GAL83_YEAST
ID GAL83_YEAST Reviewed; 417 AA.
AC Q04739; D3DLS6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=SNF1 protein kinase subunit beta-3;
DE AltName: Full=Glucose repression protein GAL83;
DE AltName: Full=Protein SPM1;
GN Name=GAL83; Synonyms=SPM1; OrderedLocusNames=YER027C;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8293971; DOI=10.1093/genetics/135.3.655;
RA Erickson J.R., Johnston M.;
RT "Genetic and molecular characterization of GAL83: its interaction and
RT similarities with other genes involved in glucose repression in
RT Saccharomyces cerevisiae.";
RL Genetics 135:655-664(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Drebot M.A., Jansma D., Himmelfarb H.J., Friesen J.D.;
RT "Dominant, pleiotropic gain-of-function suppressors of temperature-
RT sensitive alleles of the Saccharomyces cerevisiae RPO21 gene.";
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP INTERACTION WITH SNF1, AND PHOSPHORYLATION.
RX PubMed=7813428; DOI=10.1002/j.1460-2075.1994.tb06933.x;
RA Yang X., Jiang R., Carlson M.;
RT "A family of proteins containing a conserved domain that mediates
RT interaction with the yeast SNF1 protein kinase complex.";
RL EMBO J. 13:5878-5886(1994).
RN [7]
RP INTERACTION WITH SNF1 AND SNF4.
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 [8]
RP FUNCTION.
RX PubMed=10990457; DOI=10.1093/emboj/19.18.4936;
RA Schmidt M.C., McCartney R.R.;
RT "beta-subunits of Snf1 kinase are required for kinase function and
RT substrate definition.";
RL EMBO J. 19:4936-4943(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11331606; DOI=10.1101/gad.879301;
RA Vincent O., Townley R., Kuchin S., Carlson M.;
RT "Subcellular localization of the Snf1 kinase is regulated by specific beta
RT subunits and a novel glucose signaling mechanism.";
RL Genes Dev. 15:1104-1114(2001).
RN [10]
RP IDENTIFICATION IN SNF1 KINASE 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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP INTERACTION WITH REE1.
RX PubMed=18851946; DOI=10.1016/j.bbrc.2008.09.146;
RA Choi I.D., Jeong M.Y., Ham M.S., Sung H.C., Yun C.W.;
RT "Novel Ree1 regulates the expression of ENO1 via the Snf1 complex pathway
RT in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 377:395-399(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-44, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-21 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Beta subunit of the SNF1 kinase complex, which is required
CC for transcriptional, metabolic, and developmental adaptations in
CC response to glucose limitation. Has a structural role, mediating
CC heterotrimer formation, and a regulatory role, defining carbon source-
CC regulated subcellular location and substrate specificity of the SNF1
CC kinase complex. Promotes the relocalization of the SNF1 kinase complex
CC to the nucleus upon shift to nonfermentable carbon sources.
CC {ECO:0000269|PubMed:10990457}.
CC -!- SUBUNIT: Component of the SNF1 kinase complex, a heterotrimeric complex
CC composed of the catalytic alpha subunit SNF1, one of the three related
CC beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit
CC SNF4. The beta subunit serves as a bridge between the catalytic and the
CC regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts
CC (via ASC domain) with SNF4. Interacts with REE1.
CC {ECO:0000269|PubMed:12393914, ECO:0000269|PubMed:18851946,
CC ECO:0000269|PubMed:7813428, ECO:0000269|PubMed:9121458}.
CC -!- INTERACTION:
CC Q04739; P06782: SNF1; NbExp=5; IntAct=EBI-7244, EBI-17516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331606}. Nucleus
CC {ECO:0000269|PubMed:11331606}. Note=Resides in the cytosol during
CC growth on fermentable carbon sources and relocalizes rapidly to the
CC nucleus in response to carbon stress. {ECO:0000269|PubMed:11331606}.
CC -!- PTM: Phosphorylated by SNF1 in vitro. {ECO:0000269|PubMed:7813428}.
CC -!- MISCELLANEOUS: Present with 3590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; X72893; CAA51411.1; -; Genomic_DNA.
DR EMBL; L13599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z14127; CAA78501.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64560.1; -; Genomic_DNA.
DR EMBL; AY692771; AAT92790.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07680.1; -; Genomic_DNA.
DR PIR; S52591; S52591.
DR RefSeq; NP_010944.1; NM_001178918.1.
DR AlphaFoldDB; Q04739; -.
DR SMR; Q04739; -.
DR BioGRID; 36762; 81.
DR ComplexPortal; CPX-231; Snf1 protein kinase complex variant GAL83.
DR DIP; DIP-1298N; -.
DR IntAct; Q04739; 9.
DR MINT; Q04739; -.
DR STRING; 4932.YER027C; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q04739; -.
DR MaxQB; Q04739; -.
DR PaxDb; Q04739; -.
DR PRIDE; Q04739; -.
DR EnsemblFungi; YER027C_mRNA; YER027C; YER027C.
DR GeneID; 856749; -.
DR KEGG; sce:YER027C; -.
DR SGD; S000000829; GAL83.
DR VEuPathDB; FungiDB:YER027C; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000176367; -.
DR HOGENOM; CLU_033562_1_0_1; -.
DR InParanoid; Q04739; -.
DR OMA; DDMGDGY; -.
DR BioCyc; YEAST:G3O-30208-MON; -.
DR BRENDA; 2.7.11.31; 984.
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 PRO; PR:Q04739; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; Q04739; protein.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IMP:SGD.
DR GO; GO:0030447; P:filamentous growth; IMP:ComplexPortal.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:ComplexPortal.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:InterPro.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IGI:SGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR030077; SIP2/GAL83.
DR PANTHER; PTHR10343:SF84; PTHR10343:SF84; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..417
FT /note="SNF1 protein kinase subunit beta-3"
FT /id="PRO_0000204373"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..342
FT /note="Kinase-interacting sequence (KIS); required for
FT interaction with SNF1"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..417
FT /note="Association with SNF1 kinase complex (ASC) domain;
FT required for interaction with SNF4"
FT /evidence="ECO:0000269|PubMed:9121458"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 417 AA; 46648 MW; E7BDAC821C1E049A CRC64;
MAGDNPENKD ASMLDVSDAA SNTTINGKHS ADSTNEASLA YTFSQMNVDN PNELEPQHPL
RHKSSLIFND DDDDEIPPYS NHAENGSGET FDSDDDIDAS SSSSIDSNEG DIHDADMTGN
TLQKMDYQPS QQPDSLQNQG FQQQQEQQQG TVEGKKGRAM MFPVDITWQQ GGNKVYVTGS
FTGWRKMIGL VPVPGQPGLM HVKLQLPPGT HRFRFIVDNE LRFSDYLPTA TDQMGNFVNY
MEVSAPPDWG NEPQQHLAEK KANHVDDSKL SKRPMSARSR IALEIEKEPD DMGDGYTRFH
DETPAKPNLE YTQDIPAVFT DPNVMEQYYL TLDQQQNNHQ NMAWLTPPQL PPHLENVILN
SYSNAQTDNT SGALPIPNHV ILNHLATSSI KHNTLCVASI VRYKQKYVTQ ILYTPLQ
