GSM1_YEAST
ID GSM1_YEAST Reviewed; 618 AA.
AC P42950; D6VW81; Q66R68;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glucose starvation modulator protein 1;
GN Name=GSM1; OrderedLocusNames=YJL103C; ORFNames=J0824;
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 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
RP PREDICTION OF FUNCTION.
RX PubMed=15583838;
RA Deng Y., He T., Wu Y., Vanka P., Yang G., Huang Y., Yao H., Brown S.J.;
RT "Computationally analyzing the possible biological function of YJL103C--an
RT ORF potentially involved in the regulation of energy process in yeast.";
RL Int. J. Mol. Med. 15:123-127(2005).
RN [6]
RP DNA-BINDING.
RX PubMed=16785442; DOI=10.1073/pnas.0509185103;
RA Ho S.-W., Jona G., Chen C.T.L., Johnston M., Snyder M.;
RT "Linking DNA-binding proteins to their recognition sequences by using
RT protein microarrays.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9940-9945(2006).
RN [7]
RP DNA-BINDING.
RX PubMed=18180247; DOI=10.1093/nar/gkm1144;
RA van Bakel H., van Werven F.J., Radonjic M., Brok M.O., van Leenen D.,
RA Holstege F.C.P., Timmers H.T.M.;
RT "Improved genome-wide localization by ChIP-chip using double-round T7 RNA
RT polymerase-based amplification.";
RL Nucleic Acids Res. 36:E21-E21(2008).
CC -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC utilization (By similarity). Binds specifically to 5'-CGGN(8)CGG-3' and
CC 5'-CGGN(9)CGG-3' sequences in the promoter region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
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DR EMBL; X85021; CAA59391.1; -; Genomic_DNA.
DR EMBL; Z49378; CAA89398.1; -; Genomic_DNA.
DR EMBL; AY723834; AAU09751.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08697.1; -; Genomic_DNA.
DR PIR; S53384; S53384.
DR RefSeq; NP_012432.1; NM_001181536.1.
DR AlphaFoldDB; P42950; -.
DR BioGRID; 33653; 44.
DR IntAct; P42950; 2.
DR STRING; 4932.YJL103C; -.
DR iPTMnet; P42950; -.
DR PaxDb; P42950; -.
DR PRIDE; P42950; -.
DR EnsemblFungi; YJL103C_mRNA; YJL103C; YJL103C.
DR GeneID; 853341; -.
DR KEGG; sce:YJL103C; -.
DR SGD; S000003639; GSM1.
DR VEuPathDB; FungiDB:YJL103C; -.
DR eggNOG; ENOG502R2ZP; Eukaryota.
DR GeneTree; ENSGT00940000176385; -.
DR HOGENOM; CLU_010748_2_2_1; -.
DR InParanoid; P42950; -.
DR OMA; CHEKHLQ; -.
DR BioCyc; YEAST:G3O-31557-MON; -.
DR PRO; PR:P42950; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P42950; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..618
FT /note="Glucose starvation modulator protein 1"
FT /id="PRO_0000114998"
FT DOMAIN 466..538
FT /note="PAS"
FT DNA_BIND 20..48
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 325..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 611
FT /note="F -> L (in Ref. 4; AAU09751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 70382 MW; 200F6AEE06582E38 CRC64;
MTKKLPSELK QTRKSIQTAC EFCHTKHIQC DVGRPCQNCL KRNIGKFCRD KKRKSRKRIE
KHGTQPYLNL GKRLVIHDVP SKTVSPSSVH LQRDFLSSDQ EKPGKTPAHN TNIQYTYNIN
DNFQSAGSIP RITNFNTNNR QTVLENTSNN ISASQAVHLM NDPIIPTVRK STLNLKSHFL
EQHKAMQQPL ATNCLVATSN VPVHSGMDDS NKSDDDVDDE TNIHFDSMWC NDEYMKLKDI
VDISTPFLPN NSQIFSLQES EYPNPSASTR GNSSLHLTNL LNSTKSVNDQ KDSSIGHSTS
TFNTYDEVVS RPFISLDMLH LNRGANANTH PSHNAKLESE CDSSSHSDAD LEKHDTDFIS
PSKFRELVKT PQDLYDNKCL IKPHNYKLAY TKLLTTLRKK FLEGAEIDKS ASVKDEHSTQ
KHNLRYDLEV IIRSILERYA PIFISLTSNM IEEDLLLQEV TLQRALLDLE NMAKLVSCTP
MCIWRRSGEI CFVSNEFYSL TGFNKNLLLD RTSFIFEYLD HKSVSNYFQI FNELLAFGYN
DINKRKKLLM LNACSSTSSK ITEGFSFTTD GKAIFTKCNL LLSNGLYLKC ACCWTVKRDS
FNIPILVMGQ FLPIFEMD
