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5'-AMP-activated protein kinase subunit gamma (AMPK gamma) (AMPK subunit gamma) (Regulatory protein CAT3) (Sucrose non-fermenting protein 4)

 AAKG_YEAST              Reviewed;         322 AA.
P12904; D6VU32;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=5'-AMP-activated protein kinase subunit gamma;
Short=AMPK gamma;
Short=AMPK subunit gamma;
AltName: Full=Regulatory protein CAT3;
AltName: Full=Sucrose non-fermenting protein 4;
Name=SNF4; Synonyms=CAT3, SCI1; OrderedLocusNames=YGL115W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=3049255; DOI=10.1016/0378-1119(88)90401-5;
Schueller H.-J., Entian K.-D.;
"Molecular characterization of yeast regulatory gene CAT3 necessary
for glucose derepression and nuclear localization of its product.";
Gene 67:247-257(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
INTERACTION WITH SNF1.
PubMed=2481228; DOI=10.1128/MCB.9.11.5045;
Celenza J.L., Eng F.J., Carlson M.;
"Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae:
evidence for physical association of the SNF4 protein with the SNF1
protein kinase.";
Mol. Cell. Biol. 9:5045-5054(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Doi A., Doi K.;
"Correct end of the ORF for the CDC20 gene of Saccharomyces
cerevisiae.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 30-34 AND 316-322.
PubMed=7905477;
Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B.,
Katsis F., Witters L.A., Kemp B.E.;
"Mammalian AMP-activated protein kinase shares structural and
functional homology with the catalytic domain of yeast Snf1 protein
kinase.";
J. Biol. Chem. 269:2361-2364(1994).
[7]
FUNCTION.
PubMed=7050076;
Entian K.D., Zimmermann F.K.;
"New genes involved in carbon catabolite repression and derepression
in the yeast Saccharomyces cerevisiae.";
J. Bacteriol. 151:1123-1128(1982).
[8]
FUNCTION.
PubMed=6392017;
Neigeborn L., Carlson M.;
"Genes affecting the regulation of SUC2 gene expression by glucose
repression in Saccharomyces cerevisiae.";
Genetics 108:845-858(1984).
[9]
FUNCTION.
PubMed=3939253; DOI=10.1128/MCB.5.10.2521;
Sarokin L., Carlson M.;
"Upstream region of the SUC2 gene confers regulated expression to a
heterologous gene in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 5:2521-2526(1985).
[10]
FUNCTION.
PubMed=3049551; DOI=10.1128/jb.170.10.4838-4845.1988;
Bisson L.F.;
"High-affinity glucose transport in Saccharomyces cerevisiae is under
general glucose repression control.";
J. Bacteriol. 170:4838-4845(1988).
[11]
FUNCTION.
PubMed=2557546; DOI=10.1128/MCB.9.11.5034;
Celenza J.L., Carlson M.;
"Mutational analysis of the Saccharomyces cerevisiae SNF1 protein
kinase and evidence for functional interaction with the SNF4
protein.";
Mol. Cell. Biol. 9:5034-5044(1989).
[12]
FUNCTION.
PubMed=2169717; DOI=10.1007/BF00423333;
Arguelles J.C., Mbonyi K., Van Aelst L., Vanhalewyn M., Jans A.W.,
Thevelein J.M.;
"Absence of glucose-induced cAMP signaling in the Saccharomyces
cerevisiae mutants cat1 and cat3 which are deficient in derepression
of glucose-repressible proteins.";
Arch. Microbiol. 154:199-205(1990).
[13]
FUNCTION, AND INTERACTION WITH SNF1.
PubMed=1468623;
Estruch F., Treitel M.A., Yang X., Carlson M.;
"N-terminal mutations modulate yeast SNF1 protein kinase function.";
Genetics 132:639-650(1992).
[14]
FUNCTION OF THE AMPK COMPLEX.
