SFL1_YEAST
ID SFL1_YEAST Reviewed; 766 AA.
AC P20134; D6W2J6; Q99194;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Flocculation suppression protein;
DE AltName: Full=Protein SFL1;
GN Name=SFL1; OrderedLocusNames=YOR140W; ORFNames=YOR3339W;
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].
RX PubMed=2697640; DOI=10.1016/0378-1119(89)90424-1;
RA Fujita A., Kikuchi Y., Kuhara S., Misumi Y., Matsumoto S., Kobayashi H.;
RT "Domains of the SFL1 protein of yeasts are homologous to Myc oncoproteins
RT or yeast heat-shock transcription factor.";
RL Gene 85:321-328(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 446-454 AND 461-462.
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 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-556 AND SER-733, 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: Involved in cell surface assembly and regulation of the gene
CC related to flocculation (asexual cell aggregation). Mutations in SFL1
CC causes constitutive cell aggregation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HSF family.
CC {ECO:0000305}.
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DR EMBL; X94335; CAA64057.1; -; Genomic_DNA.
DR EMBL; Z75047; CAA99338.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10912.2; -; Genomic_DNA.
DR PIR; S61694; S61694.
DR RefSeq; NP_014783.4; NM_001183559.4.
DR AlphaFoldDB; P20134; -.
DR SMR; P20134; -.
DR BioGRID; 34534; 354.
DR DIP; DIP-5501N; -.
DR IntAct; P20134; 2.
DR MINT; P20134; -.
DR STRING; 4932.YOR140W; -.
DR iPTMnet; P20134; -.
DR MaxQB; P20134; -.
DR PaxDb; P20134; -.
DR PRIDE; P20134; -.
DR EnsemblFungi; YOR140W_mRNA; YOR140W; YOR140W.
DR GeneID; 854307; -.
DR KEGG; sce:YOR140W; -.
DR SGD; S000005666; SFL1.
DR VEuPathDB; FungiDB:YOR140W; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_371782_0_0_1; -.
DR InParanoid; P20134; -.
DR OMA; DSNTHDD; -.
DR BioCyc; YEAST:G3O-33661-MON; -.
DR PRO; PR:P20134; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P20134; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IPI:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:2001159; P:regulation of protein localization by the Cvt pathway; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR027722; Sfl1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR PANTHER; PTHR10015:SF388; PTHR10015:SF388; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..766
FT /note="Flocculation suppression protein"
FT /id="PRO_0000124595"
FT DNA_BIND 64..186
FT /evidence="ECO:0000250"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 446..454
FT /note="FVQYQPQSQ -> LYNTNRSRN (in Ref. 2; CAA64057 and 3;
FT CAA99338)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..462
FT /note="KQ -> SE (in Ref. 2; CAA64057 and 3; CAA99338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 83345 MW; 85D2594DFF42F938 CRC64;
MSEEETVSAP APASTPAPAG TDVGSGGAAA GIANAGAEGG DGAEDVKKHG SKMLVGPRPP
QNAIFIHKLY QILEDESLHD LIWWTPSGLS FMIKPVERFS KALATYFKHT NITSFVRQLN
IYGFHKVSHD HSSNDANSGD DANTNDDSNT HDDNSGNKNS SGDENTGGGV QEKEKSNPTK
IWEFKHSSGI FKKGDIEGLK HIKRRASSRN NSSINSRKNS SNQNYDIDSG ARVRPSSIQD
PSTSSNSFGN FVPQIPGANN SIPEYFNNSH VTYENANHAP LESNNPEMQE QNRPPNFQDE
TLKHLKEINF DMVKIIESMQ HFISLQHSFC SQSFTFKNVS KKKSENIVKD HQKQLQAFES
DMLTFKQHVM SRAHRTIDSL CAVNAAATAA SVAPAPAPTS TSAYAPKSQY EMMVPPGNQY
VPQKSSSTTN IPSRFNTASV PPSQLFVQYQ PQSQQHVTYA KQPAHVPNFI NQPIPIQQLP
PQYADTFSTP QMMHNPFASK NNNKPGNTKR TNSVLMDPLT PAASVGVQGP LNYPIMNINP
SVRDYNKPVP QNMAPSPIYP INEPTTRLYS QPKMRSLGST SSLPNDRRNS PLKLTPRSSL
NEDSLYPKPR NSLKSSISGT SLSSSFTLVA NNPAPIRYSQ QGLLRSLNKA ANCAPDSVTP
LDSSVLTGPP PKNMDNLPAV SSNLINSPMN VEHSSSLSQA EPAPQIELPQ PSLPTTSTTK
NTGEADNSKR KGSGVYSLLN QEDSSTSSAD PKTEDKAAPA LKKVKM