SWI1_YEAST
ID SWI1_YEAST Reviewed; 1314 AA.
AC P09547; D6W3Z6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=SWI/SNF chromatin-remodeling complex subunit SWI1;
DE AltName: Full=Regulatory protein GAM3;
DE AltName: Full=SWI/SNF complex subunit SWI1;
DE AltName: Full=Transcription regulatory protein ADR6;
DE AltName: Full=Transcription regulatory protein SWI1;
GN Name=SWI1; Synonyms=ADR6, GAM3; OrderedLocusNames=YPL016W; ORFNames=LPA1;
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=3143101; DOI=10.1093/nar/16.21.10153;
RA O'Hara P.J., Horowitz H., Eichinger G., Young E.T.;
RT "The yeast ADR6 gene encodes homopolymeric amino acid sequences and a
RT potential metal-binding domain.";
RL Nucleic Acids Res. 16:10153-10169(1988).
RN [2]
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 [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 CHARACTERIZATION.
RX PubMed=1339306; DOI=10.1016/0092-8674(92)90192-f;
RA Peterson C.L., Herskowitz I.;
RT "Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a
RT global activator of transcription.";
RL Cell 68:573-583(1992).
RN [5]
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 [6]
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 [7]
RP PRION FORMATION, PRION CURING, AND SUBCELLULAR LOCATION OF PRION
RP AGGREGATES.
RX PubMed=18362884; DOI=10.1038/ng.112;
RA Du Z., Park K.W., Yu H., Fan Q., Li L.;
RT "Newly identified prion linked to the chromatin-remodeling factor Swi1 in
RT Saccharomyces cerevisiae.";
RL Nat. Genet. 40:460-465(2008).
RN [8]
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 [9]
RP PRION FORMATION, AND AMYLOID FORMATION.
RX PubMed=20679490; DOI=10.1128/mcb.00225-10;
RA Du Z., Crow E.T., Kang H.S., Li L.;
RT "Distinct subregions of Swi1 manifest striking differences in prion
RT transmission and SWI/SNF function.";
RL Mol. Cell. Biol. 30:4644-4655(2010).
RN [10]
RP DOMAIN PRION.
RX PubMed=21670156; DOI=10.1128/mcb.05338-11;
RA Crow E.T., Du Z., Li L.;
RT "A small, glutamine-free domain propagates the [SWI(+)] prion in budding
RT yeast.";
RL Mol. Cell. Biol. 31:3436-3444(2011).
RN [11]
RP PRION FORMATION.
RX PubMed=21379326; DOI=10.1371/journal.pgen.1001309;
RA Hines J.K., Li X., Du Z., Higurashi T., Li L., Craig E.A.;
RT "[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly
RT sensitive to alterations in Hsp70 chaperone system activity.";
RL PLoS Genet. 7:E1001309-E1001309(2011).
RN [12]
RP 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP THE SWI/SNF COMPLEX.
RX PubMed=12524530; DOI=10.1038/nsb888;
RA Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA Peterson C.L.;
RT "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL Nat. Struct. Biol. 10:141-145(2003).
RN [13]
RP STRUCTURE BY NMR OF 405-506.
RX PubMed=11727987; DOI=10.1023/a:1012434510376;
RA Tu X., Wu J., Xu Y., Shi Y.;
RT "1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-
RT binding domain.";
RL J. Biomol. NMR 21:187-188(2001).
CC -!- FUNCTION: Involved in transcriptional activation. Component of the
CC SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which
CC is required for the positive and negative regulation of gene expression
CC of a large number of genes. It changes chromatin structure by altering
CC DNA-histone contacts within a nucleosome, leading eventually to a
CC change in nucleosome position, thus facilitating or repressing binding
CC of gene-specific transcription factors.
CC -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC complex. The 1.14 MDa SWI/SNF complex is composed of 11 different
CC subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73,
CC ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82;
CC and three copies of TAF14/SWP29.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:18362884}. Note=While the soluble protein is
CC nuclear, [SWI+] aggregates appear to be cytoplasmic.
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 (By similarity). The first
CC 37 residues of this domain are sufficient for aggregation, propagation,
CC and transmission of the [SWI+] prion. {ECO:0000250,
CC ECO:0000269|PubMed:21670156}.
