed:31461616). Phosphorylation at Ser-90 reduces the binding
CC affinity to oxaloacetate and converts the enzyme into an atypical
CC protein kinase using GTP as donor (By similarity).
CC {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:26322521,
CC ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:31461616}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for oxaloacetate {ECO:0000269|PubMed:30193097};
CC KM=161 uM for GTP {ECO:0000269|PubMed:30193097};
CC KM=301 uM for phosphoenolpyruvate {ECO:0000269|PubMed:30193097};
CC KM=79 uM for GDP {ECO:0000269|PubMed:30193097};
CC KM=475 uM for phosphoenolpyruvate (for phosphoenolpyruvate
CC carboxykinase in the backward reaction)
CC {ECO:0000269|PubMed:26709450};
CC KM=207 uM for GDP (for phosphoenolpyruvate carboxykinase in the
CC backward reaction) {ECO:0000269|PubMed:26709450};
CC KM=435 uM for CO2 (for phosphoenolpyruvate carboxykinase in the
CC backward reaction) {ECO:0000269|PubMed:26709450};
CC KM=51 uM for oxaloacetate (for phosphoenolpyruvate carboxykinase in
CC the forward reaction) {ECO:0000269|PubMed:26709450};
CC KM=55 uM for GTP (for phosphoenolpyruvate carboxykinase in the
CC forward reaction) {ECO:0000269|PubMed:26709450};
CC Note=kcat is 76 sec(-1) with oxaloacetate as substrate
CC (PubMed:30193097). kcat is 27 sec(-1) with phosphoenolpyruvate as
CC substrate (PubMed:30193097). kcat is 65 sec(-1) with GTP as substrate
CC (PubMed:30193097). kcat is 25 sec(-1) with GDP as substrate
CC (PubMed:30193097). kcat is 52 sec(-1) with phosphoenolpyruvate
CC carboxykinase in the forward reaction (PubMed:26709450). kcat is 19
CC sec(-1) with phosphoenolpyruvate carboxykinase in the backward
CC forward reaction (PubMed:26709450). {ECO:0000269|PubMed:26709450,
CC ECO:0000269|PubMed:30193097};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000269|PubMed:30193097}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17685635,
CC ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
CC ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:24863970,
CC ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450,
CC ECO:0000269|PubMed:31461616}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:4186849}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}.
CC Note=Phosphorylation at Ser-90 promotes translocation to the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.
CC -!- INDUCTION: Regulated by cAMP, dexamethasone, glucagon and by insulin.
CC Dexamthasone, glucagon and cAMP increase levels, insulin decreases
CC levels. {ECO:0000269|PubMed:18335579, ECO:0000269|PubMed:6096365}.
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. Deacetylation of Lys-91 is carried out by SIRT1 and depends on
CC PCK1 phosphorylation levels (By similarity).
CC {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.
CC -!- PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation
CC affects the efficiency of SIRT1-mediated deacetylation, and regulates
CC PCK1 ubiquitination and degradation (PubMed:30193097). Phosphorylation
CC at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and
CC promotes the protein kinase activity: phosphorylated PCK1 translocates
CC to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2
CC (By similarity). {ECO:0000250|UniProtKB:P35558,
CC ECO:0000269|PubMed:30193097}.
CC -!- PTM: Ubiquitination by UBR5 leads to proteasomal degradation.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K03248; AAC98698.1; -; Genomic_DNA.
DR EMBL; K03243; AAC98698.1; JOINED; Genomic_DNA.
DR EMBL; K03244; AAC98698.1; JOINED; Genomic_DNA.
DR EMBL; K03245; AAC98698.1; JOINED; Genomic_DNA.
DR EMBL; K03246; AAC98698.1; JOINED; Genomic_DNA.
DR EMBL; K03247; AAC98698.1; JOINED; Genomic_DNA.
DR EMBL; BC081900; AAH81900.1; -; mRNA.
DR PIR; A23927; QYRTGP.
DR RefSeq; NP_942075.1; NM_198780.3.
DR PDB; 2QEW; X-ray; 1.80 A; A=1-622.
DR PDB; 2QEY; X-ray; 1.90 A; A=1-622.
