AAKG_YEAST
ID AAKG_YEAST Reviewed; 322 AA.
AC P12904; D6VU32;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=5'-AMP-activated protein kinase subunit gamma;
DE Short=AMPK gamma;
DE Short=AMPK subunit gamma;
DE AltName: Full=Regulatory protein CAT3;
DE AltName: Full=Sucrose non-fermenting protein 4;
GN Name=SNF4; Synonyms=CAT3, SCI1; OrderedLocusNames=YGL115W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3049255; DOI=10.1016/0378-1119(88)90401-5;
RA Schueller H.-J., Entian K.-D.;
RT "Molecular characterization of yeast regulatory gene CAT3 necessary for
RT glucose derepression and nuclear localization of its product.";
RL Gene 67:247-257(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SNF1.
RX PubMed=2481228; DOI=10.1128/mcb.9.11.5045-5054.1989;
RA Celenza J.L., Eng F.J., Carlson M.;
RT "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence
RT for physical association of the SNF4 protein with the SNF1 protein
RT kinase.";
RL Mol. Cell. Biol. 9:5045-5054(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RA Doi A., Doi K.;
RT "Correct end of the ORF for the CDC20 gene of Saccharomyces cerevisiae.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 30-34 AND 316-322.
RX PubMed=7905477; DOI=10.1016/s0021-9258(17)41951-x;
RA Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F.,
RA Witters L.A., Kemp B.E.;
RT "Mammalian AMP-activated protein kinase shares structural and functional
RT homology with the catalytic domain of yeast Snf1 protein kinase.";
RL J. Biol. Chem. 269:2361-2364(1994).
RN [7]
RP FUNCTION.
RX PubMed=7050076; DOI=10.1128/jb.151.3.1123-1128.1982;
RA Entian K.D., Zimmermann F.K.;
RT "New genes involved in carbon catabolite repression and derepression in the
RT yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 151:1123-1128(1982).
RN [8]
RP FUNCTION.
RX PubMed=6392017; DOI=10.1093/genetics/108.4.845;
RA Neigeborn L., Carlson M.;
RT "Genes affecting the regulation of SUC2 gene expression by glucose
RT repression in Saccharomyces cerevisiae.";
RL Genetics 108:845-858(1984).
RN [9]
RP FUNCTION.
RX PubMed=3939253; DOI=10.1128/mcb.5.10.2521-2526.1985;
RA Sarokin L., Carlson M.;
RT "Upstream region of the SUC2 gene confers regulated expression to a
RT heterologous gene in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 5:2521-2526(1985).
RN [10]
RP FUNCTION.
RX PubMed=3049551; DOI=10.1128/jb.170.10.4838-4845.1988;
RA Bisson L.F.;
RT "High-affinity glucose transport in Saccharomyces cerevisiae is under
RT general glucose repression control.";
RL J. Bacteriol. 170:4838-4845(1988).
RN [11]
RP FUNCTION.
RX PubMed=2557546; DOI=10.1128/mcb.9.11.5034-5044.1989;
RA Celenza J.L., Carlson M.;
RT "Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase
RT and evidence for functional interaction with the SNF4 protein.";
RL Mol. Cell. Biol. 9:5034-5044(1989).
RN [12]
RP FUNCTION.
RX PubMed=2169717; DOI=10.1007/bf00423333;
RA Arguelles J.C., Mbonyi K., Van Aelst L., Vanhalewyn M., Jans A.W.,
RA Thevelein J.M.;
RT "Absence of glucose-induced cAMP signaling in the Saccharomyces cerevisiae
RT mutants cat1 and cat3 which are deficient in derepression of glucose-
RT repressible proteins.";
RL Arch. Microbiol. 154:199-205(1990).
RN [13]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=1468623; DOI=10.1093/genetics/132.3.639;
RA Estruch F., Treitel M.A., Yang X., Carlson M.;
RT "N-terminal mutations modulate yeast SNF1 protein kinase function.";
RL Genetics 132:639-650(1992).
