entry created 1988-04-01 dataset Swiss-Prot modified 2023-02-22 version 183 accession P07379 name PCKGC_RAT protein recommendedName fullName evidence 20 Phosphoenolpyruvate-carboxykinase,-cytosolic-[GTP] shortName PEPCK-C ecNumber evidence 11-12-13-15-16 4.1.1.32 alternativeName fullName evidence 20 Serine-protein-kinase-PCK1 ecNumber evidence 1 2.7.11.- gene name evidence 19-22 type primary Pck1 organism name type scientific Rattus-norvegicus name type common Rat dbReference id 10116 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Chordata taxon Craniata taxon Vertebrata taxon Euteleostomi taxon Mammalia taxon Eutheria taxon Euarchontoglires taxon Glires taxon Rodentia taxon Myomorpha taxon Muroidea taxon Muridae taxon Murinae taxon Rattus reference key 1 citation date 1985 first 10748 last 10760 name J.-Biol.-Chem. type journal-article volume 260 title Rat-hepatic-cytosolic-phosphoenolpyruvate-carboxykinase-(GTP).-Structures-of-the-protein,-messenger-RNA,-and-gene. authorList person name Beale-E.G. person name Chrapkiewicz-N.B. person name Scoble-H.A. person name Metz-R.J. person name Quick-D.P. person name Noble-R.L. person name Donelson-J.E. person name Biemann-K. person name Granner-D.K. dbReference id 2993287 type PubMed dbReference id 10.1016/s0021-9258(19)85145-1 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] source tissue Liver reference key 2 citation date 2004 first 2121 last 2127 name Genome-Res. type journal-article volume 14 title The-status,-quality,-and-expansion-of-the-NIH-full-length-cDNA-project:-the-Mammalian-Gene-Collection-(MGC). authorList consortium name The-MGC-Project-Team dbReference id 15489334 type PubMed dbReference id 10.1101/gr.2596504 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-MRNA] source tissue Kidney reference key 3 citation date 1989 first 27 last 33 name J.-Biol.-Chem. type journal-article volume 264 title Cysteine-288:-an-essential-hyperreactive-thiol-of-cytosolic-phosphoenolpyruvate-carboxykinase-(GTP). authorList person name Lewis-C.T. person name Seyer-J.M. person name Carlson-G.M. dbReference id 2909519 type PubMed dbReference id 10.1016/s0021-9258(17)31219-x type DOI scope PROTEIN-SEQUENCE-OF-279-290 scope ACTIVE-SITE source tissue Liver reference key 4 citation date 1969 first 5625 last 5630 name J.-Biol.-Chem. type journal-article volume 244 title Purification-of-phosphoenolpyruvate-carboxykinase-from-the-cytosol-fraction-of-rat-liver-and-the-immunochemical-demonstration-of-differences-between-this-enzyme-and-the-mitochondrial-phosphoenolpyruvate-carboxykinase. authorList person name Ballard-F.J. person name Hanson-R.W. dbReference id 4186849 type PubMed dbReference id 10.1016/s0021-9258(18)63606-3 type DOI scope FUNCTION scope SUBCELLULAR-LOCATION reference key 5 citation date 1984 first 15242 last 15251 name J.-Biol.-Chem. type journal-article volume 259 title Multihormonal-regulation-of-phosphoenolpyruvate-carboxykinase-gene-transcription.-The-dominant-role-of-insulin. authorList person name Sasaki-K. person name Cripe-T.P. person name Koch-S.R. person name Andreone-T.L. person name Petersen-D.D. person name Beale-E.G. person name Granner-D.K. dbReference id 6096365 type PubMed dbReference id 10.1016/s0021-9258(17)42541-5 type DOI scope INDUCTION reference key 6 citation date 2008 first 18 last 23 name Horm.-Metab.-Res. type journal-article volume 40 title Inhibition-of-glucagon-signaling-and-downstream-actions-by-interleukin-1beta-and-tumor-necrosis-factor-alpha-in-cultured-primary-rat-hepatocytes. authorList person name Christ-B. dbReference id 18335579 type PubMed dbReference id 10.1055/s-2007-1004526 type DOI scope INDUCTION reference key 7 citation date 2012 first 876 last 876 name Nat.-Commun. type journal-article volume 3 title Quantitative-maps-of-protein-phosphorylation-sites-across-14-different-rat-organs-and-tissues. authorList person name Lundby-A. person name Secher-A. person name Lage-K. person name Nordsborg-N.B. person name Dmytriyev-A. person name Lundby-C. person name Olsen-J.V. dbReference id 22673903 type PubMed dbReference id 10.1038/ncomms1871 type DOI scope PHOSPHORYLATION-[LARGE-SCALE-ANALYSIS]-AT-SER-19-AND-SER-118 scope IDENTIFICATION-BY-MASS-SPECTROMETRY-[LARGE-SCALE-ANALYSIS] reference key 8 citation date 2018 first 718 last 732 name Mol.-Cell type journal-article volume 71 title Dynamic-acetylation-of-phosphoenolpyruvate-carboxykinase-toggles-enzyme-activity-between-gluconeogenic-and-anaplerotic-reactions. authorList person name Latorre-Muro-P. person name Baeza-J. person name Armstrong-E.A. person name Hurtado-Guerrero-R. person name Corzana-F. person name Wu-L.E. person name Sinclair-D.A. person name Lopez-Buesa-P. person name Carrodeguas-J.A. person name Denu-J.M. dbReference id 30193097 type PubMed dbReference id 10.1016/j.molcel.2018.07.031 type DOI scope FUNCTION scope PATHWAY scope CATALYTIC-ACTIVITY scope BIOPHYSICOCHEMICAL-PROPERTIES scope ACTIVITY-REGULATION scope ACETYLATION-AT-LYS-91;-LYS-473;-LYS-521-AND-LYS-524 scope PHOSPHORYLATION scope MUTAGENESIS-OF-SER-90-AND-LYS-91 reference key 9 citation date 2007 first 10078 last 10088 name Biochemistry type journal-article volume 46 title Structures-of-rat-cytosolic-PEPCK:-insight-into-the-mechanism-of-phosphorylation-and-decarboxylation-of-oxaloacetic-acid. authorList person name Sullivan-S.M. person name Holyoak-T. dbReference id 17685635 type PubMed dbReference id 10.1021/bi701038x type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.65-ANGSTROMS)-OF-APOENZYME-AND-IN-COMPLEX-WITH-MANGANESE;-GTP-AND-SUBSTRATE scope COFACTOR scope SUBUNIT scope REACTION-MECHANISM reference key 10 citation date 2008 first 2099 last 2109 name Biochemistry type journal-article volume 47 title Differential-inhibition-of-cytosolic-PEPCK-by-substrate-analogues.