ID   SWC3_YEAST              Reviewed;         625 AA.
AC   P31376; D6VPK7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   02-SEP-2026, entry version 169.
DE   RecName: Full=SWR1-complex protein 3;
GN   Name=SWC3; Synonyms=FUN36, SWC1; OrderedLocusNames=YAL011W;
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].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8458570; DOI=10.1139/g93-005;
RA   Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA   Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT   "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT   kb region between the LTE1 and SPO7 genes.";
RL   Genome 36:32-42(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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   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   [5]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
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   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   [9]
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   [10]
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: 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 1380 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SWC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC04946.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L05146; AAC04946.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006935; DAA06977.1; -; Genomic_DNA.
DR   PIR; S36723; S36723.
DR   RefSeq; NP_009391.2; NM_001178156.1.
DR   PDB; 9B1E; EM; 4.40 A; K=1-625.
DR   AlphaFoldDB; P31376; -.
DR   EMDB; EMD-44075; -.
DR   SMR; P31376; -.
DR   BioGRID; 31755; 599.
DR   ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR   DIP; DIP-2986N; -.
DR   FunCoup; P31376; 170.
DR   IntAct; P31376; 26.
DR   MINT; P31376; -.
DR   STRING; 4932.YAL011W; -.
DR   GlyGen; P31376; 1 site.
DR   iPTMnet; P31376; -.
DR   PaxDb; 4932-YAL011W; -.
DR   PeptideAtlas; P31376; -.
DR   EnsemblFungi; YAL011W_mRNA; YAL011W; YAL011W.
DR   GeneID; 851222; -.
DR   KEGG; sce:YAL011W; -.
DR   AGR; SGD:S000000009; -.
DR   SGD; S000000009; SWC3.
DR   VEuPathDB; FungiDB:YAL011W; -.
DR   eggNOG; ENOG502QWM7; Eukaryota.
DR   HOGENOM; CLU_008595_1_0_1; -.
DR   InParanoid; P31376; -.
DR   OMA; MQKMCDC; -.
DR   OrthoDB; 4097064at2759; -.
DR   BioCyc; YEAST:G3O-28824-MONOMER; -.
DR   BioGRID-ORCS; 851222; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P31376; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P31376; protein.
DR   GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR   GO; GO:0140849; F:ATP-dependent H2AZ histone chaperone activity; IEA:InterPro.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   InterPro; IPR037651; Swc3.
DR   InterPro; IPR058986; Swc3_C.
DR   InterPro; IPR057558; Swc3_dom.
DR   PANTHER; PTHR28108; SWR1-COMPLEX PROTEIN 3; 1.
DR   PANTHER; PTHR28108:SF1; SWR1-COMPLEX PROTEIN 3; 1.
DR   Pfam; PF24707; Swc3; 1.
DR   Pfam; PF26242; Swc3_C; 1.
DR   PDBsum; 9B1E; -.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..625
FT                   /note="SWR1-complex protein 3"
FT                   /id="PRO_0000072344"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..31
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  72514 MW;  A4F13DB85B657D59 CRC64;
     MPAVLRTRSK ESSIEQKPAS RTRTRSRRGK RGRDDDDDDD DEESDDAYDE VGNDYDEYAS
     RAKLATNRPF EIVAGLPASV ELPNYNSSLT HPQSIKNSGV LYDSLVSSRR TWVQGEMFEL
     YWRRPKKIVS ESTPAATESP TSGTIPLIRD KMQKMCDCVM SGGPHTFKVR LFILKNDKIE
     QKWQDEQELK KKEKELKRKN DAEAKRLRME ERKRQQMQKK IAKEQKLQLQ KENKAKQKLE
     QEALKLKRKE EMKKLKEQNK NKQGSPSSSM HDPRMIMNLN LMAQEDPKLN TLMETVAKGL
     ANNSQLEEFK KFIEIAKKRS LEENPVNKRP SVTTTRPAPP SKAKDVAEDH RLNSITLVKS
     SKTAATEPEP KKADDENAEK QQSKEAKTTA ESTQVDVKKE EEDVKEKGVK SEDTQKKEDN
     QVVPKRKRRK NAIKEDKDMQ LTAFQQKYVQ GAEIILEYLE FTHSRYYLPK KSVVEFLEDT
     DEIIISWIVI HNSKEIEKFK TKKIKAKLKA DQKLNKEDAK PGSDVEKEVS FNPLFEADCP
     TPLYTPMTMK LSGIHKRFNQ IIRNSVSPME EVVKEMEKIL QIGTRLSGYN LWYQLDGYDD
     EALSESLRFE LNEWEHAMRS RRHKR
//