CC -!- MISCELLANEOUS: [SWI+] is the prion form of SWI1 (PubMed:18362884).
CC [SWI+] is the result of a conformational change of the cellular SWI1
CC protein that becomes self-propagating and infectious. This
CC conformational change generates a form of SWI1 that assembles into
CC amyloid fibrils (PubMed:20679490). [SWI+]-aggregates sequester soluble
CC SWI1, resulting in reduced growth on carbon sources other than glucose,
CC reminiscent of a partial loss of function of the SWI/SNF chromatin-
CC remodeling complex. [SWI+] can be cured by GdnHCl and by deletion of
CC the molecular chaperone HSP104, which is required for [SWI+]
CC propagation (PubMed:18362884). [SWI+] propagation is highly dependent
CC upon the action of members of the Hsp70 molecular chaperone system,
CC specifically the Hsp70 SSA, two of its J-protein co-chaperones, SIS1
CC and YDJ1, and the nucleotide exchange factors of the Hsp110 family
CC (SSE1/2). Both under- and overexpression of components of this system
CC initiate rapid loss of the prion from the cell population. It is
CC speculated that prion properties of transcription factors may generate
CC an optimized phenotypic heterogeneity that buffers yeast populations
CC against diverse environmental insults (PubMed:21379326).
CC {ECO:0000305|PubMed:18362884, ECO:0000305|PubMed:20679490,
CC ECO:0000305|PubMed:21379326}.
CC -!- MISCELLANEOUS: Present with 92 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SWI1 family. {ECO:0000305}.
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DR EMBL; X12493; CAA31013.1; -; Genomic_DNA.
DR EMBL; U33335; AAB68089.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11412.1; -; Genomic_DNA.
DR PIR; S05728; TNBYR6.
DR RefSeq; NP_015309.1; NM_001183830.2.
DR PDB; 1KKX; NMR; -; A=405-506.
DR PDB; 1KN5; NMR; -; A=405-506.
DR PDB; 2LI6; NMR; -; A=390-505.
DR PDB; 6UXV; EM; 4.70 A; B=1-1314.
DR PDB; 6UXW; EM; 8.96 A; B=1-1314.
DR PDB; 7C4J; EM; 2.89 A; I=1-1314.
DR PDB; 7EGM; EM; 3.60 A; B=251-1314.
DR PDB; 7EGP; EM; 6.90 A; B=251-1314.
DR PDBsum; 1KKX; -.
DR PDBsum; 1KN5; -.
DR PDBsum; 2LI6; -.
DR PDBsum; 6UXV; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EGM; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; P09547; -.
DR BMRB; P09547; -.
DR SMR; P09547; -.
DR BioGRID; 36161; 335.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-1032N; -.
DR IntAct; P09547; 39.
DR MINT; P09547; -.
DR STRING; 4932.YPL016W; -.
DR iPTMnet; P09547; -.
DR MaxQB; P09547; -.
DR PaxDb; P09547; -.
DR PRIDE; P09547; -.
DR EnsemblFungi; YPL016W_mRNA; YPL016W; YPL016W.
DR GeneID; 856091; -.
DR KEGG; sce:YPL016W; -.
DR SGD; S000005937; SWI1.
DR VEuPathDB; FungiDB:YPL016W; -.
DR eggNOG; KOG2744; Eukaryota.
DR HOGENOM; CLU_002419_0_0_1; -.
DR InParanoid; P09547; -.
DR OMA; GPHMSPS; -.
DR BioCyc; YEAST:G3O-33935-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR EvolutionaryTrace; P09547; -.
