AAKG3_HUMAN
ID AAKG3_HUMAN Reviewed; 489 AA.
AC Q9UGI9; Q4QQG8; Q4V779; Q9NRL1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-3;
DE Short=AMPK gamma3;
DE Short=AMPK subunit gamma-3;
GN Name=PRKAG3; Synonyms=AMPKG3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10698692; DOI=10.1042/bj3460659;
RA Cheung P.C.F., Salt I.P., Davies S.P., Hardie D.G., Carling D.;
RT "Characterization of AMP-activated protein kinase gamma-subunit isoforms
RT and their role in AMP binding.";
RL Biochem. J. 346:659-669(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=10818001; DOI=10.1126/science.288.5469.1248;
RA Milan D., Jeon J.-T., Looft C., Amarger V., Robic A., Thelander M.,
RA Rogel-Gaillard C., Paul S., Iannuccelli N., Rask L., Ronne H.,
RA Lundstroem K., Reinsch N., Gellin J., Kalm E., Le Roy P., Chardon P.,
RA Andersson L.;
RT "A mutation in PRKAG3 associated with excess glycogen content in pig
RT skeletal muscle.";
RL Science 288:1248-1251(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-71.
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 [4]
RP DOMAIN CBS, AMP-BINDING, ATP-BINDING, AND FUNCTION.
RX PubMed=14722619; DOI=10.1172/jci200419874;
RA Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A.,
RA Norman D.G., Hardie D.G.;
RT "CBS domains form energy-sensing modules whose binding of adenosine ligands
RT is disrupted by disease mutations.";
RL J. Clin. Invest. 113:274-284(2004).
RN [5]
RP DOMAIN AMPK PSEUDOSUBSTRATE.
RX PubMed=17255938; DOI=10.1038/sj.emboj.7601542;
RA Scott J.W., Ross F.A., Liu J.K., Hardie D.G.;
RT "Regulation of AMP-activated protein kinase by a pseudosubstrate sequence
RT on the gamma subunit.";
RL EMBO J. 26:806-815(2007).
RN [6]
RP REVIEW ON FUNCTION.
RX PubMed=17307971; DOI=10.1161/01.res.0000256090.42690.05;
RA Towler M.C., Hardie D.G.;
RT "AMP-activated protein kinase in metabolic control and insulin signaling.";
RL Circ. Res. 100:328-341(2007).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=17712357; DOI=10.1038/nrm2249;
RA Hardie D.G.;
RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular
RT energy.";
RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
RN [8]
RP PHOSPHORYLATION BY ULK1.
RX PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [9]
RP VARIANTS ALA-71; GLN-76; GLY-103; VAL-113; VAL-153; PRO-161; SER-171;
RP SER-180; THR-197; GLN-211; GLN-225; TRP-225; ARG-260; THR-269; CYS-307;
RP GLN-340; TRP-340; MET-446; VAL-482 AND ASN-485, INVOLVEMENT IN SMGMQTL,
RP FUNCTION, AND CHARACTERIZATION OF VARIANT TRP-225.
RX PubMed=17878938; DOI=10.1371/journal.pone.0000903;
RA Costford S.R., Kavaslar N., Ahituv N., Chaudhry S.N., Schackwitz W.S.,
RA Dent R., Pennacchio L.A., McPherson R., Harper M.E.;
RT "Gain-of-function R225W mutation in human AMPKgamma(3) causing increased
RT glycogen and decreased triglyceride in skeletal muscle.";
RL PLoS ONE 2:E903-E903(2007).