-Kinetic-and-structural-characterization-of-inhibitor-recognition. authorList person name Stiffin-R.M. person name Sullivan-S.M. person name Carlson-G.M. person name Holyoak-T. dbReference id 18197707 type PubMed dbReference id 10.1021/bi7020662 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.80-ANGSTROMS)-IN-COMPLEX-WITH-MANGANESE-AND-SUBSTRATE-ANALOG scope COFACTOR scope SUBUNIT reference key 11 citation date 2008 first 13829 last 13834 name Proc.-Natl.-Acad.-Sci.-U.S.A. type journal-article volume 105 title Enzymes-with-lid-gated-active-sites-must-operate-by-an-induced-fit-mechanism-instead-of-conformational-selection. authorList person name Sullivan-S.M. person name Holyoak-T. dbReference id 18772387 type PubMed dbReference id 10.1073/pnas.0805364105 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.3-ANGSTROMS)-OF-APOENZYME-AND-IN-COMPLEX-WITH-MANGANESE;-GTP-AND-SUBSTRATE scope COFACTOR scope SUBUNIT scope REACTION-MECHANISM reference key 12 citation date 2010 first 5176 last 5187 name Biochemistry type journal-article volume 49 title Increasing-the-conformational-entropy-of-the-Omega-loop-lid-domain-in-phosphoenolpyruvate-carboxykinase-impairs-catalysis-and-decreases-catalytic-fidelity. authorList person name Johnson-T.A. person name Holyoak-T. dbReference id 20476774 type PubMed dbReference id 10.1021/bi100399e type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.25-ANGSTROMS)-IN-COMPLEX-WITH-MANGANESE;-GTP-AND-SUBSTRATES scope COFACTOR scope SUBUNIT reference key 13 citation date 2012 first 9547 last 9559 name Biochemistry type journal-article volume 51 title The-Omega-loop-lid-domain-of-phosphoenolpyruvate-carboxykinase-is-essential-for-catalytic-function. authorList person name Johnson-T.A. person name Holyoak-T. dbReference id 23127136 type PubMed dbReference id 10.1021/bi301278t type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.20-ANGSTROMS)-OF-1-463-AND-475-622-IN-COMPLEX-WITH-MANGANESE;-GTP-AND-SUBSTRATES scope COFACTOR scope ACTIVE-SITE reference key 14 citation date 2014 first 161 last 170 name Mol.-Genet.-Metab. type journal-article volume 113 title Three-rare-diseases-in-one-sib-pair:-RAI1,-PCK1,-GRIN2B-mutations-associated-with-Smith-Magenis-Syndrome,-cytosolic-PEPCK-deficiency-and-NMDA-receptor-glutamate-insensitivity. authorList person name Adams-D.R. person name Yuan-H. person name Holyoak-T. person name Arajs-K.H. person name Hakimi-P. person name Markello-T.C. person name Wolfe-L.A. person name Vilboux-T. person name Burton-B.K. person name Fajardo-K.F. person name Grahame-G. person name Holloman-C. person name Sincan-M. person name Smith-A.C. person name Wells-G.A. person name Huang-Y. person name Vega-H. person name Snyder-J.P. person name Golas-G.A. person name Tifft-C.J. person name Boerkoel-C.F. person name Hanson-R.W. person name Traynelis-S.F. person name Kerr-D.S. person name Gahl-W.A. dbReference id 24863970 type PubMed dbReference id 10.1016/j.ymgme.2014.04.001 type DOI scope X-RAY-CRYSTALLOGRAPHY-(2.00-ANGSTROMS)-IN-COMPLEX-WITH-MANGANESE;-GTP-AND-SUBSTRATE scope COFACTOR scope SUBUNIT reference evidence 23-24-25-26 key 15 citation date 2015 first 5878 last 5887 name Biochemistry type journal-article volume 54 title Inhibition-and-allosteric-regulation-of-monomeric-phosphoenolpyruvate-carboxykinase-by-3-mercaptopicolinic-acid. authorList person name Balan-M.D. person name Mcleod-M.J. person name Lotosky-W.R. person name Ghaly-M. person name Holyoak-T. dbReference id 26322521 type PubMed dbReference id 10.1021/acs.biochem.5b00822 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.40-ANGSTROMS)-IN-COMPLEX-WITH-3-MERCAPTOPICOLINATE;-GTP-AND-MANGANESE scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope SUBUNIT scope ACTIVITY-REGULATION reference evidence 27-28-29-30-31-32 key 16 citation date 2016 first 575 last 587 name Biochemistry type journal-article volume 55 title Utilization-of-substrate-intrinsic-binding-energy-for-conformational-change-and-catalytic-function-in-phosphoenolpyruvate-carboxykinase. authorList person name Johnson-T.A. person name Mcleod-M.J. person name Holyoak-T. dbReference id 26709450 type PubMed dbReference id 10.1021/acs.biochem.5b01215 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.49-ANGSTROMS)-IN-COMPLEX-WITH-GTP-AND-MANGANESE scope FUNCTION scope CATALYTIC-ACTIVITY scope BIOPHYSICOCHEMICAL-PROPERTIES scope COFACTOR scope SUBUNIT scope MUTAGENESIS-OF-GLU-89 reference evidence 33-34-35-36-37 key 17 citation date 2017 first 2106 last 2115 name Biochemistry type journal-article volume 56 title Asymmetric-anchoring-is-required-for-efficient-omega-loop-opening-and-closing-in-cytosolic-phosphoenolpyruvate-carboxykinase. authorList person name Cui-D.S. person name Broom-A. person name Mcleod-M.J. person name Meiering-E.M. person name Holyoak-T. dbReference id 28345895 type PubMed dbReference id 10.1021/acs.biochem.7b00178 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.80-ANGSTROMS)-IN-COMPLEX-WITH-GTP-AND-MANGANESE scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope SUBUNIT scope ACTIVITY-REGULATION scope MUTAGENESIS-OF-HIS-477 reference evidence 38 key 18 citation date 2019 first 3918 last 3926 name Biochemistry type journal-article volume 58 title Characterization-of-3-[(carboxymethyl)thio]picolinic-acid:-a-novel-inhibitor-of-phosphoenolpyruvate-carboxykinase. authorList person name Mcleod-M.J. person name Krismanich-A.P. person name Assoud-A. person name Dmitrienko-G.I. person name Holyoak-T. dbReference id 31461616 type PubMed dbReference id 10.1021/acs.biochem.9b00583 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.49-ANGSTROMS)-IN-COMPLEX-WITH-3-[(CARBOXYMETHYL)THIO]PICOLINATE-AND-MANGANESE comment type function text evidence 1-3-11-12-13-15-16-17 Cytosolic-phosphoenolpyruvate-carboxykinase-that-catalyzes-the-reversible-decarboxylation-and-phosphorylation-of-oxaloacetate-(OAA)-and-acts-as-the-rate-limiting-enzyme-in-gluconeogenesis-(PubMed:4186849,-PubMed:30193097,-PubMed:26322521,-PubMed:26709450,-PubMed:28345895,-PubMed:31461616).-Regulates-cataplerosis-and-anaplerosis,-the-processes-that-control-the-levels-of-metabolic-intermediates-in-the-citric-acid-cycle-(PubMed:30193097).