DR PRO; PR:P09547; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P09547; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IMP:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0031496; P:positive regulation of mating type switching; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061412; P:positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Amyloid; DNA-binding; Metal-binding; Nucleus;
KW Prion; Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1314
FT /note="SWI/SNF chromatin-remodeling complex subunit SWI1"
FT /id="PRO_0000200596"
FT DOMAIN 406..493
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT ZN_FING 1241..1258
FT /note="C4-type"
FT REGION 1..323
FT /note="Prion domain (PrD)"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2LI6"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:2LI6"
FT HELIX 408..422
FT /evidence="ECO:0007829|PDB:1KKX"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:1KKX"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:1KKX"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:1KKX"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:1KKX"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:1KKX"
FT HELIX 460..469
FT /evidence="ECO:0007829|PDB:1KKX"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:1KKX"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:1KN5"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:1KN5"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 673..677
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 679..692
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 707..715
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 719..733
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 747..764
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 791..808
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 868..871
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 884..895
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 910..928
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 932..940
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 942..956
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 959..961
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 965..982
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 991..1002
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1036..1046
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1052..1062
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1078..1093
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1104..1115
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1119..1124
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1130..1153
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1189..1194
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 1196..1198
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1200..1213
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1234..1259
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1265..1270
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1279..1287
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 1289..1291
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 1293..1313
FT /evidence="ECO:0007829|PDB:7C4J"
SQ SEQUENCE 1314 AA; 147938 MW; F442D5A82013CDBD CRC64;
MDFFNLNNNN NNNNTTTTTT TTNNNNTNNN NTNNNNNPAN NTNNNNSTGH SSNTNNNTNN
NNTNTGASGV DDFQNFFDPK PFDQNLDSNN NNSNSNNNDN NNSNTVASST NFTSPTAVVN
NAAPANVTGG KAANFIQNQS PQFNSPYDSN NSNTNLNSLS PQAILAKNSI IDSSNLPLQA
QQQLYGGNNN NNSTGIANDN VITPHFITNV QSISQNSSSS TPNTNSNSTP NANQQFLPFN
NSASNNGNLT SNQLISNYAA SNSMDRSSSA SNEFVPNTSD NNNNSNNHNM RNNSNNKTSN
NNNVTAVPAA TPANTNNSTS NANTVFSERA AMFAALQQKQ QQRFQALQQQ QQQQQNQQQQ
NQQPQQQQQQ QQNPKFLQSQ RQQQQRSILQ SLNPALQEKI STELNNKQYE LFMKSLIENC
KKRNMPLQSI PEIGNRKINL FYLYMLVQKF GGADQVTRTQ QWSMVAQRLQ ISDYQQLESI
YFRILLPYER HMISQEGIKE TQAKRIFLQQ FLQELLKKVQ QQQQAAALAN ANNNINSASS
APTPAAPGAS VPATAAPGTE AGIVPVSANT PKSLNSNINI NVNNNNIGQQ QVKKPRKQRV
KKKTKKELEL ERKEREDFQK RQQKLLEDQQ RQQKLLLETK LRQQYEIELK KLPKVYKRSI
VRNYKPLINR LKHYNGYDIN YISKIGEKID SNKPIFLFAP ELGAINLHAL SMSLQSKNLG
EINTALNTLL VTSADSNLKI SLVKYPELLD SLAILGMNLL SNLSQNVVPY HRNTSDYYYE
DAGSNQYYVT QHDKMVDKIF EKVNNNATLT PNDSNDEKVT ILVDSLTGNQ LPTPTPTEME
PDLDTECFIS MQSTSPAVKQ WDLLPEPIRF LPNQFPLKIH RTPYLTSLKK IKDEIDDPFT
KINTRGAEDP KVLINDQLST ISMILRNISF SDNNSRIMSR NFYLKRFISD LLWLVLIHPE
NFTCNRKILN FKKDLVIVLS NISHLLEIAS SIDCLLILIL VISFGQPKLN PMASSSSFGS
ESLTFNEFQL QWGKYQTFGV DILAKLFSLE KPNLNYFKSI LLNKNTGNNL YDRNSNNNHK
DKKLLRRLLN LYNDNNKNNN NRHNLLNDVV SFLFSAIPLQ QVLSQSADPS LLIDQFSPVI
SQSLTSILVI VQKILPLSNE VFEISENNSD SNSNNNGNKD SSFNFNKNLP FVWLSSEENI
GSGLLKLSEI ILNINNSTSK NTLLQQQNYS KVLLPSINIS CVQLIKCLVE KSICFENCLN
NDPEILKKIA SIPNLFPTDL EIFQLFTNPS VDIQIINQYQ LLYNLKNDIL TNLE