PubMed=8224185; DOI=10.1016/0014-5793(93)80661-D;
Fernandez E., Fernandez M., Moreno F., Rodicio R.;
"Transcriptional regulation of the isocitrate lyase encoding gene in
Saccharomyces cerevisiae.";
FEBS Lett. 333:238-242(1993).
[15]
FUNCTION.
PubMed=8544831; DOI=10.1007/BF00418035;
Blazquez M.A., Gancedo C.;
"Mode of action of the qcr9 and cat3 mutations in restoring the
ability of Saccharomyces cerevisiae tps1 mutants to grow on glucose.";
Mol. Gen. Genet. 249:655-664(1995).
[16]
FUNCTION, AND INTERACTION WITH SNF1.
PubMed=8985180; DOI=10.1101/gad.10.24.3105;
Jiang R., Carlson M.;
"Glucose regulates protein interactions within the yeast SNF1 protein
kinase complex.";
Genes Dev. 10:3105-3115(1996).
[17]
INTERACTION WITH SNF1; SIP1; SIP2 AND GAL83.
PubMed=9121458; DOI=10.1128/MCB.17.4.2099;
Jiang R., Carlson M.;
"The Snf1 protein kinase and its activating subunit, Snf4, interact
with distinct domains of the Sip1/Sip2/Gal83 component in the kinase
complex.";
Mol. Cell. Biol. 17:2099-2106(1997).
[18]
FUNCTION.
PubMed=10099331;
DOI=10.1002/(SICI)1097-0290(19980720)59:2<203::AID-BIT8>3.0.CO;2-L;
Aon M.A., Cortassa S.;
"Catabolite repression mutants of Saccharomyces cerevisiae show
altered fermentative metabolism as well as cell cycle behavior in
glucose-limited chemostat cultures.";
Biotechnol. Bioeng. 59:203-213(1998).
[19]
FUNCTION, AND INTERACTION WITH SNF1.
PubMed=9600950; DOI=10.1073/pnas.95.11.6245;
Ludin K., Jiang R., Carlson M.;
"Glucose-regulated interaction of a regulatory subunit of protein
phosphatase 1 with the Snf1 protein kinase in Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 95:6245-6250(1998).
[20]
DISRUPTION PHENOTYPE.
PubMed=9841784; DOI=10.1007/PL00006773;
Aon M.A., Cortassa S.;
"Quantitation of the effects of disruption of catabolite
(de)repression genes on the cell cycle behavior of Saccharomyces
cerevisiae.";
Curr. Microbiol. 38:57-60(1999).
[21]
INTERACTION WITH SNIF1, AND FUNCTION OF THE AMPK COMPLEX.
PubMed=10224244;
Shirra M.K., Arndt K.M.;
"Evidence for the involvement of the Glc7-Reg1 phosphatase and the
Snf1-Snf4 kinase in the regulation of INO1 transcription in
Saccharomyces cerevisiae.";
Genetics 152:73-87(1999).
[22]
FUNCTION.
PubMed=11486005; DOI=10.1074/jbc.M104418200;
McCartney R.R., Schmidt M.C.;
"Regulation of Snf1 kinase. Activation requires phosphorylation of
threonine 210 by an upstream kinase as well as a distinct step
mediated by the Snf4 subunit.";
J. Biol. Chem. 276:36460-36466(2001).
[23]
IDENTIFICATION IN THE AMPK COMPLEX, AND FUNCTION OF THE AMPK COMPLEX.
PubMed=12393914; DOI=10.1074/jbc.M207058200;
Nath N., McCartney R.R., Schmidt M.C.;
"Purification and characterization of Snf1 kinase complexes containing
a defined beta subunit composition.";
J. Biol. Chem. 277:50403-50408(2002).
[24]
FUNCTION OF THE AMPK COMPLEX.
PubMed=12960168; DOI=10.1074/jbc.M307447200;
Haurie V., Boucherie H., Sagliocco F.;
"The Snf1 protein kinase controls the induction of genes of the iron
uptake pathway at the diauxic shift in Saccharomyces cerevisiae.";
J. Biol. Chem. 278:45391-45396(2003).
[25]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[26]
IDENTIFICATION IN THE AMPK COMPLEX.