RN [14]
RP FUNCTION OF THE AMPK COMPLEX.
RX PubMed=8224185; DOI=10.1016/0014-5793(93)80661-d;
RA Fernandez E., Fernandez M., Moreno F., Rodicio R.;
RT "Transcriptional regulation of the isocitrate lyase encoding gene in
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 333:238-242(1993).
RN [15]
RP FUNCTION.
RX PubMed=8544831; DOI=10.1007/bf00418035;
RA Blazquez M.A., Gancedo C.;
RT "Mode of action of the qcr9 and cat3 mutations in restoring the ability of
RT Saccharomyces cerevisiae tps1 mutants to grow on glucose.";
RL Mol. Gen. Genet. 249:655-664(1995).
RN [16]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=8985180; DOI=10.1101/gad.10.24.3105;
RA Jiang R., Carlson M.;
RT "Glucose regulates protein interactions within the yeast SNF1 protein
RT kinase complex.";
RL Genes Dev. 10:3105-3115(1996).
RN [17]
RP INTERACTION WITH SNF1; SIP1; SIP2 AND GAL83.
RX PubMed=9121458; DOI=10.1128/mcb.17.4.2099;
RA Jiang R., Carlson M.;
RT "The Snf1 protein kinase and its activating subunit, Snf4, interact with
RT distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex.";
RL Mol. Cell. Biol. 17:2099-2106(1997).
RN [18]
RP FUNCTION.
RX PubMed=10099331;
RX DOI=10.1002/(sici)1097-0290(19980720)59:2<203::aid-bit8>3.0.co;2-l;
RA Aon M.A., Cortassa S.;
RT "Catabolite repression mutants of Saccharomyces cerevisiae show altered
RT fermentative metabolism as well as cell cycle behavior in glucose-limited
RT chemostat cultures.";
RL Biotechnol. Bioeng. 59:203-213(1998).
RN [19]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=9600950; DOI=10.1073/pnas.95.11.6245;
RA Ludin K., Jiang R., Carlson M.;
RT "Glucose-regulated interaction of a regulatory subunit of protein
RT phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6245-6250(1998).
RN [20]
RP DISRUPTION PHENOTYPE.
RX PubMed=9841784; DOI=10.1007/pl00006773;
RA Aon M.A., Cortassa S.;
RT "Quantitation of the effects of disruption of catabolite (de)repression
RT genes on the cell cycle behavior of Saccharomyces cerevisiae.";
RL Curr. Microbiol. 38:57-60(1999).
RN [21]
RP INTERACTION WITH SNIF1, AND FUNCTION OF THE AMPK COMPLEX.
RX PubMed=10224244; DOI=10.1093/genetics/152.1.73;
RA Shirra M.K., Arndt K.M.;
RT "Evidence for the involvement of the Glc7-Reg1 phosphatase and the Snf1-
RT Snf4 kinase in the regulation of INO1 transcription in Saccharomyces
RT cerevisiae.";
RL Genetics 152:73-87(1999).
RN [22]
RP FUNCTION.
RX PubMed=11486005; DOI=10.1074/jbc.m104418200;
RA McCartney R.R., Schmidt M.C.;
RT "Regulation of Snf1 kinase. Activation requires phosphorylation of
RT threonine 210 by an upstream kinase as well as a distinct step mediated by
RT the Snf4 subunit.";
RL J. Biol. Chem. 276:36460-36466(2001).
RN [23]
RP IDENTIFICATION IN THE AMPK COMPLEX, AND FUNCTION OF THE AMPK COMPLEX.
RX PubMed=12393914; DOI=10.1074/jbc.m207058200;
RA Nath N., McCartney R.R., Schmidt M.C.;
RT "Purification and characterization of Snf1 kinase complexes containing a
RT defined beta subunit composition.";
RL J. Biol. Chem. 277:50403-50408(2002).