CC -!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase
CC (AMPK), an energy sensor protein kinase that plays a key role in
CC regulating cellular energy metabolism. In response to reduction of
CC intracellular ATP levels, AMPK activates energy-producing pathways and
CC inhibits energy-consuming processes: inhibits protein, carbohydrate and
CC lipid biosynthesis, as well as cell growth and proliferation. AMPK acts
CC via direct phosphorylation of metabolic enzymes, and by longer-term
CC effects via phosphorylation of transcription regulators. AMPK also acts
CC as a regulator of cellular polarity by remodeling the actin
CC cytoskeleton; probably by indirectly activating myosin. The AMPK gamma3
CC subunit is a non-catalytic subunit with a regulatory role in muscle
CC energy metabolism (PubMed:17878938). It mediates binding to AMP, ADP
CC and ATP, leading to AMPK activation or inhibition: AMP-binding results
CC in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2)
CC both by inducing phosphorylation and preventing dephosphorylation of
CC catalytic subunits. ADP also stimulates phosphorylation, without
CC stimulating already phosphorylated catalytic subunit. ATP promotes
CC dephosphorylation of catalytic subunit, rendering the AMPK enzyme
CC inactive. {ECO:0000269|PubMed:14722619, ECO:0000269|PubMed:17878938}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UGI9; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-7428853, EBI-1048945;
CC Q9UGI9; O43741: PRKAB2; NbExp=5; IntAct=EBI-7428853, EBI-1053424;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI9-2; Sequence=VSP_015587;
CC -!- TISSUE SPECIFICITY: Skeletal muscle, with weak expression in heart and
CC pancreas.
CC -!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence around
CC sites phosphorylated on target proteins of AMPK, except the presence of
CC a non-phosphorylatable residue in place of Ser. In the absence of AMP
CC this pseudosubstrate sequence may bind to the active site groove on the
CC alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the
CC upstream activating kinase STK11/LKB1.
CC -!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
CC potential nucleotide-binding sites, 3 are occupied, designated as sites
CC 1, 3, and 4 based on the CBS modules that provide the acidic residue
CC for coordination with the 2'- and 3'-hydroxyl groups of the ribose of
CC AMP. Of these, site 4 appears to be a structural site that retains a
CC tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can
CC bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-
CC affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP,
CC ADP or ATP 2) is the weakest nucleotide-binding site on the gamma
CC subunit, yet it is exquisitely sensitive to changes in nucleotide
CC levels and this allows AMPK to respond rapidly to changes in cellular
CC energy status. Site 3 is likely to be responsible for protection of a
CC conserved threonine in the activation loop of the alpha catalytic
CC subunit through conformational changes induced by binding of AMP or
CC ADP. {ECO:0000250|UniProtKB:P80385}.
CC -!- PTM: Phosphorylated by ULK1; leading to negatively regulate AMPK
CC activity and suggesting the existence of a regulatory feedback loop
CC between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}.
CC -!- POLYMORPHISM: Genetic variation in PRKAG3 defines the skeletal muscle
CC glycogen content and metabolism quantitative trait locus (SMGMQTL)
CC [MIM:619030]. Muscle fibers from carriers of variant Trp-225 have
CC approximately 90% more muscle glycogen content than controls and
CC decreased levels of intramuscular triglyceride.
CC {ECO:0000269|PubMed:17878938}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; AJ249977; CAB65117.1; -; mRNA.
DR EMBL; AF214519; AAF73987.1; -; mRNA.
DR EMBL; BC098102; AAH98102.1; -; mRNA.
DR EMBL; BC098255; AAH98255.1; -; mRNA.
DR EMBL; BC098277; AAH98277.1; -; mRNA.
DR EMBL; BC098306; AAH98306.1; -; mRNA.
DR CCDS; CCDS2424.1; -. [Q9UGI9-1]
DR RefSeq; NP_059127.2; NM_017431.2. [Q9UGI9-1]
DR RefSeq; XP_016859832.1; XM_017004343.1. [Q9UGI9-1]
DR AlphaFoldDB; Q9UGI9; -.
DR SMR; Q9UGI9; -.
DR BioGRID; 119791; 53.
DR ComplexPortal; CPX-5840; AMPK complex, alpha2-beta2-gamma3 variant.
DR ComplexPortal; CPX-5841; AMPK complex, alpha1-beta2-gamma3 variant.
DR ComplexPortal; CPX-5842; AMPK complex, alpha1-beta1-gamma3 variant.
DR ComplexPortal; CPX-5843; AMPK complex, alpha2-beta1-gamma3 variant.