PubMed=16847059; DOI=10.1074/jbc.M603811200;
Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.;
"Subunits of the Snf1 kinase heterotrimer show interdependence for
association and activity.";
J. Biol. Chem. 281:26170-26180(2006).
[27]
SUBCELLULAR LOCATION.
PubMed=17237508; DOI=10.1534/genetics.106.068932;
Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A.,
Santangelo G.M.;
"Glucose-responsive regulators of gene expression in Saccharomyces
cerevisiae function at the nuclear periphery via a reverse recruitment
mechanism.";
Genetics 175:1127-1135(2007).
[28]
FUNCTION, AND MUTAGENESIS OF VAL-63; CYS-136; GLY-145; ARG-146;
THR-166; ASN-177; ASN-251 AND HIS-293.
PubMed=18474591; DOI=10.1074/jbc.M803624200;
Momcilovic M., Iram S.H., Liu Y., Carlson M.;
"Roles of the glycogen-binding domain and Snf4 in glucose inhibition
of SNF1 protein kinase.";
J. Biol. Chem. 283:19521-19529(2008).
[29]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 179-322, AND MUTAGENESIS OF
LEU-242; ARG-291 AND HIS-293.
PubMed=17223533; DOI=10.1016/j.str.2006.11.014;
Rudolph M.J., Amodeo G.A., Iram S.H., Hong S.P., Pirino G.,
Carlson M., Tong L.;
"Structure of the Bateman2 domain of yeast Snf4: dimeric association
and relevance for AMP binding.";
Structure 15:65-74(2007).
[30]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 7-321 IN COMPLEX WITH SNF1
AND SIP2.
PubMed=17851534; DOI=10.1038/nature06127;
Amodeo G.A., Rudolph M.J., Tong L.;
"Crystal structure of the heterotrimer core of Saccharomyces
cerevisiae AMPK homologue SNF1.";
Nature 449:492-495(2007).
[31]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-322, ADP-BINDING, AND
FUNCTION.
PubMed=22019086; DOI=10.1016/j.cmet.2011.09.009;
Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D.,
McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A.,
Haire L.F., Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J.,
Carling D.;
"ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-
activated protein kinase.";
Cell Metab. 14:707-714(2011).
-!- FUNCTION: Adenine nucleotides-binding subunit gamma of AMP-
activated protein kinase (AMPK), an energy sensor protein kinase
that plays a key role in regulating cellular energy metabolism. In
response to reduction of intracellular ATP levels, AMPK activates
energy-producing pathways and inhibits energy-consuming processes:
inhibits protein, carbohydrate and lipid biosynthesis, as well as
cell growth and proliferation. AMPK acts via direct
phosphorylation of metabolic enzymes, and by longer-term effects
via phosphorylation of transcription regulators. Gamma non-
catalytic subunit mediates binding to AMP, ADP and ATP, leading to
activate or inhibit AMPK: AMP-binding results in allosteric
activation of alpha catalytic subunit (SNF1) both by inducing
phosphorylation and preventing dephosphorylation of catalytic
subunits. {ECO:0000269|PubMed:10099331,
ECO:0000269|PubMed:10224244, ECO:0000269|PubMed:11486005,
ECO:0000269|PubMed:12393914, ECO:0000269|PubMed:12960168,
ECO:0000269|PubMed:1468623, ECO:0000269|PubMed:18474591,
ECO:0000269|PubMed:2169717, ECO:0000269|PubMed:22019086,
ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3049551,
ECO:0000269|PubMed:3939253, ECO:0000269|PubMed:6392017,
ECO:0000269|PubMed:7050076, ECO:0000269|PubMed:8224185,
ECO:0000269|PubMed:8544831, ECO:0000269|PubMed:8985180,
ECO:0000269|PubMed:9600950}.