RN [24]
RP FUNCTION OF THE AMPK COMPLEX.
RX PubMed=12960168; DOI=10.1074/jbc.m307447200;
RA Haurie V., Boucherie H., Sagliocco F.;
RT "The Snf1 protein kinase controls the induction of genes of the iron uptake
RT pathway at the diauxic shift in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:45391-45396(2003).
RN [25]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [26]
RP IDENTIFICATION IN THE AMPK COMPLEX.
RX PubMed=16847059; DOI=10.1074/jbc.m603811200;
RA Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.;
RT "Subunits of the Snf1 kinase heterotrimer show interdependence for
RT association and activity.";
RL J. Biol. Chem. 281:26170-26180(2006).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=17237508; DOI=10.1534/genetics.106.068932;
RA Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A.,
RA Santangelo G.M.;
RT "Glucose-responsive regulators of gene expression in Saccharomyces
RT cerevisiae function at the nuclear periphery via a reverse recruitment
RT mechanism.";
RL Genetics 175:1127-1135(2007).
RN [28]
RP FUNCTION, AND MUTAGENESIS OF VAL-63; CYS-136; GLY-145; ARG-146; THR-166;
RP ASN-177; ASN-251 AND HIS-293.
RX PubMed=18474591; DOI=10.1074/jbc.m803624200;
RA Momcilovic M., Iram S.H., Liu Y., Carlson M.;
RT "Roles of the glycogen-binding domain and Snf4 in glucose inhibition of
RT SNF1 protein kinase.";
RL J. Biol. Chem. 283:19521-19529(2008).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 179-322, AND MUTAGENESIS OF
RP LEU-242; ARG-291 AND HIS-293.
RX PubMed=17223533; DOI=10.1016/j.str.2006.11.014;
RA Rudolph M.J., Amodeo G.A., Iram S.H., Hong S.P., Pirino G., Carlson M.,
RA Tong L.;
RT "Structure of the Bateman2 domain of yeast Snf4: dimeric association and
RT relevance for AMP binding.";
RL Structure 15:65-74(2007).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 7-321 IN COMPLEX WITH SNF1 AND
RP SIP2.
RX PubMed=17851534; DOI=10.1038/nature06127;
RA Amodeo G.A., Rudolph M.J., Tong L.;
RT "Crystal structure of the heterotrimer core of Saccharomyces cerevisiae
RT AMPK homologue SNF1.";
RL Nature 449:492-495(2007).
RN [31] {ECO:0007744|PDB:3T4N, ECO:0007744|PDB:3TDH, ECO:0007744|PDB:3TE5}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-322 IN COMPLEX WITH ADP; AMP AND
RP NAD, AND FUNCTION.
RX PubMed=22019086; DOI=10.1016/j.cmet.2011.09.009;
RA Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D.,
RA McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A., Haire L.F.,
RA Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., Carling D.;
RT "ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated
RT protein kinase.";
RL Cell Metab. 14:707-714(2011).
CC -!- FUNCTION: Adenine nucleotides-binding subunit gamma of AMP-activated
CC protein kinase (AMPK), an energy sensor protein kinase that plays a key
CC role in regulating cellular energy metabolism. In response to reduction
CC of intracellular ATP levels, AMPK activates energy-producing pathways
CC and inhibits energy-consuming processes: inhibits protein, carbohydrate
CC and lipid biosynthesis, as well as cell growth and proliferation. AMPK
CC acts via direct phosphorylation of metabolic enzymes, and by longer-
CC term effects via phosphorylation of transcription regulators. Gamma
CC non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to
CC activate or inhibit AMPK: AMP-binding results in allosteric activation
CC of alpha catalytic subunit (SNF1) both by inducing phosphorylation and
CC preventing dephosphorylation of catalytic subunits.