DR PDB; 2QF1; X-ray; 1.80 A; A=1-622.
DR PDB; 2QF2; X-ray; 1.65 A; A/B=1-622.
DR PDB; 2RK7; X-ray; 1.90 A; A/B=1-622.
DR PDB; 2RK8; X-ray; 2.00 A; A/B=1-622.
DR PDB; 2RKA; X-ray; 1.95 A; A/C=1-622.
DR PDB; 2RKD; X-ray; 1.90 A; A=1-622.
DR PDB; 2RKE; X-ray; 1.80 A; A=1-622.
DR PDB; 3DT2; X-ray; 1.50 A; A=1-622.
DR PDB; 3DT4; X-ray; 1.45 A; A/C=1-622.
DR PDB; 3DT7; X-ray; 1.50 A; A/B=1-622.
DR PDB; 3DTB; X-ray; 1.30 A; A/B=1-622.
DR PDB; 3MOE; X-ray; 1.25 A; A=1-622.
DR PDB; 3MOF; X-ray; 1.75 A; A/B=1-622.
DR PDB; 3MOH; X-ray; 2.10 A; A/B=1-622.
DR PDB; 4GMM; X-ray; 1.74 A; A=1-463, A=475-622.
DR PDB; 4GMU; X-ray; 1.20 A; A=1-463, A=475-622.
DR PDB; 4GMW; X-ray; 1.75 A; A=1-463, A=475-622.
DR PDB; 4GMZ; X-ray; 2.05 A; A=1-463, A=475-622.
DR PDB; 4GNL; X-ray; 1.70 A; A=1-463, A=475-622.
DR PDB; 4GNM; X-ray; 1.50 A; A=1-463, A=475-622.
DR PDB; 4GNO; X-ray; 1.50 A; A=1-463, A=475-622.
DR PDB; 4GNP; X-ray; 1.74 A; A=1-463, A=475-622.
DR PDB; 4GNQ; X-ray; 1.40 A; A=1-463, A=475-622.
DR PDB; 4OX2; X-ray; 2.00 A; A/B=1-622.
DR PDB; 4YW8; X-ray; 1.55 A; A=1-622.
DR PDB; 4YW9; X-ray; 1.40 A; A=1-622.
DR PDB; 4YWB; X-ray; 1.50 A; A/C=1-622.
DR PDB; 4YWD; X-ray; 2.10 A; A=1-622.
DR PDB; 5FH0; X-ray; 1.60 A; A=1-622.
DR PDB; 5FH1; X-ray; 1.55 A; A=1-622.
DR PDB; 5FH2; X-ray; 1.49 A; A=1-622.
DR PDB; 5FH3; X-ray; 1.60 A; A=1-622.
DR PDB; 5FH4; X-ray; 1.49 A; A=1-622.
DR PDB; 5FH5; X-ray; 1.55 A; A=1-622.
DR PDB; 5V95; X-ray; 2.30 A; A=1-622.
DR PDB; 5V97; X-ray; 1.80 A; A=1-622.
DR PDB; 5V9F; X-ray; 2.05 A; A=1-622.
DR PDB; 5V9G; X-ray; 1.95 A; A=1-622.
DR PDB; 5V9H; X-ray; 2.15 A; A/B=1-622.
DR PDB; 6P5O; X-ray; 1.49 A; A=1-622.
DR PDB; 6YI9; X-ray; 1.75 A; A=1-622.
DR PDB; 7L36; X-ray; 1.84 A; A=1-622.
DR PDB; 7L3M; X-ray; 2.07 A; A=1-622.
DR PDB; 7L3V; X-ray; 1.98 A; A=1-622.
DR PDBsum; 2QEW; -.
DR PDBsum; 2QEY; -.
DR PDBsum; 2QF1; -.
DR PDBsum; 2QF2; -.
DR PDBsum; 2RK7; -.
DR PDBsum; 2RK8; -.
DR PDBsum; 2RKA; -.
DR PDBsum; 2RKD; -.
DR PDBsum; 2RKE; -.
DR PDBsum; 3DT2; -.
DR PDBsum; 3DT4; -.
DR PDBsum; 3DT7; -.