DR CORUM; Q9UGI9; -.
DR IntAct; Q9UGI9; 45.
DR MINT; Q9UGI9; -.
DR STRING; 9606.ENSP00000397133; -.
DR BindingDB; Q9UGI9; -.
DR ChEMBL; CHEMBL3038452; -.
DR ChEMBL; CHEMBL3038457; -.
DR ChEMBL; CHEMBL4106159; -.
DR ChEMBL; CHEMBL4106162; -.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00273; Topiramate.
DR GlyGen; Q9UGI9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGI9; -.
DR PhosphoSitePlus; Q9UGI9; -.
DR BioMuta; PRKAG3; -.
DR DMDM; 85681287; -.
DR EPD; Q9UGI9; -.
DR MassIVE; Q9UGI9; -.
DR MaxQB; Q9UGI9; -.
DR PaxDb; Q9UGI9; -.
DR PeptideAtlas; Q9UGI9; -.
DR PRIDE; Q9UGI9; -.
DR ProteomicsDB; 84220; -. [Q9UGI9-1]
DR ProteomicsDB; 84221; -. [Q9UGI9-2]
DR Antibodypedia; 1331; 262 antibodies from 24 providers.
DR DNASU; 53632; -.
DR Ensembl; ENST00000233944.7; ENSP00000233944.3; ENSG00000115592.11. [Q9UGI9-1]
DR Ensembl; ENST00000439262.6; ENSP00000397133.3; ENSG00000115592.11. [Q9UGI9-1]
DR Ensembl; ENST00000529249.5; ENSP00000436068.1; ENSG00000115592.11. [Q9UGI9-1]
DR GeneID; 53632; -.
DR KEGG; hsa:53632; -.
DR UCSC; uc002vjb.2; human. [Q9UGI9-1]
DR CTD; 53632; -.
DR DisGeNET; 53632; -.
DR GeneCards; PRKAG3; -.
DR HGNC; HGNC:9387; PRKAG3.
DR HPA; ENSG00000115592; Group enriched (skeletal muscle, tongue).
DR MalaCards; PRKAG3; -.
DR MIM; 604976; gene.
DR MIM; 619030; phenotype.
DR neXtProt; NX_Q9UGI9; -.
DR OpenTargets; ENSG00000115592; -.
DR PharmGKB; PA33753; -.
DR VEuPathDB; HostDB:ENSG00000115592; -.
DR eggNOG; KOG1764; Eukaryota.
DR GeneTree; ENSGT00950000183019; -.
DR HOGENOM; CLU_021740_6_0_1; -.
DR OMA; DFIMVLM; -.
DR PhylomeDB; Q9UGI9; -.
DR TreeFam; TF313247; -.
DR BRENDA; 2.7.11.31; 2681.
DR PathwayCommons; Q9UGI9; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-9613354; Lipophagy.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR SignaLink; Q9UGI9; -.
DR SIGNOR; Q9UGI9; -.
DR BioGRID-ORCS; 53632; 9 hits in 1074 CRISPR screens.
DR GeneWiki; PRKAG3; -.
DR GenomeRNAi; 53632; -.
DR Pharos; Q9UGI9; Tbio.
DR PRO; PR:Q9UGI9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UGI9; protein.
DR Bgee; ENSG00000115592; Expressed in hindlimb stylopod muscle and 78 other tissues.
DR ExpressionAtlas; Q9UGI9; baseline and differential.
DR Genevisible; Q9UGI9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:ComplexPortal.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; IEA:Ensembl.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR039168; AMPKG-3.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR PANTHER; PTHR13780:SF31; PTHR13780:SF31; 1.