CC {ECO:0000269|PubMed:10099331, ECO:0000269|PubMed:10224244,
CC ECO:0000269|PubMed:11486005, ECO:0000269|PubMed:12393914,
CC ECO:0000269|PubMed:12960168, ECO:0000269|PubMed:1468623,
CC ECO:0000269|PubMed:18474591, ECO:0000269|PubMed:2169717,
CC ECO:0000269|PubMed:22019086, ECO:0000269|PubMed:2557546,
CC ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3939253,
CC ECO:0000269|PubMed:6392017, ECO:0000269|PubMed:7050076,
CC ECO:0000269|PubMed:8224185, ECO:0000269|PubMed:8544831,
CC ECO:0000269|PubMed:8985180, ECO:0000269|PubMed:9600950}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a
CC beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4).
CC Note=Interaction between SNF1 and SNF4 is inhibited by high levels of
CC glucose. {ECO:0000269|PubMed:12393914, ECO:0000269|PubMed:16847059,
CC ECO:0000269|PubMed:17851534}.
CC -!- INTERACTION:
CC P12904; P32578: SIP1; NbExp=4; IntAct=EBI-17537, EBI-17179;
CC P12904; P34164: SIP2; NbExp=9; IntAct=EBI-17537, EBI-17187;
CC P12904; P06782: SNF1; NbExp=22; IntAct=EBI-17537, EBI-17516;
CC P12904; P12904: SNF4; NbExp=4; IntAct=EBI-17537, EBI-17537;
CC P12904; P25575: YCL046W; NbExp=3; IntAct=EBI-17537, EBI-21748;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17237508,
CC ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:3049255}. Cytoplasm
CC {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228}.
CC -!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
CC potential nucleotide-binding sites, 2 are occupied, designated as sites
CC 2 and 3 based on the CBS modules that provide the acidic residue for
CC coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP.
CC Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2
CC binds specifically ADP (ADP 1) and is likely to be responsible for
CC protection of a conserved threonine in the activation loop of the alpha
CC catalytic subunit through conformational changes induced by binding of
CC ADP (PubMed:22019086). {ECO:0000269|PubMed:22019086}.
CC -!- DISRUPTION PHENOTYPE: Leads to a decrease in the length of G1 with
CC respect to the wild-type strain along with a smaller difference in the
CC cell cycle length of parent and daughter cells.
CC {ECO:0000269|PubMed:9841784}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; M21760; AAA34472.1; -; Genomic_DNA.
DR EMBL; M30470; AAA35061.1; -; Genomic_DNA.
DR EMBL; Z72637; CAA96823.1; -; Genomic_DNA.
DR EMBL; D16506; BAA03958.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07993.1; -; Genomic_DNA.
DR PIR; A38906; RGBYC3.
DR RefSeq; NP_011400.1; NM_001180980.1.
DR PDB; 2NYC; X-ray; 1.90 A; A=179-322.
DR PDB; 2NYE; X-ray; 2.50 A; A/B=179-322.
DR PDB; 2QLV; X-ray; 2.60 A; C/F=7-321.
DR PDB; 3T4N; X-ray; 2.30 A; C=2-322.
DR PDB; 3TDH; X-ray; 2.30 A; C=2-322.
DR PDB; 3TE5; X-ray; 2.50 A; C=2-322.
DR PDBsum; 2NYC; -.
DR PDBsum; 2NYE; -.
DR PDBsum; 2QLV; -.
DR PDBsum; 3T4N; -.
DR PDBsum; 3TDH; -.
DR PDBsum; 3TE5; -.
DR AlphaFoldDB; P12904; -.
DR SMR; P12904; -.
DR BioGRID; 33136; 675.
DR ComplexPortal; CPX-231; Snf1 protein kinase complex variant GAL83.
DR ComplexPortal; CPX-232; Snf1 protein kinase complex variant SIP1.
DR ComplexPortal; CPX-2800; Snf1 protein kinase complex variant SIP2.
DR DIP; DIP-592N; -.
DR IntAct; P12904; 43.
DR MINT; P12904; -.
DR STRING; 4932.YGL115W; -.