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic
subunits (SNF4). Note=Interaction between SNF1 and SNF4 is
inhibited by high levels of glucose. {ECO:0000269|PubMed:12393914,
ECO:0000269|PubMed:16847059, ECO:0000269|PubMed:17851534}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-17537, EBI-17537;
P32578:SIP1; NbExp=4; IntAct=EBI-17537, EBI-17179;
P34164:SIP2; NbExp=9; IntAct=EBI-17537, EBI-17187;
P06782:SNF1; NbExp=20; IntAct=EBI-17537, EBI-17516;
P25575:YCL046W; NbExp=3; IntAct=EBI-17537, EBI-21748;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17237508,
ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:3049255}. Cytoplasm
{ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228}.
-!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
potential nucleotide-binding sites, 2 are occupied, designated as
sites 2 and 3 based on the CBS modules that provide the acidic
residue for coordination with the 2'- and 3'-hydroxyl groups of
the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP,
ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely
to be responsible for protection of a conserved threonine in the
activation loop of the alpha catalytic subunit through
conformational changes induced by binding of ADP
(PubMed:22019086). {ECO:0000269|PubMed:22019086}.
-!- DISRUPTION PHENOTYPE: Leads to a decrease in the length of G1 with
respect to the wild-type strain along with a smaller difference in
the cell cycle length of parent and daughter cells.
{ECO:0000269|PubMed:9841784}.
-!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
subunit family. {ECO:0000305}.
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EMBL; M21760; AAA34472.1; -; Genomic_DNA.
EMBL; M30470; AAA35061.1; -; Genomic_DNA.
EMBL; Z72637; CAA96823.1; -; Genomic_DNA.
EMBL; D16506; BAA03958.1; -; Genomic_DNA.
EMBL; BK006941; DAA07993.1; -; Genomic_DNA.
PIR; A38906; RGBYC3.
RefSeq; NP_011400.1; NM_001180980.1.
PDB; 2NYC; X-ray; 1.90 A; A=179-322.
PDB; 2NYE; X-ray; 2.50 A; A/B=179-322.
PDB; 2QLV; X-ray; 2.60 A; C/F=7-321.
PDB; 3T4N; X-ray; 2.30 A; C=2-322.
PDB; 3TDH; X-ray; 2.30 A; C=2-322.
PDB; 3TE5; X-ray; 2.50 A; C=2-322.
PDBsum; 2NYC; -.
PDBsum; 2NYE; -.
PDBsum; 2QLV; -.
PDBsum; 3T4N; -.
PDBsum; 3TDH; -.
PDBsum; 3TE5; -.
ProteinModelPortal; P12904; -.
SMR; P12904; -.
BioGrid; 33136; 637.
DIP; DIP-592N; -.
IntAct; P12904; 43.
MINT; MINT-364345; -.
STRING; 4932.YGL115W; -.
iPTMnet; P12904; -.
MaxQB; P12904; -.
PRIDE; P12904; -.
EnsemblFungi; YGL115W; YGL115W; YGL115W.
GeneID; 852763; -.
KEGG; sce:YGL115W; -.
EuPathDB; FungiDB:YGL115W; -.
SGD; S000003083; SNF4.
GeneTree; ENSGT00390000009849; -.
HOGENOM; HOG000176880; -.
KO; K07200; -.
OMA; FPGVVIC; -.
OrthoDB; EOG092C39BT; -.
BioCyc; YEAST:G3O-30613-MONOMER; -.
Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
EvolutionaryTrace; P12904; -.
PRO; PR:P12904; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:SGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0007031; P:peroxisome organization; IMP:SGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IGI:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000644; CBS_dom.
Pfam; PF00571; CBS; 3.
SMART; SM00116; CBS; 4.
PROSITE; PS51371; CBS; 4.
1: Evidence at protein level;
3D-structure; ATP-binding; Carbohydrate metabolism; CBS domain;
Complete proteome; Cytoplasm; Direct protein sequencing;
Nucleotide-binding; Nucleus; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 322 5'-AMP-activated protein kinase subunit
gamma.
/FTId=PRO_0000204389.