DR PDBsum; 3DTB; -.
DR PDBsum; 3MOE; -.
DR PDBsum; 3MOF; -.
DR PDBsum; 3MOH; -.
DR PDBsum; 4GMM; -.
DR PDBsum; 4GMU; -.
DR PDBsum; 4GMW; -.
DR PDBsum; 4GMZ; -.
DR PDBsum; 4GNL; -.
DR PDBsum; 4GNM; -.
DR PDBsum; 4GNO; -.
DR PDBsum; 4GNP; -.
DR PDBsum; 4GNQ; -.
DR PDBsum; 4OX2; -.
DR PDBsum; 4YW8; -.
DR PDBsum; 4YW9; -.
DR PDBsum; 4YWB; -.
DR PDBsum; 4YWD; -.
DR PDBsum; 5FH0; -.
DR PDBsum; 5FH1; -.
DR PDBsum; 5FH2; -.
DR PDBsum; 5FH3; -.
DR PDBsum; 5FH4; -.
DR PDBsum; 5FH5; -.
DR PDBsum; 5V95; -.
DR PDBsum; 5V97; -.
DR PDBsum; 5V9F; -.
DR PDBsum; 5V9G; -.
DR PDBsum; 5V9H; -.
DR PDBsum; 6P5O; -.
DR PDBsum; 6YI9; -.
DR PDBsum; 7L36; -.
DR PDBsum; 7L3M; -.
DR PDBsum; 7L3V; -.
DR AlphaFoldDB; P07379; -.
DR SMR; P07379; -.
DR BioGRID; 263330; 1.
DR STRING; 10116.ENSRNOP00000030913; -.
DR BindingDB; P07379; -.
DR ChEMBL; CHEMBL1075234; -.
DR iPTMnet; P07379; -.
DR PhosphoSitePlus; P07379; -.
DR jPOST; P07379; -.
DR PaxDb; P07379; -.
DR PRIDE; P07379; -.
DR Ensembl; ENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616.
DR GeneID; 362282; -.
DR KEGG; rno:362282; -.
DR CTD; 5105; -.
DR RGD; 3267; Pck1.
DR eggNOG; KOG3749; Eukaryota.
DR GeneTree; ENSGT00390000001912; -.
DR HOGENOM; CLU_028872_1_0_1; -.
DR InParanoid; P07379; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 286671at2759; -.
DR PhylomeDB; P07379; -.
DR TreeFam; TF314402; -.
DR BRENDA; 4.1.1.32; 5301.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P07379; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P07379; -.
DR PRO; PR:P07379; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000028616; Expressed in kidney and 17 other tissues.
DR Genevisible; P07379; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; IDA:BHF-UCL.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
DR GO; GO:0000287; F:magnesium ion binding; ISS:BHF-UCL.
DR GO; GO:0030145; F:manganese ion binding; IDA:BHF-UCL.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; EXP:Reactome.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IDA:UniProtKB.
DR GO; GO:0004611; F:phosphoenolpyruvate carboxykinase activity; IDA:RGD.
DR GO; GO:0106264; F:protein serine kinase activity (using GTP as donor); ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; IEP:RGD.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; ISO:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0006094; P:gluconeogenesis; IDA:BHF-UCL.
DR GO; GO:0042593; P:glucose homeostasis; IDA:BHF-UCL.
DR GO; GO:0006006; P:glucose metabolic process; IMP:BHF-UCL.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IDA:BHF-UCL.
DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; ISO:RGD.
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; IEP:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISS:BHF-UCL.
DR GO; GO:0070741; P:response to interleukin-6; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:1904640; P:response to methionine; IEP:RGD.