DR iPTMnet; P12904; -.
DR MaxQB; P12904; -.
DR PaxDb; P12904; -.
DR PRIDE; P12904; -.
DR EnsemblFungi; YGL115W_mRNA; YGL115W; YGL115W.
DR GeneID; 852763; -.
DR KEGG; sce:YGL115W; -.
DR SGD; S000003083; SNF4.
DR VEuPathDB; FungiDB:YGL115W; -.
DR eggNOG; KOG1764; Eukaryota.
DR GeneTree; ENSGT00950000183019; -.
DR HOGENOM; CLU_021740_1_0_1; -.
DR OMA; ACVKMLE; -.
DR BioCyc; YEAST:G3O-30613-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR EvolutionaryTrace; P12904; -.
DR PRO; PR:P12904; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P12904; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:ComplexPortal.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD.
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:1904547; P:regulation of cellular response to glucose starvation; EXP:ComplexPortal.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:SGD.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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 3D-structure; ATP-binding; Carbohydrate metabolism; CBS domain; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..322
FT /note="5'-AMP-activated protein kinase subunit gamma"
FT /id="PRO_0000204389"
FT DOMAIN 37..97
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 118..181
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 194..253
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 262..322
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 42
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 146
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 166..169
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 195
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 195
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3TDH"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3T4N"
FT BINDING 200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3TDH"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3T4N"
FT BINDING 221..222
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 221..222
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3TDH"
FT BINDING 221..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3T4N"
FT BINDING 291..293
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 309..312
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 309..312
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3TDH"
FT BINDING 309..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22019086,
FT ECO:0007744|PDB:3T4N"
FT MUTAGEN 63
FT /note="V->Q: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 136
FT /note="C->Y: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 145
FT /note="G->E: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 146
FT /note="R->A,Q: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 166
FT /note="T->N: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 177
FT /note="N->A,Y: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 242
FT /note="L->E: Decreases SNF1-activation efficiency; when
FT associated with A-291 and E-293."
FT /evidence="ECO:0000269|PubMed:17223533"
FT MUTAGEN 251
FT /note="N->I: Leads to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:18474591"
FT MUTAGEN 291
FT /note="R->A: Decreases SNF1-activation efficiency; when
FT associated with E-242 and E-293."
FT /evidence="ECO:0000269|PubMed:17223533"
FT MUTAGEN 293
FT /note="H->A: Reduces glucose inhibition of SNF1 and leads
FT to resistance to 2-deoxyglucose."
FT /evidence="ECO:0000269|PubMed:17223533,
FT ECO:0000269|PubMed:18474591"
FT MUTAGEN 293
FT /note="H->E: Decreases SNF1-activation efficiency; when
FT associated with E-242 and A-291."
FT /evidence="ECO:0000269|PubMed:17223533,
FT ECO:0000269|PubMed:18474591"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3T4N"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3T4N"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2QLV"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2NYC"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2NYC"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:2NYC"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2NYC"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:2NYC"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:2NYC"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:2NYC"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:2NYC"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:2NYC"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2NYC"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:2NYC"
SQ SEQUENCE 322 AA; 36401 MW; 51B387E346EE9561 CRC64;
MKPTQDSQEK VSIEQQLAVE SIRKFLNSKT SYDVLPVSYR LIVLDTSLLV KKSLNVLLQN
SIVSAPLWDS KTSRFAGLLT TTDFINVIQY YFSNPDKFEL VDKLQLDGLK DIERALGVDQ
LDTASIHPSR PLFEACLKML ESRSGRIPLI DQDEETHREI VVSVLTQYRI LKFVALNCRE
THFLKIPIGD LNIITQDNMK SCQMTTPVID VIQMLTQGRV SSVPIIDENG YLINVYEAYD
VLGLIKGGIY NDLSLSVGEA LMRRSDDFEG VYTCTKNDKL STIMDNIRKA RVHRFFVVDD
VGRLVGVLTL SDILKYILLG SN