-At-low-glucose-levels,-it-catalyzes-the-cataplerotic-conversion-of-oxaloacetate-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-(PubMed:30193097).-At-high-glucose-levels,-it-catalyzes-the-anaplerotic-conversion-of-phosphoenolpyruvate-to-oxaloacetate-(PubMed:30193097).-Acts-as-a-regulator-of-formation-and-maintenance-of-memory-CD8(+)-T-cells:-up-regulated-in-these-cells,-where-it-generates-phosphoenolpyruvate,-via-gluconeogenesis-(By-similarity).-The-resultant-phosphoenolpyruvate-flows-to-glycogen-and-pentose-phosphate-pathway,-which-is-essential-for-memory-CD8(+)-T-cells-homeostasis-(By-similarity).-In-addition-to-the-phosphoenolpyruvate-carboxykinase-activity,-also-acts-as-a-protein-kinase-when-phosphorylated-at-Ser-90:-phosphorylation-at-Ser-90-by-AKT1-reduces-the-binding-affinity-to-oxaloacetate-and-promotes-an-atypical-serine-protein-kinase-activity-using-GTP-as-donor-(By-similarity).-The-protein-kinase-activity-regulates-lipogenesis:-upon-phosphorylation-at-Ser-90,-translocates-to-the-endoplasmic-reticulum-and-catalyzes-phosphorylation-of-INSIG-proteins-(INSIG1-and-INSIG2),-thereby-disrupting-the-interaction-between-INSIG-proteins-and-SCAP-and-promoting-nuclear-translocation-of-SREBP-proteins-(SREBF1/SREBP1-or-SREBF2/SREBP2)-and-subsequent-transcription-of-downstream-lipogenesis-related-genes-(By-similarity). comment type catalytic-activity reaction evidence 11-12-13-15-16 text GTP-+-oxaloacetate-=-CO2-+-GDP-+-phosphoenolpyruvate dbReference id RHEA:10388 type Rhea dbReference id CHEBI:16452 type ChEBI dbReference id CHEBI:16526 type ChEBI dbReference id CHEBI:37565 type ChEBI dbReference id CHEBI:58189 type ChEBI dbReference id CHEBI:58702 type ChEBI dbReference id 4.1.1.32 type EC physiologicalReaction direction left-to-right evidence 11-15 dbReference id RHEA:10389 type Rhea physiologicalReaction direction right-to-left evidence 11-13-15 dbReference id RHEA:10390 type Rhea comment type catalytic-activity reaction evidence 1 text GTP-+-L-seryl-[protein]-=-GDP-+-H(+)-+-O-phospho-L-seryl-[protein] dbReference id RHEA:64020 type Rhea dbReference id RHEA-COMP:9863 type Rhea dbReference id RHEA-COMP:11604 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:29999 type ChEBI dbReference id CHEBI:37565 type ChEBI dbReference id CHEBI:58189 type ChEBI dbReference id CHEBI:83421 type ChEBI physiologicalReaction direction left-to-right evidence 1 dbReference id RHEA:64021 type Rhea comment type cofactor cofactor evidence 4-5-7-8-9-10-11-12-13 name Mn(2+) dbReference id CHEBI:29035 type ChEBI text evidence 4-5-7-8-9-10-11-12-13 Binds-1-Mn(2+)-ion-per-subunit. comment type activity-regulation text evidence 1-11-15-16 Phosphoenolpyruvate-carboxykinase-activity-is-regulated-by-acetylation-and-glucose-levels-(PubMed:30193097).-The-anaplerotic-conversion-of-phosphoenolpyruvate-to-oxaloacetate-is-improved-by-PCK1-acetylation-on-Lys-91-(K91ac),-Lys-473-(K473ac)-and-Lys-521-(K521ac)-(PubMed:30193097).-High-glucose-concentrations-favor-PCK1-anaplerotic-activity-by-triggering-acetylation-on-Lys-91-(K91ac).-At-low-glucose-levels,-SIRT1-mediated-deacetylation-of-Lys-91-promotes-the-cataplerotic-conversion-of-oxaloacetate-to-phosphoenolpyruvate-(By-similarity).-Phosphoenolpyruvate-carboxykinase-activity-is-inhibited-by-3-mercaptopicolinate-(PubMed:26322521).-Phosphoenolpyruvate-carboxykinase-activity-is-inhibited-by-3-[(carboxymethyl)thio]picolinate-(CMP),-which-acts-as-a-competitive-inhibitor-at-the-oxaloacetate/phosphoenolpyruvate-binding-site-(PubMed:31461616).-Phosphorylation-at-Ser-90-reduces-the-binding-affinity-to-oxaloacetate-and-converts-the-enzyme-into-an-atypical-protein-kinase-using-GTP-as-donor-(By-similarity). comment type biophysicochemical-properties kinetics KM evidence 15 39-uM-for-oxaloacetate KM evidence 15 161-uM-for-GTP KM evidence 15 301-uM-for-phosphoenolpyruvate KM evidence 15 79-uM-for-GDP KM evidence 12 475-uM-for-phosphoenolpyruvate-(for-phosphoenolpyruvate-carboxykinase-in-the-backward-reaction) KM evidence 12 207-uM-for-GDP-(for-phosphoenolpyruvate-carboxykinase-in-the-backward-reaction) KM evidence 12 435-uM-for-CO2-(for-phosphoenolpyruvate-carboxykinase-in-the-backward-reaction) KM evidence 12 51-uM-for-oxaloacetate-(for-phosphoenolpyruvate-carboxykinase-in-the-forward-reaction) KM evidence 12 55-uM-for-GTP-(for-phosphoenolpyruvate-carboxykinase-in-the-forward-reaction) text evidence 12-15 kcat-is-76-sec(-1)-with-oxaloacetate-as-substrate-(PubMed:30193097).-kcat-is-27-sec(-1)-with-phosphoenolpyruvate-as-substrate-(PubMed:30193097).-kcat-is-65-sec(-1)-with-GTP-as-substrate-(PubMed:30193097).-kcat-is-25-sec(-1)-with-GDP-as-substrate-(PubMed:30193097).-kcat-is-52-sec(-1)-with-phosphoenolpyruvate-carboxykinase-in-the-forward-reaction-(PubMed:26709450).-kcat-is-19-sec(-1)-with-phosphoenolpyruvate-carboxykinase-in-the-backward-forward-reaction-(PubMed:26709450). comment type pathway text evidence 15 Carbohydrate-biosynthesis;-gluconeogenesis. comment type subunit text evidence 4-5-7-8-10-11-12-16 Monomer. comment type subcellular-location subcellularLocation location evidence 21 Cytoplasm location evidence 21 Cytosol subcellularLocation location evidence 1 Endoplasmic-reticulum text evidence 1 Phosphorylation-at-Ser-90-promotes-translocation-to-the-endoplasmic-reticulum. comment type induction text evidence 6-18 Regulated-by-cAMP,-dexamethasone,-glucagon-and-by-insulin.-Dexamthasone,-glucagon-and-cAMP-increase-levels,-insulin-decreases-levels. comment type PTM text evidence 1-15 Acetylated-(PubMed:30193097).-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.-Deacetylation-of-Lys-91-is-carried-out-by-SIRT1-and-depends-on-PCK1-phosphorylation-levels-(By-similarity). comment type PTM text evidence 1-15 Phosphorylated-in-a-GSK3B-mediated-pathway;-phosphorylation-affects-the-efficiency-of-SIRT1-mediated-deacetylation,-and-regulates-PCK1-ubiquitination-and-degradation-(PubMed:30193097).