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 3D-structure; Acetylation; Cytoplasm; Decarboxylase;
KW Direct protein sequencing; Endoplasmic reticulum; Gluconeogenesis;
KW GTP-binding; Kinase; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..622
FT /note="Phosphoenolpyruvate carboxykinase, cytosolic [GTP]"
FT /id="PRO_0000103630"
FT REGION 457..487
FT /note="Omega-loop"
FT /evidence="ECO:0000269|PubMed:28345895"
FT ACT_SITE 288
FT /evidence="ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:2909519"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18197707,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
FT ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521,
FT ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895,
FT ECO:0000269|PubMed:31461616, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5FH5,
FT ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F,
FT ECO:0007744|PDB:5V9G, ECO:0007744|PDB:6P5O"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
FT ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521,
FT ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895,
FT ECO:0000269|PubMed:31461616, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5FH5,
FT ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F,
FT ECO:0007744|PDB:5V9G, ECO:0007744|PDB:6P5O"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
FT ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:24863970"
FT BINDING 287..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970,
FT ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450,
FT ECO:0000269|PubMed:28345895, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5V97,
FT ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387,
FT ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521,
FT ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895,
FT ECO:0000269|PubMed:31461616, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5FH5,
FT ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F,
FT ECO:0007744|PDB:5V9G, ECO:0007744|PDB:6P5O"
FT BINDING 403..405
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18197707,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970"
FT BINDING 405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136,
FT ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521,
FT ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895,
FT ECO:0007744|PDB:4YW9, ECO:0007744|PDB:5FH0,
FT ECO:0007744|PDB:5FH1, ECO:0007744|PDB:5FH2,
FT ECO:0007744|PDB:5FH3, ECO:0007744|PDB:5FH4,
FT ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F,
FT ECO:0007744|PDB:5V9G"
FT BINDING 436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970,
FT ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450,
FT ECO:0000269|PubMed:28345895, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5V97,
FT ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17685635,
FT ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774,
FT ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970,
FT ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450,
FT ECO:0000269|PubMed:28345895, ECO:0007744|PDB:4YW9,
FT ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1,
FT ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3,
FT ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5V97,
FT ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 ECO:0000269|PubMed:30193097"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16822"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16822"
FT MOD_RES 473
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30193097"
FT MOD_RES 521
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30193097"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30193097"
FT MOD_RES 594
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000250|UniProtKB:P35558"
FT MUTAGEN 89
FT /note="E->A,D,Q: Abolished phosphoenolpyruvate
FT carboxykinase activity; decreased affinity for
FT oxaloacetate."
FT /evidence="ECO:0000269|PubMed:26709450"
FT MUTAGEN 90
FT /note="S->A: Decreased phosphorylation and increased
FT acetylation levels."
FT /evidence="ECO:0000269|PubMed:30193097"
FT MUTAGEN 91
FT /note="K->Q: 3-fold decrease of affinity for
FT phosphoenolpyruvate."
FT /evidence="ECO:0000269|PubMed:30193097"
FT MUTAGEN 477
FT /note="H->R: Destabilization of the closed state of the
FT omega-loop, resulting in decreased capture rates for the
FT weaker binding substrates associated with catalysis in the
FT phosphoenolpyruvate to oxaloacetate direction."
FT /evidence="ECO:0000269|PubMed:28345895"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:4GNQ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 137..148
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6YI9"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:3DT4"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:3MOE"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 490..499
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:2RKD"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 534..544
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:4GMU"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:4GMU"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:5FH4"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 582..599
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:4GMU"
FT HELIX 606..620
FT /evidence="ECO:0007829|PDB:4GMU"
SQ SEQUENCE 622 AA; 69416 MW; F800F73F8F127B04 CRC64;
MPPQLHNGLD FSAKVIQGSL DSLPQEVRKF VEGNAQLCQP EYIHICDGSE EEYGRLLAHM
QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR DTVPIPKSGQ SQLGRWMSEE
DFEKAFNARF PGCMKGRTMY VIPFSMGPLG SPLAKIGIEL TDSPYVVASM RIMTRMGTSV
LEALGDGEFI KCLHSVGCPL PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL
LGKKCFALRI ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPTL
PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV
AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDEEPCA HPNSRFCTPA SQCPIIDPAW
ESPEGVPIEG IIFGGRRPAG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKVIMHDPF
AMRPFFGYNF GKYLAHWLSM AHRPAAKLPK IFHVNWFRKD KNGKFLWPGF GENSRVLEWM
FGRIEGEDSA KLTPIGYVPK EDALNLKGLG DVNVEELFGI SKEFWEKEVE EIDKYLEDQV
NADLPYEIER ELRALKQRIS QM
