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SWC5_YEAST
ID   SWC5_YEAST              Reviewed;         303 AA.
AC   P38326; D6VQM7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=SWR1-complex protein 5;
GN   Name=SWC5; Synonyms=AOR1; OrderedLocusNames=YBR231C; ORFNames=YBR1529;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA   Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA   Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA   Hughes T.R., Buratowski S., Greenblatt J.F.;
RT   "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT   variant Htz1.";
RL   Mol. Cell 12:1565-1576(2003).
RN   [4]
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   [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 IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA   Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA   Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT   "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT   deposits histone variant H2A.Z into euchromatin.";
RL   PLoS Biol. 2:587-599(2004).
RN   [7]
RP   IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14645854; DOI=10.1126/science.1090701;
RA   Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT   "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT   remodeling complex.";
RL   Science 303:343-348(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Involved in chromosome stability. {ECO:0000269|PubMed:14645854,
CC       ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin remodeling complex composed of
CC       at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4,
CC       SWC5, SWC7 and SWR1, and perhaps BDF1. {ECO:0000269|PubMed:14645854,
CC       ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1680 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SWC5 family. {ECO:0000305}.
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DR   EMBL; Z36100; CAA85194.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07347.1; -; Genomic_DNA.
DR   PIR; S46107; S46107.
DR   RefSeq; NP_009790.3; NM_001178579.3.
DR   PDB; 6KBB; X-ray; 2.37 A; E/F=1-79.
DR   PDBsum; 6KBB; -.
DR   AlphaFoldDB; P38326; -.
DR   SMR; P38326; -.
DR   BioGRID; 32926; 903.
DR   ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR   DIP; DIP-4260N; -.
DR   IntAct; P38326; 16.
DR   MINT; P38326; -.
DR   STRING; 4932.YBR231C; -.
DR   iPTMnet; P38326; -.
DR   MaxQB; P38326; -.
DR   PaxDb; P38326; -.
DR   PRIDE; P38326; -.
DR   EnsemblFungi; YBR231C_mRNA; YBR231C; YBR231C.
DR   GeneID; 852532; -.
DR   KEGG; sce:YBR231C; -.
DR   SGD; S000000435; SWC5.
DR   VEuPathDB; FungiDB:YBR231C; -.
DR   eggNOG; KOG4776; Eukaryota.
DR   HOGENOM; CLU_062474_1_0_1; -.
DR   InParanoid; P38326; -.
DR   OMA; LDWAAYV; -.
DR   BioCyc; YEAST:G3O-29163-MON; -.
DR   PRO; PR:P38326; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38326; protein.
DR   GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0043486; P:histone exchange; IMP:SGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   InterPro; IPR011421; BCNT-C.
DR   Pfam; PF07572; BCNT; 1.
DR   PROSITE; PS51279; BCNT_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..303
FT                   /note="SWR1-complex protein 5"
FT                   /id="PRO_0000212513"
FT   DOMAIN          217..294
FT                   /note="BCNT-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:6KBB"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:6KBB"
SQ   SEQUENCE   303 AA;  34344 MW;  985F66B3E3CB3F25 CRC64;
     MPEVETKIIP NEKEDEDEDG YIEEEDEDFQ PEKDKLGGGS DDSDASDGGD DYDDGVNRDK
     GRNKVDYSRI ESESGGLIKT RRARQAEEEY AKTHKYESLT VESIPAKVNS IWEELQEASK
     NRLLSSSGKV GSVLDGSKEA RSTTAAQQED KILIERNYKF AGETVHEKKW VSRSSAEGQE
     YLNSLKFKQQ APAAPVQLEK AVRTKSNESR QHLRRPLKRP PLLEQIISGG LRPKLTTLEK
     SQLDWASYVD RAGLNDELVL HNKDGFLARQ EFLQRVGSAE DERYKELRRQ QLAQQLQQDS
     EAS
 
 
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