-Phosphorylation-at-Ser-90-by-AKT1-reduces-the-binding-affinity-to-oxaloacetate-and-promotes-the-protein-kinase-activity:-phosphorylated-PCK1-translocates-to-the-endoplasmic-reticulum,-where-it-phosphorylates-INSIG1-and-INSIG2-(By-similarity). comment type PTM text evidence 1 Ubiquitination-by-UBR5-leads-to-proteasomal-degradation. comment type miscellaneous text evidence 20 In-eukaryotes-there-are-two-isozymes:-a-cytoplasmic-one-and-a-mitochondrial-one. comment type similarity text evidence 20 Belongs-to-the-phosphoenolpyruvate-carboxykinase-[GTP]-family. dbReference evidence 11-12-13-15-16 id 4.1.1.32 type EC dbReference evidence 1 id 2.7.11.- type EC dbReference id K03248 type EMBL property type protein-sequence-ID value AAC98698.1 property type molecule-type value Genomic_DNA dbReference id K03243 type EMBL property type protein-sequence-ID value AAC98698.1 property type status value JOINED property type molecule-type value Genomic_DNA dbReference id K03244 type EMBL property type protein-sequence-ID value AAC98698.1 property type status value JOINED property type molecule-type value Genomic_DNA dbReference id K03245 type EMBL property type protein-sequence-ID value AAC98698.1 property type status value JOINED property type molecule-type value Genomic_DNA dbReference id K03246 type EMBL property type protein-sequence-ID value AAC98698.1 property type status value JOINED property type molecule-type value Genomic_DNA dbReference id K03247 type EMBL property type protein-sequence-ID value AAC98698.1 property type status value JOINED property type molecule-type value Genomic_DNA dbReference id BC081900 type EMBL property type protein-sequence-ID value AAH81900.1 property type molecule-type value mRNA dbReference id A23927 type PIR property type entry-name value QYRTGP dbReference id NP_942075.1 type RefSeq property type nucleotide-sequence-ID value NM_198780.3 dbReference id 2QEW type PDB property type method value X-ray property type resolution value 1.80-A property type chains value A=1-622 dbReference id 2QEY type PDB property type method value X-ray property type resolution value 1.90-A property type chains value A=1-622 dbReference id 2QF1 type PDB property type method value X-ray property type resolution value 1.80-A property type chains value A=1-622 dbReference id 2QF2 type PDB property type method value X-ray property type resolution value 1.65-A property type chains value A/B=1-622 dbReference id 2RK7 type PDB property type method value X-ray property type resolution value 1.90-A property type chains value A/B=1-622 dbReference id 2RK8 type PDB property type method value X-ray property type resolution value 2.00-A property type chains value A/B=1-622 dbReference id 2RKA type PDB property type method value X-ray property type resolution value 1.95-A property type chains value A/C=1-622 dbReference id 2RKD type PDB property type method value X-ray property type resolution value 1.90-A property type chains value A=1-622 dbReference id 2RKE type PDB property type method value X-ray property type resolution value 1.80-A property type chains value A=1-622 dbReference id 3DT2 type PDB property type method value X-ray property type resolution value 1.50-A property type chains value A=1-622 dbReference 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type match-status value 1 dbReference id SSF53795 type SUPFAM property type entry-name value PEP-carboxykinase-like property type match-status value 1 dbReference id PS00505 type PROSITE property type entry-name value PEPCK_GTP property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0007 Acetylation keyword id KW-0963 Cytoplasm keyword id KW-0210 Decarboxylase keyword id KW-0903 Direct-protein-sequencing keyword id KW-0256 Endoplasmic-reticulum keyword id KW-0312 Gluconeogenesis keyword id KW-0342 GTP-binding keyword id KW-0418 Kinase keyword id KW-0456 Lyase keyword id KW-0464 Manganese keyword id KW-0479 Metal-binding keyword id KW-0547 Nucleotide-binding keyword id KW-0597 Phosphoprotein keyword id KW-1185 Reference-proteome keyword id KW-0808 Transferase keyword id KW-0832 Ubl-conjugation feature description Phosphoenolpyruvate-carboxykinase,-cytosolic-[GTP] id PRO_0000103630 type chain location begin position 1 end position 622 feature description Omega-loop evidence 13 type region-of-interest location begin position 457 end position 487 feature evidence 9-14 type active-site location position position 288 feature evidence 4-7-8-9-10 type binding-site location position position 87 ligand name substrate feature evidence 5-7-8-9-10 type binding-site location begin position 235 end position 237 ligand name substrate feature evidence 4-5-7-8-9-10-11-12-13-16-24-27-28-29-30-31-32-34-35-36-38 type binding-site location position position 244 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature evidence 4-5-7-8-9-10-11-12-13-16-24-27-28-29-30-31-32-34-35-36-38 type binding-site location position position 264 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature evidence 4-5-7-8-9-10 type binding-site location position position 286 ligand name substrate feature evidence 4-7-8-9-10-11-12-13-24-27-28-29-30-31-34-35-36 type binding-site location begin position 287 end position 292 ligand name GTP dbReference id CHEBI:37565 type ChEBI feature evidence 4-5-7-8-9-10-11-12-13-16-24-27-28-29-30-31-32-34-35-36-38 type binding-site location position position 311 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature evidence 5-7-8-9-10 type binding-site location begin position 403 end position 405 ligand name substrate feature evidence 4-8-9-10-11-12-13-24-27-28-29-30-31-34-35-36 type binding-site location position position 405 ligand name GTP dbReference id CHEBI:37565 type ChEBI feature evidence 4-7-8-9-10-11-12-13-24-27-28-29-30-31-34-35-36 type binding-site location position position 436 ligand name GTP dbReference id CHEBI:37565 type ChEBI feature evidence 4-7-8-9-10-11-12-13-24-27-28-29-30-31-34-35-36 type binding-site location begin position 530 end position 533 ligand name GTP dbReference id CHEBI:37565 type ChEBI feature description Phosphoserine evidence 39 type modified-residue