SFP1_YEAST
ID SFP1_YEAST Reviewed; 683 AA.
AC P32432; D6VZ36;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Transcription factor SFP1;
DE AltName: Full=Split finger protein 1;
GN Name=SFP1; OrderedLocusNames=YLR403W; ORFNames=L8084.4;
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=1743508; DOI=10.1016/0378-1119(91)90302-r;
RA Blumberg H., Silver P.;
RT "A split zinc-finger protein is required for normal yeast growth.";
RL Gene 107:101-110(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9832520; DOI=10.1093/genetics/150.4.1419;
RA Xu Z., Norris D.;
RT "The SFP1 gene product of Saccharomyces cerevisiae regulates G2/M
RT transitions during the mitotic cell cycle and DNA-damage response.";
RL Genetics 150:1419-1428(1998).
RN [5]
RP IDENTIFICATION OF PRION FORM.
RX PubMed=11805042; DOI=10.1093/genetics/160.1.25;
RA Volkov K.V., Aksenova A.Y., Soom M.J., Osipov K.V., Svitin A.V.,
RA Kurischko C., Shkundina I.S., Ter-Avanesyan M.D., Inge-Vechtomov S.G.,
RA Mironova L.N.;
RT "Novel non-Mendelian determinant involved in the control of translation
RT accuracy in Saccharomyces cerevisiae.";
RL Genetics 160:25-36(2002).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=15466158; DOI=10.1101/gad.1228804;
RA Jorgensen P., Rupes I., Sharom J.R., Schneper L., Broach J.R., Tyers M.;
RT "A dynamic transcriptional network communicates growth potential to
RT ribosome synthesis and critical cell size.";
RL Genes Dev. 18:2491-2505(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15353587; DOI=10.1073/pnas.0405353101;
RA Marion R.M., Regev A., Segal E., Barash Y., Koller D., Friedman N.,
RA O'Shea E.K.;
RT "Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein
RT gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14315-14322(2004).
RN [10]
RP FUNCTION.
RX PubMed=15806610; DOI=10.1002/yea.1218;
RA Cipollina C., Alberghina L., Porro D., Vai M.;
RT "SFP1 is involved in cell size modulation in respiro-fermentative growth
RT conditions.";
RL Yeast 22:385-399(2005).
RN [11]
RP IDENTIFICATION BY 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 [12]
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 [13]
RP FUNCTION, INTERACTION WITH TORC1 AND MRS6, AND PHOSPHORYLATION BY TORC1.
RX PubMed=19328065; DOI=10.1016/j.molcel.2009.01.034;
RA Lempiainen H., Uotila A., Urban J., Dohnal I., Ammerer G., Loewith R.,
RA Shore D.;
RT "Sfp1 interaction with TORC1 and Mrs6 reveals feedback regulation on TOR
RT signaling.";
RL Mol. Cell 33:704-716(2009).
RN [14]
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).
RN [15]
RP PRION FORMATION.
RX PubMed=20498075; DOI=10.1073/pnas.1005949107;
RA Rogoza T., Goginashvili A., Rodionova S., Ivanov M., Viktorovskaya O.,
RA Rubel A., Volkov K., Mironova L.;
RT "Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form
RT of the global transcriptional regulator Sfp1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10573-10577(2010).
CC -!- FUNCTION: Transcription factor that regulates ribosomal protein (RP)
CC and ribosome biogenesis (Ribi) gene expression in response to nutrients
CC and stress. Promotes RP gene expression under optimal growth
CC conditions. Leaves the nucleus upon environmental challenges, resulting
CC in a down-regulation of RP gene transcription. The effect of the
CC environmental cues on SFP1 localization is mediated through the TOR
CC pathway. Also regulates the expression of genes involved in the G2/M
CC transition during the mitotic cell cycle and the DNA-damage response.
CC Required for carbon-source modulation of cell size.
CC {ECO:0000269|PubMed:15353587, ECO:0000269|PubMed:15466158,
CC ECO:0000269|PubMed:15806610, ECO:0000269|PubMed:19328065,
CC ECO:0000269|PubMed:9832520}.
CC -!- SUBUNIT: Interacts with the target of rapamycin complex 1 (TORC1) in a
CC rapamycin-dependent manner. Interacts with MRS6.
CC {ECO:0000269|PubMed:19328065}.
CC -!- INTERACTION:
CC P32432; P32864: MRS6; NbExp=5; IntAct=EBI-17035, EBI-14799;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear under optimal
CC growth conditions. Leaves the nucleus in response to stress or changes
CC in nutrient availability. The [ISP+] aggregates appear to be nuclear.
CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is
CC unstructured in its native, soluble form, and which forms a parallel
CC in-register beta-sheet in its amyloid form. {ECO:0000250}.
CC -!- PTM: Phosphorylated by TORC1 kinase at multiple sites. Phosphorylation
CC regulates nuclear localization and RP promoter binding.
CC {ECO:0000269|PubMed:19328065}.
CC -!- MISCELLANEOUS: [ISP+] is the prion form of SFP1. [ISP+] is the result
CC of a conformational change of the cellular SFP1 protein that becomes
CC self-propagating and infectious. This conformational change generates a
CC form of SFP1 that assembles into amyloid fibrils. [ISP+]-aggregates
CC accumulate in the nucleus, and results in significantly larger cell
CC size and increased drug resistance (PubMed:20498075). [ISP+] can be
CC cured by GdnHCl (PubMed:11805042). It is speculated that prion
CC properties of transcription factors may generate an optimized
CC phenotypic heterogeneity that buffers yeast populations against diverse
CC environmental insults (PubMed:20498075). {ECO:0000305|PubMed:11805042,
CC ECO:0000305|PubMed:20498075}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M63577; AAA35041.1; ALT_INIT; Genomic_DNA.
DR EMBL; U19729; AAB82343.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09702.1; -; Genomic_DNA.
DR PIR; JH0497; JH0497.
DR RefSeq; NP_013507.1; NM_001182291.1.
DR AlphaFoldDB; P32432; -.
DR BioGRID; 31660; 56.
DR DIP; DIP-1379N; -.
DR IntAct; P32432; 19.
DR MINT; P32432; -.
DR STRING; 4932.YLR403W; -.
DR iPTMnet; P32432; -.
DR MaxQB; P32432; -.
DR PaxDb; P32432; -.
DR PRIDE; P32432; -.
DR EnsemblFungi; YLR403W_mRNA; YLR403W; YLR403W.
DR GeneID; 851119; -.
DR KEGG; sce:YLR403W; -.
DR SGD; S000004395; SFP1.
DR VEuPathDB; FungiDB:YLR403W; -.
DR eggNOG; KOG4124; Eukaryota.
DR GeneTree; ENSGT00390000003635; -.
DR HOGENOM; CLU_013026_0_1_1; -.
DR InParanoid; P32432; -.
DR OMA; DHEEHKP; -.
DR BioCyc; YEAST:G3O-32465-MON; -.
DR PRO; PR:P32432; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32432; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0008361; P:regulation of cell size; IMP:SGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Amyloid; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Prion; Reference proteome; Repeat; Stress response; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..683
FT /note="Transcription factor SFP1"
FT /id="PRO_0000046851"
FT ZN_FING 598..623
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 659..683
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 156..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..458
FT /note="Prion domain (PrD)"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74785 MW; 0332A381D75A6F14 CRC64;
MDFTTMTMAS NMATSTTTTA TSAHASINSS SNFNIDIDSN QNTPSILINN NSDSSNGKNT
DFNGVNNIHQ KNIMNNTNNV HLYSPNIMDQ TLLTPQDIAK LRRESIAHSQ GMGGVSWGSI
SVGSWLRDEI ISRRNSIVPA SANGAASAAA SATTTATNTL QIQQPTKRPS VSNPPYHRGY
SISPQIAYTA YLPNLEKQYC KDYSCCGLSL PGLHDLLRHY EEAHISTSPN TTNMSQIPMN
SAGNTSSSVR MTNNTSSANY NLQNNMAANT KNAGHKTNTM QAHSSNATNN TSINNMHANL
QSNMDSNSTI RQSQHPHHQQ NIIQQQLQSN SVNHTSGAVP TPSVMGSATA SSTTANPNVI
SITGAPNSGL SMANHSQQLH LNGNLVDAVS TNDVFLRTSN SPSRHVPHNK QINSNNNSGI
NINNNTSHNS NINMGSKNAM VNRPHTFNNY SLNKTSRNPI QHQSRKIDPH QTDLSPLVLV
QDIDLSFMDD DILGPSNHNS MNSVVNPTTG SHNYNTFHSS VHAKSSQNMV EDQDIDDIDD
DDDVDDDDDD DDDDDTENGS SSNGKSVHNN NYKMPQQAYI DDPARRLYVM DHEEQKPFKC
PVIGCEKTYK NQNGLKYHRL HGHQNQKLHE NPDGTFSVID PDSTDSFGDG MGSAKDKPYR
CEVCGKRYKN LNGLKYHRGH STH
