USV1_YEAST
ID USV1_YEAST Reviewed; 391 AA.
AC Q12132; D6W3E0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Nutrient and stress factor 1;
DE AltName: Full=Up in starvation protein 1;
GN Name=USV1; Synonyms=NSF1; OrderedLocusNames=YPL230W; ORFNames=P1421;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP DOMAIN.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [4]
RP FUNCTION.
RX PubMed=12740579; DOI=10.1038/ng1165;
RA Segal E., Shapira M., Regev A., Pe'er D., Botstein D., Koller D.,
RA Friedman N.;
RT "Module networks: identifying regulatory modules and their condition-
RT specific regulators from gene expression data.";
RL Nat. Genet. 34:166-176(2003).
RN [5]
RP INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18667581; DOI=10.1099/mic.0.2008/019976-0;
RA Hlynialuk C., Schierholtz R., Vernooy A., van der Merwe G.;
RT "Nsf1/Ypl230w participates in transcriptional activation during non-
RT fermentative growth and in response to salt stress in Saccharomyces
RT cerevisiae.";
RL Microbiology 154:2482-2491(2008).
RN [6]
RP FUNCTION.
RX PubMed=19197357; DOI=10.1371/journal.pgen.1000364;
RA Gaillard H., Tous C., Botet J., Gonzalez-Aguilera C., Quintero M.J.,
RA Viladevall L., Garcia-Rubio M.L., Rodriguez-Gil A., Marin A., Arino J.,
RA Revuelta J.L., Chavez S., Aguilera A.;
RT "Genome-wide analysis of factors affecting transcription elongation and DNA
RT repair: a new role for PAF and Ccr4-not in transcription-coupled repair.";
RL PLoS Genet. 5:E1000364-E1000364(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-163, 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: Transcription factor that participates in the transcriptional
CC activation of glucose-repressed genes during exponential growth in non-
CC fermentable carbon conditions. Also involved in salt-stress response.
CC {ECO:0000269|PubMed:12740579, ECO:0000269|PubMed:18667581,
CC ECO:0000269|PubMed:19197357}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18667581}. Note=Found
CC in the nucleus in conditions under which NSF1 is actively transcribed,
CC such as growth with non-fermentable carbon sources or salt stress.
CC -!- INDUCTION: Repressed by glucose but is activated in the presence of
CC non-fermentable carbon sources or salt stress. The latter
CC transcriptional activation of NSF1 is partially dependent on the SNF1
CC signaling pathway. {ECO:0000269|PubMed:18667581}.
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DR EMBL; Z73586; CAA97946.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64257.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11206.1; -; Genomic_DNA.
DR PIR; S61704; S61704.
DR RefSeq; NP_015094.1; NM_001184044.1.
DR AlphaFoldDB; Q12132; -.
DR SMR; Q12132; -.
DR BioGRID; 35955; 101.
DR STRING; 4932.YPL230W; -.
DR iPTMnet; Q12132; -.
DR MaxQB; Q12132; -.
DR PaxDb; Q12132; -.
DR PRIDE; Q12132; -.
DR EnsemblFungi; YPL230W_mRNA; YPL230W; YPL230W.
DR GeneID; 855871; -.
DR KEGG; sce:YPL230W; -.
DR SGD; S000006151; USV1.
DR VEuPathDB; FungiDB:YPL230W; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176682; -.
DR HOGENOM; CLU_704392_0_0_1; -.
DR InParanoid; Q12132; -.
DR OMA; ENEKAPQ; -.
DR BioCyc; YEAST:G3O-34118-MON; -.
DR PRO; PR:Q12132; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12132; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..391
FT /note="Nutrient and stress factor 1"
FT /id="PRO_0000255973"
FT ZN_FING 41..66
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 72..95
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 391 AA; 43518 MW; 56C9DFEC6CD2BF9D CRC64;
MENTTNRNTA GVLTSSNGNF ATNSVAASTP KRSKSARRKT FKCTGYDGCT MSFTRAEHLA
RHIRKHTGEK PFQCPACLKF FSRVDNLKQH RESVHAHKNH HSTSSHQRKP SSSSLSSSSS
ASSSSSASSS TSYSDPYRKT NINSGNMPMM AENEKAPQII HSSPEFITST RSIPPISPRS
IYNTQRQQQH QQQQHQQAPY YFPSHPITDS YYQYPLPSNN NTINYLPSVD VQYPLNVSPS
STSHPASEVI ISSFPPRSMP STSFKYKDSA DFQARTTMNK YNIRPSNINV NTSNINNHLD
SFSPPFSPST TVAEAKPIIL PQYQQAFSQP PNGNKNNNMS SSKNGGKGGE NFKNTDDRND
NNNKKRSETL SESDISVNTN KKRLSVDYIL T