location position position 19 feature description N6-acetyllysine;-by-p300/EP300 evidence 1 type modified-residue location position position 70 feature description N6-acetyllysine;-by-p300/EP300 evidence 1 type modified-residue location position position 71 feature description Phosphoserine evidence 1 type modified-residue location position position 90 feature description N6-acetyllysine;-by-p300/EP300 evidence 1-15 type modified-residue location position position 91 feature description Phosphoserine evidence 39 type modified-residue location position position 118 feature description Phosphothreonine evidence 2 type modified-residue location position position 178 feature description Phosphoserine evidence 2 type modified-residue location position position 286 feature description N6-acetyllysine evidence 15 type modified-residue location position position 473 feature description N6-acetyllysine evidence 15 type modified-residue location position position 521 feature description N6-acetyllysine evidence 15 type modified-residue location position position 524 feature description N6-acetyllysine;-by-p300/EP300 evidence 1 type modified-residue location position position 594 feature description Abolished-phosphoenolpyruvate-carboxykinase-activity;-decreased-affinity-for-oxaloacetate. evidence 12 type mutagenesis-site original E variation A variation D variation Q location position position 89 feature description Decreased-phosphorylation-and-increased-acetylation-levels. evidence 15 type mutagenesis-site original S variation A location position position 90 feature description 3-fold-decrease-of-affinity-for-phosphoenolpyruvate. evidence 15 type mutagenesis-site original K variation Q location position position 91 feature description Destabilization-of-the-closed-state-of-the-omega-loop,-resulting-in-decreased-capture-rates-for-the-weaker-binding-substrates-associated-with-catalysis-in-the-phosphoenolpyruvate-to-oxaloacetate-direction. evidence 13 type mutagenesis-site original H variation R location position position 477 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dbReference id 5V9F type PDB evidence key 36 type ECO:0007744 source dbReference id 5V9G type PDB evidence key 37 type ECO:0007744 source dbReference id 5V9H type PDB evidence key 38 type ECO:0007744 source dbReference id 6P5O type PDB evidence key 39 type ECO:0007744 source ref 3903 evidence key 40 type ECO:0007829 source dbReference id 2RKD type PDB evidence key 41 type ECO:0007829 source dbReference id 3DT4 type PDB evidence key 42 type ECO:0007829 source dbReference id 3MOE type PDB evidence key 43 type ECO:0007829 source dbReference id 4GMU type PDB evidence key 44 type ECO:0007829 source dbReference id 4GNQ type PDB evidence key 45 type ECO:0007829 source dbReference id 5FH4 type PDB evidence key 46 type ECO:0007829 source dbReference id 6YI9 type PDB sequence checksum F800F73F8F127B04 length 622 mass 69416 modified 1988-04-01 version 1 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entry created 1986-07-21 dataset Swiss-Prot modified 2023-02-22 version 148 accession P0A988 accession P00583 accession Q2M813 name DPO3B_ECOLI protein recommendedName fullName evidence 30 Beta-sliding-clamp shortName Beta-clamp shortName Sliding-clamp alternativeName fullName Beta-clamp-processivity-factor alternativeName fullName DNA-polymerase-III-beta-sliding-clamp-subunit gene name type primary dnaN name type ordered-locus b3701 name type ordered-locus JW3678 organism name type scientific Escherichia-coli-(strain-K12) dbReference id 83333 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Enterobacterales taxon Enterobacteriaceae taxon Escherichia reference key 1 citation date 1984 first 159 last 170 name Gene type journal-article volume 28 title Structural-analysis-of-the-dnaA-and-dnaN-genes-of-Escherichia-coli. authorList person name Ohmori-H. person name Kimura-M. person name Nagata-T. person name Sakakibara-Y. dbReference id 6234204 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Cellular-DNA-replicases:-components-and-dynamics-at-the-replication-fork. authorList person name Johnson-A. person name O'Donnell-M. dbReference id 15952889 type PubMed dbReference id 10.1146/annurev.biochem.73.011303.073859 type DOI scope REVIEW comment type function text evidence 1-7-8-11-12-13-14-17-19-22-24-25-26-28-32 Confers-DNA-tethering-and-processivity-to-DNA-polymerases-and-other-proteins.-Acts-as-a-clamp,-forming-a-ring-around-DNA-(a-reaction-catalyzed-by-the-clamp-loading-complex)-which-diffuses-in-an-ATP-independent-manner-freely-and-bidirectionally-along-dsDNA-(PubMed:2040637).-DNA-bound-in-the-ring-is-bent-22-degrees,-in-solution-primed-DNA-is-bound-more-tightly-than-dsDNA,-suggesting-the-clamp-binds-both-ss--and-dsDNA-(PubMed:18191219).-In-a-complex-of-DNA-with-this-protein,-alpha,-epsilon-and-tau-subunits-however-the-DNA-is-only-slightly-bent-(PubMed:26499492).-Coordinates-protein-traffic-at-the-replication-fork,-where-it-interacts-with-multiple-DNA-polymerases,-repair-factors-and-other-proteins-(PubMed:15466025,-PubMed:16168375,-PubMed:22716942,-PubMed:14592985,-PubMed:14729336,-PubMed:26499492,-PubMed:15952889).-Initially-characterized-for-its-ability-to-contact-the-alpha-subunit-(dnaE)-of-DNA-polymerase-III-(Pol-III),-tethering-it-to-the-DNA-and-conferring-very-high-processivity-(PubMed:2040637).-Pol-III-is-a-complex,-multichain-enzyme-responsible-for-most-of-the-replicative-synthesis-in-bacteria;-it-also-exhibits-3'-5'-exonuclease-proofreading-activity.-The-beta-chain-is-required-for-initiation-of-replication-as-well-as-for-processivity-of-DNA-replication-(PubMed:3519609,-PubMed:2040637).-A-single-clamp-can-bind-both-Pol-III-and-IV,-allowing-the-repair-Pol-IV-to-access-DNA-when-it-is-damaged-and-needs-to-be-fixed,-a-process-the-replicative-polymerase-cannot-perform;-when-DNA-is-repaired-Pol-III-takes-over-again-(PubMed:16168375).-Serves-as-a-processivity-factor-for-DNA-polymerases-II-(PubMed:1999435,-PubMed:1534562),-IV-(PubMed:10801133)-and-V-(PubMed:10801133).