DOMAIN 37 97 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 118 181 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 194 253 CBS 3. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 262 322 CBS 4. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 166 169 ADP 1. {ECO:0000250|UniProtKB:Q10343}.
NP_BIND 221 222 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:22019086}.
NP_BIND 291 293 ADP 1. {ECO:0000250|UniProtKB:Q10343}.
NP_BIND 309 312 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:22019086}.
BINDING 146 146 ADP 1. {ECO:0000250|UniProtKB:Q10343}.
BINDING 195 195 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:22019086}.
BINDING 200 200 AMP, ADP or ATP 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:22019086}.
MUTAGEN 63 63 V->Q: Reduces glucose inhibition of SNF1
and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 136 136 C->Y: Reduces glucose inhibition of SNF1
and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 145 145 G->E: Reduces glucose inhibition of SNF1
and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 146 146 R->A,Q: Reduces glucose inhibition of
SNF1 and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 166 166 T->N: Reduces glucose inhibition of SNF1
and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 177 177 N->A,Y: Reduces glucose inhibition of
SNF1 and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 242 242 L->E: Decreases SNF1-activation
efficiency; when associated with A-291
and E-293. {ECO:0000269|PubMed:17223533}.
MUTAGEN 251 251 N->I: Leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:18474591}.
MUTAGEN 291 291 R->A: Decreases SNF1-activation
efficiency; when associated with E-242
and E-293. {ECO:0000269|PubMed:17223533}.
MUTAGEN 293 293 H->A: Reduces glucose inhibition of SNF1
and leads to resistance to 2-
deoxyglucose.
{ECO:0000269|PubMed:17223533,
ECO:0000269|PubMed:18474591}.
MUTAGEN 293 293 H->E: Decreases SNF1-activation
efficiency; when associated with E-242
and A-291. {ECO:0000269|PubMed:17223533,
ECO:0000269|PubMed:18474591}.
HELIX 8 28 {ECO:0000244|PDB:3T4N}.
HELIX 31 34 {ECO:0000244|PDB:3T4N}.
STRAND 37 45 {ECO:0000244|PDB:3T4N}.
HELIX 50 59 {ECO:0000244|PDB:3T4N}.
STRAND 65 69 {ECO:0000244|PDB:3T4N}.
TURN 70 73 {ECO:0000244|PDB:3T4N}.
STRAND 74 79 {ECO:0000244|PDB:3T4N}.
HELIX 81 93 {ECO:0000244|PDB:3T4N}.
HELIX 95 103 {ECO:0000244|PDB:3T4N}.
HELIX 106 115 {ECO:0000244|PDB:3T4N}.
HELIX 132 142 {ECO:0000244|PDB:3T4N}.
STRAND 145 152 {ECO:0000244|PDB:3T4N}.
TURN 154 156 {ECO:0000244|PDB:3T4N}.
STRAND 159 166 {ECO:0000244|PDB:3T4N}.
HELIX 167 177 {ECO:0000244|PDB:3T4N}.
HELIX 179 181 {ECO:0000244|PDB:2QLV}.
HELIX 182 185 {ECO:0000244|PDB:2NYC}.
HELIX 188 190 {ECO:0000244|PDB:2NYC}.
HELIX 208 218 {ECO:0000244|PDB:2NYC}.
STRAND 221 226 {ECO:0000244|PDB:2NYC}.
STRAND 231 237 {ECO:0000244|PDB:2NYC}.
HELIX 238 246 {ECO:0000244|PDB:2NYC}.
HELIX 249 252 {ECO:0000244|PDB:3T4N}.
HELIX 257 263 {ECO:0000244|PDB:2NYC}.
STRAND 272 274 {ECO:0000244|PDB:3T4N}.
HELIX 280 290 {ECO:0000244|PDB:2NYC}.
STRAND 293 298 {ECO:0000244|PDB:2NYC}.
STRAND 302 309 {ECO:0000244|PDB:2NYC}.
HELIX 310 319 {ECO:0000244|PDB:2NYC}.
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


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