EAF3_YEAST
ID EAF3_YEAST Reviewed; 401 AA.
AC Q12432; D6W433;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Chromatin modification-related protein EAF3;
DE AltName: Full=ESA1-associated factor 3;
GN Name=EAF3; OrderedLocusNames=YPR023C; ORFNames=YP9367.03C;
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=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 [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 PROTEIN SEQUENCE OF 2-13; 37-54; 61-75; 86-96; 121-127; 131-143; 157-170;
RP 175-187; 201-227; 230-241; 248-260; 304-311 AND 316-333, IDENTIFICATION IN
RP THE NUA4 COMPLEX, AND FUNCTION.
RX PubMed=11036083; DOI=10.1074/jbc.m008159200;
RA Eisen A., Utley R.T., Nourani A., Allard S., Schmidt P., Lane W.S.,
RA Lucchesi J.C., Cote J.;
RT "The yeast NuA4 and Drosophila MSL complexes contain homologous subunits
RT important for transcriptional regulation.";
RL J. Biol. Chem. 276:3484-3491(2001).
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 FUNCTION.
RX PubMed=14701747; DOI=10.1128/mcb.24.2.757-764.2004;
RA Reid J.L., Moqtaderi Z., Struhl K.;
RT "Eaf3 regulates the global pattern of histone acetylation in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 24:757-764(2004).
RN [7]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15485911; DOI=10.1128/mcb.24.21.9424-9436.2004;
RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H.,
RA Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper
RT gene expression, histone H4 acetylation, and Htz1 replacement near
RT telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP 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 NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP 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 NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. {ECO:0000269|PubMed:11036083,
CC ECO:0000269|PubMed:14701747, ECO:0000269|PubMed:15045029}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6,
CC EAF7, EPL1, ESA1, TRA1 and YNG2. {ECO:0000269|PubMed:11036083,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15353583,
CC ECO:0000269|PubMed:15485911}.
CC -!- INTERACTION:
CC Q12432; P39995: EAF5; NbExp=11; IntAct=EBI-6281, EBI-22312;
CC Q12432; Q08649: ESA1; NbExp=11; IntAct=EBI-6281, EBI-6648;
CC Q12432; P22579: SIN3; NbExp=8; IntAct=EBI-6281, EBI-17160;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MRG family. {ECO:0000305}.
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DR EMBL; Z71255; CAA95019.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89277.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11449.1; -; Genomic_DNA.
DR PIR; S54497; S54497.
DR RefSeq; NP_015348.1; NM_001184120.1.
DR PDB; 2K3X; NMR; -; A=1-113.
DR PDB; 2K3Y; NMR; -; A=1-115.
DR PDB; 3E9F; X-ray; 1.80 A; A=1-113.
DR PDB; 3E9G; X-ray; 2.50 A; A/B=1-124.
DR PDB; 6K5W; NMR; -; A=1-120.
DR PDBsum; 2K3X; -.
DR PDBsum; 2K3Y; -.
DR PDBsum; 3E9F; -.
DR PDBsum; 3E9G; -.
DR PDBsum; 6K5W; -.
DR AlphaFoldDB; Q12432; -.
DR SMR; Q12432; -.
DR BioGRID; 36200; 479.
DR ComplexPortal; CPX-1851; RPD3S histone deacetylase complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-3184; EAF5-7-3 nucleosome disassembly/reassembly complex.
DR DIP; DIP-2871N; -.
DR IntAct; Q12432; 41.
DR MINT; Q12432; -.
DR STRING; 4932.YPR023C; -.
DR iPTMnet; Q12432; -.
DR MaxQB; Q12432; -.
DR PaxDb; Q12432; -.
DR PRIDE; Q12432; -.
DR EnsemblFungi; YPR023C_mRNA; YPR023C; YPR023C.
DR GeneID; 856134; -.
DR KEGG; sce:YPR023C; -.
DR SGD; S000006227; EAF3.
DR VEuPathDB; FungiDB:YPR023C; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q12432; -.
DR OMA; GLQTYFD; -.
DR BioCyc; YEAST:G3O-34183-MON; -.
DR EvolutionaryTrace; Q12432; -.
DR PRO; PR:Q12432; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12432; protein.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990453; C:nucleosome disassembly/reassembly complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IMP:ComplexPortal.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IMP:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:ComplexPortal.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0043487; P:regulation of RNA stability; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR DisProt; DP02466; -.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Direct protein sequencing; DNA damage;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..401
FT /note="Chromatin modification-related protein EAF3"
FT /id="PRO_0000088783"
FT DOMAIN 13..98
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 216..399
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 39..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2K3Y"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6K5W"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:3E9F"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2K3X"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2K3Y"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3E9F"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3E9F"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3E9F"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2K3X"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:3E9F"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6K5W"
SQ SEQUENCE 401 AA; 45203 MW; 63758DE9510D70DC CRC64;
MVDLEQEFAL GGRCLAFHGP LMYEAKILKI WDPSSKMYTS IPNDKPGGSS QATKEIKPQK
LGEDESIPEE IINGKCFFIH YQGWKSSWDE WVGYDRIRAY NEENIAMKKR LANEAKEAKK
SLLEQQKKKK LSTSLGGPSN GGKRKGDSRS NASISKSTSQ SFLTSSVSGR KSGRSSANSL
HPGSSLRSSS DQNGNDDRRR SSSLSPNMLH HIAGYPTPKI SLQIPIKLKS VLVDDWEYVT
KDKKICRLPA DVTVEMVLNK YEHEVSQELE SPGSQSQLSE YCAGLKLYFD KCLGNMLLYR
LERLQYDELL KKSSKDQKPL VPIRIYGAIH LLRLISVLPE LISSTTMDLQ SCQLLIKQTE
DFLVWLLMHV DEYFNDKDPN RSDDALYVNT SSQYEGVALG M