-A-shorter-protein-beta*-may-be-important-for-increasing-survival-after-UV-irradiation,-and-stimulates-DNA-synthesis-with-increased-processivity-in-the-presence-of-core-Pol-III-plus-the-clamp-loader-complex-(PubMed:8576210,-PubMed:8576212). comment type subunit text evidence 2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-19-20-21-22-23-24-28-29 Forms-a-ring-shaped-head-to-tail-homodimer-(PubMed:2040637,-PubMed:9927437,-PubMed:1349852,-PubMed:12832762,-PubMed:14592985,-PubMed:14729336,-PubMed:18191219,-PubMed:18678908)-around-DNA-(PubMed:18191219),-which-can-be-opened-by-the-delta-subunit-(PubMed:9927437,-PubMed:11525728).-Binds-interacting-factors-in-a-hydrophobic-surface-cleft-between-domains-2-and-3,-each-monomer-is-able-to-bind-different-proteins-simultaneously-(PubMed:16168375,-PubMed:11525728,-PubMed:14592985,-PubMed:14729336,-PubMed:26499492).-The-beta*-isoform-probably-forms-homotrimers-which-probably-load-onto-DNA-(PubMed:8576212).-The-DNA-polymerase-III-holoenzyme-complex-contains-at-least-10-different-subunits-organized-into-3-functionally-essential-subassemblies:-the-Pol-III-core,-the-beta-sliding-clamp-processivity-factor-and-the-clamp-loading-complex.-The-Pol-III-core-(subunits-alpha,-epsilon-and-theta)-contains-the-polymerase-and-the-3'-5'-exonuclease-proofreading-activities.-The-polymerase-is-tethered-to-the-template-via-the-dimeric-beta-sliding-clamp-processivity-factor-(this-entry)-(PubMed:15466025).-The-clamp-loader-(also-called-gamma-complex)-assembles-the-beta-sliding-clamp-onto-the-primed-template-and-plays-a-central-role-in-the-organization-and-communication-at-the-replication-fork.-The-clamp-loader-contains-delta,-delta',-psi-and-chi,-and-3-copies-of-either-or-both-of-two-different-DnaX-proteins,-gamma-and-tau.-The-DNA-replisome-complex-has-a-single-clamp-loader-(3-tau-and-1-each-of-delta,-delta',-psi-and-chi-subunits)-which-binds-3-Pol-III-cores-(1-core-on-the-leading-strand-and-2-on-the-lagging-strand)-each-with-a-beta-sliding-clamp-dimer.-Additional-proteins-in-the-replisome-are-other-copies-of-gamma,-psi-and-chi,-Ssb,-DNA-helicase-and-RNA-primase-(PubMed:20413500,-PubMed:22157955,-PubMed:26499492).-The-beta-sliding-clamp-can-also-be-part-of-the-RIDA-complex-(regulatory-inactivation-of-DnaA),-consisting-of-ATP-DnaA,-ADP-Hda-and-DNA-loaded-beta-clamp-(PubMed:15150238,-PubMed:18977760,-PubMed:22716942).-Also-interacts-with-a-number-of-other-DNA-machines-such-as-DNA-polymerases-I-(PubMed:11459978),-II-(PubMed:1999435,-PubMed:1534562),-IV-(PubMed:14729336)-and-V,-DNA-mismatch-repair-enzyme-MutS-(PubMed:11459978,-PubMed:11573000)-and-DNA-ligase-(PubMed:11459978).-Binds-to-CrfC-homooligomers-at-the-midcell-position-during-DNA-replication-(PubMed:23994470).-Many-proteins-that-bind-the-beta-sliding-clamp-have-the-consensus-sequence-Gln-Leu[Ser/Asp]Leu-Phe-(PubMed:15134440). comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-545297 id P77395 label cnoX organismsDiffer false experiments 2 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-1037359 id Q47155 label dinB organismsDiffer false experiments 2 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-549111 id P10443 label dnaE organismsDiffer false experiments 19 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-542385 id P0A988 label dnaN organismsDiffer false experiments 9 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-549131 id P03007 label dnaQ organismsDiffer false experiments 6 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-549140 id P06710 label dnaX organismsDiffer false experiments 4 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-545453 id P69931 label hda organismsDiffer false experiments 9 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-549153 id P28630 label holA organismsDiffer false experiments 10 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-561113 id P0AFX0 label hpf organismsDiffer false experiments 2 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-546020 id P0AG07 label rpe organismsDiffer false experiments 4 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-370752 id P0A8E7 label yajQ organismsDiffer false experiments 2 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-555656 id P0AC53 label zwf organismsDiffer false experiments 2 comment type interaction interactant intactId EBI-542385 id P0A988 interactant intactId EBI-2434514 id P05845 label tnsE organismsDiffer true experiments 4 comment type subcellular-location subcellularLocation location evidence 23 Cytoplasm text evidence 23 Localizes-to-midcell-position-when-chromosomes-are-condensed-during-DNA-replication-(PubMed:23994470). comment type alternative-products event type alternative-promoter isoform id P0A988-1 name evidence 27 Beta sequence type displayed isoform id P0A988-2 name evidence 27 Beta* sequence ref VSP_059030 type described comment type induction text evidence 18-26-27 Induced-1.5-fold-by-hydroxyurea-(PubMed:20005847).-A-shorter-isoform,-beta*-is-induced-by-UV-treatment-and-also-at-low-levels-in-late-logarithmic/early-stationary-phase-growth-(at-protein-level)-(PubMed:8576210).-Beta*-transcription-induced-by-naldixic-acid-(PubMed:8576211). comment type biotechnology text evidence 15 Small-molecules-can-bind-to-the-hydrophobic-cleft-and-inhibit-binding-of-various-protein-factors,-suggesting-this-may-make-and-attractive-antibiotic-target-(PubMed:18678908). comment type miscellaneous text evidence 12 The-temperature--and-UV-sensitive-allele-dnaN159-does-not-grow-at-temperatures-higher-than-37-degrees-Celsius.-The-global-SOS-response-is-chronically-induced.-The-UV-sensitivity-of-dnaN159-is-dependent-upon-Pol-IV-(dinB),-it-has-an-enhanced-Pol-V-dependent-mutation-rate-(umuC,-umuD),-and-is-absolutely-dependent-on-the-polymerase-activity-of-Pol-I-(polA)-for-viability. comment type miscellaneous molecule Isoform-Beta* text evidence 26-27 Beta*-protein-is-expressed-in-late-logarithmic/early-stationary-phase-and-induced-by-UV-treatment-(PubMed:8576210).