DR Pfam; PF00571; CBS; 3.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; CBS domain; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..489
FT /note="5'-AMP-activated protein kinase subunit gamma-3"
FT /id="PRO_0000204384"
FT DOMAIN 197..258
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 280..340
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 355..415
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 427..486
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..314
FT /note="AMPK pseudosubstrate"
FT COMPBIAS 14..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 225
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 240..245
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 240..245
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 240..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 285
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 285
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 306..307
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 306..307
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 306..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 306
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 325
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 325
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 355
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 360
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 381..382
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 397..400
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 397..400
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 397..400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 424
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 424
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 432
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 432
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 453..454
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 453..454
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 453..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 453
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 469..472
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10818001"
FT /id="VSP_015587"
FT VARIANT 71
FT /note="P -> A (in dbSNP:rs692243)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17878938"
FT /id="VAR_023484"
FT VARIANT 76
FT /note="E -> Q (in dbSNP:rs864622003)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069470"
FT VARIANT 103
FT /note="D -> G (in dbSNP:rs371222838)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069471"
FT VARIANT 113
FT /note="G -> V (in dbSNP:rs864622004)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069472"
FT VARIANT 153
FT /note="L -> V (in dbSNP:rs35050588)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_048251"
FT VARIANT 161
FT /note="L -> P (in dbSNP:rs962993719)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069473"
FT VARIANT 171
FT /note="G -> S (in dbSNP:rs200004875)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069474"
FT VARIANT 180
FT /note="G -> S (in dbSNP:rs372752820)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069475"
FT VARIANT 197
FT /note="M -> T (in dbSNP:rs776255177)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069476"
FT VARIANT 211
FT /note="E -> Q (in dbSNP:rs776263291)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069477"
FT VARIANT 225
FT /note="R -> Q (in dbSNP:rs370008874)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069478"
FT VARIANT 225
FT /note="R -> W (associated with increased glycogen content
FT and metabolism in skeletal muscle; results in increased
FT basal and AMP-activated AMPK activity; dbSNP:rs138130157)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069479"
FT VARIANT 260
FT /note="Q -> R (in dbSNP:rs41272689)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069480"
FT VARIANT 269
FT /note="I -> T (in dbSNP:rs367916025)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069481"
FT VARIANT 307
FT /note="R -> C (in dbSNP:rs864622005)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069482"
FT VARIANT 340
FT /note="R -> Q (in dbSNP:rs551272603)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069483"
FT VARIANT 340
FT /note="R -> W (in dbSNP:rs33985460)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_048252"
FT VARIANT 446
FT /note="R -> M (in dbSNP:rs200750014)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069484"
FT VARIANT 482
FT /note="A -> V (in dbSNP:rs34720726)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069485"
FT VARIANT 485
FT /note="D -> N (in dbSNP:rs149508864)"
FT /evidence="ECO:0000269|PubMed:17878938"
FT /id="VAR_069486"
FT CONFLICT 83
FT /note="A -> T (in Ref. 2; AAF73987)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="MQ -> IE (in Ref. 1; CAB65117)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="Q -> K (in Ref. 1; CAB65117)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..489
FT /note="ALGA -> PSGPEKI (in Ref. 1; CAB65117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54258 MW; 0E93E2B5117B328D CRC64;
MEPGLEHALR RTPSWSSLGG SEHQEMSFLE QENSSSWPSP AVTSSSERIR GKRRAKALRW
TRQKSVEEGE PPGQGEGPRS RPAAESTGLE ATFPKTTPLA QADPAGVGTP PTGWDCLPSD
CTASAAGSST DDVELATEFP ATEAWECELE GLLEERPALC LSPQAPFPKL GWDDELRKPG
AQIYMRFMQE HTCYDAMATS SKLVIFDTML EIKKAFFALV ANGVRAAPLW DSKKQSFVGM
LTITDFILVL HRYYRSPLVQ IYEIEQHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYTL
IKNRIHRLPV LDPVSGNVLH ILTHKRLLKF LHIFGSLLPR PSFLYRTIQD LGIGTFRDLA
VVLETAPILT ALDIFVDRRV SALPVVNECG QVVGLYSRFD VIHLAAQQTY NHLDMSVGEA
LRQRTLCLEG VLSCQPHESL GEVIDRIARE QVHRLVLVDE TQHLLGVVSL SDILQALVLS
PAGIDALGA