-Mutations-in-the-Shine-Dalgarno-region-of-beta*-(some-silent-at-the-amino-acid-level)-decrease-production-of-beta*-(PubMed:8576211). comment type similarity text evidence 31 Belongs-to-the-beta-sliding-clamp-family. dbReference id J01602 type EMBL property type protein-sequence-ID value AAB59150.1 property type molecule-type value Genomic_DNA dbReference id L10328 type EMBL property type 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type entry-name value DNA_polIII_beta_N dbReference id PTHR30478:SF0 type PANTHER property type entry-name value BETA-SLIDING-CLAMP property type match-status value 1 dbReference id PTHR30478 type PANTHER property type entry-name value DNA-POLYMERASE-III-SUBUNIT-BETA property type match-status value 1 dbReference id PF00712 type Pfam property type entry-name value DNA_pol3_beta property type match-status value 1 dbReference id PF02767 type Pfam property type entry-name value DNA_pol3_beta_2 property type match-status value 1 dbReference id PF02768 type Pfam property type entry-name value DNA_pol3_beta_3 property type match-status value 1 dbReference id PIRSF000804 type PIRSF property type entry-name value DNA_pol_III_b property type match-status value 1 dbReference id SM00480 type SMART property type entry-name value POL3Bc property type match-status value 1 dbReference id SSF55979 type SUPFAM property type entry-name value DNA-clamp property type match-status value 3 dbReference id TIGR00663 type TIGRFAMs property type entry-name value dnan property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0877 Alternative-promoter-usage keyword id KW-0963 Cytoplasm keyword id KW-0235 DNA-replication keyword id KW-0238 DNA-binding keyword id KW-0239 DNA-directed-DNA-polymerase keyword id KW-0548 Nucleotidyltransferase keyword id KW-1185 Reference-proteome keyword id KW-0808 Transferase feature description Beta-sliding-clamp id PRO_0000105434 type chain location begin position 1 end position 366 feature description 1 evidence 31 type region-of-interest location begin position 1 end position 120 feature description 2 evidence 31 type region-of-interest location begin position 129 end position 243 feature description 3 evidence 31 type region-of-interest location begin position 245 end position 365 feature evidence 33 type binding-site location position position 24 ligand name DNA dbReference id CHEBI:16991 type ChEBI feature evidence 14 type binding-site location position position 73 ligand name DNA dbReference id CHEBI:16991 type ChEBI feature evidence 33 type binding-site location position position 149 ligand name DNA dbReference id CHEBI:16991 type ChEBI feature evidence 33 type binding-site location begin position 153 end position 154 ligand name DNA dbReference id CHEBI:16991 type ChEBI feature description In-isoform-Beta*. evidence 27 id VSP_059030 type splice-variant location begin position 1 end position 134 feature description Mild-defect-in-DNA-replication,-impaired-loading-of-clamp-on-DNA,-polymerase-speed-is-wild-type.-More-severe-replication-defect-and-very-poor-clamp-loading;-when-associated-with-A-149. evidence 14 type mutagenesis-site original R variation A location position position 24 feature description In-dnaN159;-a-temperature--and-UV-sensitive-mutation,-displays-altered-DNA-polymerase-usage,-chronically-induced-SOS-response;-when-associated-with-A-174. evidence 12 type mutagenesis-site original G variation E location position position 66 feature description Reduction-of-synthesis-of-beta*,-probably-due-to-mutation-of-its-promoter. evidence 27 type mutagenesis-site original A variation T location position position 133 feature description 3-fold-reduction-of-synthesis-of-beta*,-probably-due-to-loss-of-its-start-codon. evidence 27 type mutagenesis-site original M variation L location position position 135 feature description No-effect-on-synthesis-of-beta*. evidence 27 type mutagenesis-site original M variation L location position position 146 feature description Mild-defect-in-DNA-replication,-impaired-loading-of-clamp-on-DNA,-polymerase-speed-is-wild-type.-More-severe-replication-defect-and-very-poor-clamp-loading;-when-associated-with-A-24. evidence 14 type mutagenesis-site original Q variation A location position position 149 feature description Very-poor-loading-of-clamp-on-DNA,-polymerase-speed-is-wild-type. evidence 14 type mutagenesis-site original YY variation SS location begin position 153 end position 154 feature description In-dnaN159;-a-temperature--and-UV-sensitive-mutation,-displays-altered-DNA-polymerase-usage,-chronically-induced-SOS-response;-when-associated-with-A-66. evidence 12 type mutagenesis-site original G variation A location position position 174 feature description Monomeric-in-solution,-binds-very-tightly-to-subunit-delta-(holA).-The-monomer-binds-tightly-to-linear-and-circular-DNA.-Cannot-bind-both-Pol-III-and-IV-simultaneously. evidence 3-13-14 type mutagenesis-site original IL variation AA location begin position 272 end position 273 feature evidence 48 type strand location begin position 2 end position 6 feature evidence 48 type helix location begin position 7 end position 17 feature evidence 50 type turn location begin position 18 end position 20 feature evidence 47 type strand location begin position 26 end position 28 feature evidence 48 type helix location begin position 29 end position 31 feature evidence 48 type strand location begin position 32 end position 38 feature evidence 48 type strand location begin position 41 end position 47 feature evidence 48 type strand location begin position 49 end position 58 feature evidence 48 type strand location begin position 66 end position 71 feature evidence 48 type helix location begin position 72 end position 81 feature evidence 48 type strand location begin position 87 end position 93 feature evidence 48 type strand location begin position 96 end position 101 feature evidence 48 type strand location begin position 104 end position 109 feature evidence 48 type helix location begin position 113 end position 115 feature evidence 48 type strand location begin position 126 end position 131 feature evidence 48 type helix location begin position 132 end position 142 feature evidence 48 type helix location begin position 143 end position 145 feature evidence 48 type helix location begin position 153 end position 156 feature evidence 48 type strand location begin position 157 end position 163 feature evidence 48 type strand location begin position 166 end position 172 feature evidence 48 type strand location begin position 174 end position 183 feature evidence 48 type strand location begin position 190 end position 195 feature evidence 48 type helix location begin position 197 end position 205 feature evidence 50 type strand location begin position 209 end position 211 feature evidence 48 type strand location begin position 213 end position 218 feature evidence 48 type strand location begin position 220 end position 227 feature evidence 48 type strand location begin position 230 end position 235 feature evidence 48 type helix location begin position 244 end position 246 feature evidence 48 type strand location begin position 254 end position 259 feature evidence 48 type helix location begin position 260 end position 271 feature evidence 48 type turn location begin position 276 end position 278 feature evidence 48 type strand location begin position 280 end position 286 feature evidence 48 type strand location begin position 289 end position 295 feature evidence 48 type strand location begin position 301 end position 307 feature evidence 49 type strand location begin position 309 end position 312 feature evidence 48 type strand location begin position 315 end position 320 feature evidence 48 type helix location begin position 321 end position 331 feature evidence 48 type strand location begin position 334 end position 340 feature evidence 47 type strand location begin position 343 end position 345 feature evidence 48 type strand location begin position 347 end position 351 feature evidence 48 type strand location begin position 354 end position 361 evidence key 1 type ECO:0000269 source dbReference id 10801133 type PubMed evidence key 2 type ECO:0000269 source dbReference id 11459978 type PubMed evidence key 3 type ECO:0000269 source dbReference id 11525728 type PubMed evidence key 4 type ECO:0000269 source dbReference id 11573000 type PubMed evidence key 5 type ECO:0000269 source dbReference id 12832762 type PubMed evidence key 6 type ECO:0000269 source dbReference id 1349852 type PubMed evidence key 7 type ECO:0000269 source dbReference id 14592985 type PubMed evidence key 8 type ECO:0000269 source dbReference id 14729336 type PubMed evidence key 9 type ECO:0000269 source dbReference id 15134440 type PubMed evidence key 10 type ECO:0000269 source dbReference id 15150238 type PubMed evidence key 11 type ECO:0000269 source dbReference id 1534562 type PubMed evidence key 12 type ECO:0000269 source dbReference id 15466025 type PubMed evidence key 13 type ECO:0000269 source dbReference id 16168375 type PubMed evidence key 14 type ECO:0000269 source dbReference id 18191219 type PubMed evidence key 15 type ECO:0000269 source dbReference id 18678908 type PubMed evidence key 16 type ECO:0000269 source dbReference id 18977760 type PubMed evidence key 17 type ECO:0000269 source dbReference id 1999435 type PubMed evidence key 18 type ECO:0000269 source dbReference id 20005847 type PubMed evidence key 19 type ECO:0000269 source dbReference id 2040637 type PubMed evidence key 20 type ECO:0000269 source dbReference id 20413500 type PubMed evidence key 21 type ECO:0000269 source dbReference id 22157955 type PubMed evidence key 22 type ECO:0000269 source dbReference id 22716942 type PubMed evidence key 23 type ECO:0000269 source dbReference id 23994470 type PubMed evidence key 24 type ECO:0000269 source dbReference id 26499492 type PubMed evidence key 25 type ECO:0000269 source dbReference id 3519609 type PubMed evidence key 26 type ECO:0000269 source dbReference id 8576210 type PubMed evidence key 27 type ECO:0000269 source dbReference id 8576211 type PubMed evidence key 28 type ECO:0000269 source dbReference id 8576212 type PubMed evidence key 29 type ECO:0000269 source dbReference id 9927437 type PubMed evidence key 30 type ECO:0000303 source dbReference id 2040637 type PubMed evidence key 31 type ECO:0000305 evidence key 32 type ECO:0000305 source dbReference id 15952889 type PubMed evidence key 33 type ECO:0000305 source dbReference id 18191219 type PubMed evidence key 34 type ECO:0007744 source dbReference id 1JQJ type PDB evidence key 35 type ECO:0007744 source dbReference id 1JQL type PDB evidence key 36 type ECO:0007744 source dbReference id 1MMI type PDB evidence key 37 type ECO:0007744 source dbReference id 1OK7 type PDB evidence key 38 type ECO:0007744 source dbReference id 1UNN type PDB evidence key 39 type ECO:0007744 source dbReference id 2POL type PDB evidence key 40 type ECO:0007744 source dbReference id 3BEP type PDB evidence key 41 type ECO:0007744 source dbReference id 3D1E type PDB evidence key 42 type ECO:0007744 source dbReference id 3D1F type PDB evidence key 43 type ECO:0007744 source dbReference id 3D1G type PDB evidence key 44 type ECO:0007744 source dbReference id 5FKU type PDB evidence key 45 type ECO:0007744 source dbReference id 5FKV type PDB evidence key 46 type ECO:0007744 source dbReference id 5FKW type PDB evidence key 47 type ECO:0007829 source dbReference id 1JQL type PDB evidence key 48 type ECO:0007829 source dbReference id 4K3L type PDB evidence key 49 type ECO:0007829 source dbReference id 4MJR type PDB evidence key 50 type ECO:0007829 source dbReference id 7AZ8 type PDB sequence checksum 7A45646F61255B5A length 366 mass 40587 modified 1988-04-01 version 1 MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALVQPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLDDWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVCSMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYVVMPMRL 
