EAF3_DROME
ID EAF3_DROME Reviewed; 424 AA.
AC Q9Y0I1; Q9VF99;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=NuA4 complex subunit EAF3 homolog;
DE AltName: Full=Protein MRG15;
GN Name=MRG15; ORFNames=CG6363;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11290425; DOI=10.1016/s0378-1119(01)00372-9;
RA Bertram M.J., Pereira-Smith O.M.;
RT "Conservation of the MORF4 related gene family: identification of a new
RT chromo domain subfamily and novel protein motif.";
RL Gene 266:111-121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; THR-175; THR-183;
RP THR-196; THR-197; SER-211 AND THR-235, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Part of the Tip60 chromatin-remodeling complex which is
CC involved in DNA repair. Upon induction of DNA double-strand breaks,
CC this complex acetylates phosphorylated H2AV in nucleosomes and
CC exchanges it with unmodified H2AV. {ECO:0000269|PubMed:15528408}.
CC -!- SUBUNIT: Component of the Tip60 chromatin-remodeling complex which
CC contains the catalytic subunit Tip60 and the subunits Domino, Tra1,
CC Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP,
CC Gas41 and YL-1. {ECO:0000269|PubMed:15528408}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AF152245; AAD38047.1; -; mRNA.
DR EMBL; AE014297; AAF55161.1; -; Genomic_DNA.
DR EMBL; AY051679; AAK93103.1; -; mRNA.
DR RefSeq; NP_650442.1; NM_142185.2.
DR PDB; 2LRQ; NMR; -; A=11-94.
DR PDBsum; 2LRQ; -.
DR AlphaFoldDB; Q9Y0I1; -.
DR SMR; Q9Y0I1; -.
DR BioGRID; 66914; 41.
DR DIP; DIP-20132N; -.
DR IntAct; Q9Y0I1; 2.
DR STRING; 7227.FBpp0306049; -.
DR iPTMnet; Q9Y0I1; -.
DR PaxDb; Q9Y0I1; -.
DR PRIDE; Q9Y0I1; -.
DR DNASU; 41850; -.
DR EnsemblMetazoa; FBtr0083125; FBpp0082579; FBgn0027378.
DR GeneID; 41850; -.
DR KEGG; dme:Dmel_CG6363; -.
DR UCSC; CG6363-RA; d. melanogaster.
DR CTD; 41850; -.
DR FlyBase; FBgn0027378; MRG15.
DR VEuPathDB; VectorBase:FBgn0027378; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_4_0_1; -.
DR InParanoid; Q9Y0I1; -.
DR PhylomeDB; Q9Y0I1; -.
DR SignaLink; Q9Y0I1; -.
DR BioGRID-ORCS; 41850; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 41850; -.
DR PRO; PR:Q9Y0I1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027378; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9Y0I1; baseline and differential.
DR Genevisible; Q9Y0I1; DM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IPI:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IPI:FlyBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:FlyBase.
DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0051304; P:chromosome separation; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
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:0010628; P:positive regulation of gene expression; IGI:FlyBase.
DR GO; GO:0000416; P:positive regulation of histone H3-K36 methylation; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..424
FT /note="NuA4 complex subunit EAF3 homolog"
FT /id="PRO_0000088771"
FT DOMAIN 23..73
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 252..424
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 88..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2LRQ"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2LRQ"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:2LRQ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2LRQ"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2LRQ"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2LRQ"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2LRQ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2LRQ"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:2LRQ"
SQ SEQUENCE 424 AA; 47194 MW; B0E1F615252D8EDD CRC64;
MGEVKPAKVE NYSTGTDANT LFVDGERVLC FHGPLIYEAK VLKTKPDATP VEYYIHYAGW
SKNWDEWVPE NRVLKYNDDN VKRRQELARQ CGERSKKDNK KGSAKAKKME QMRNESRAST
PSKDSNTSQS TASSTPTTSA GPGSKSEAGS TGTTTTNSTA NSTTSRAHRK STQSTPSTAR
PGTPSDKKED PAAAETTEEE GPVAPKKKRM SEQRPSLTGS DVAEKPLPPT TTPSTPTTEP
APCVESEEAY AAKVEVKIKI PDELKHYLTD DWYAVVREHK LLELPAKVTV QQISEQYLAH
KKSVKSTSAS KEVAINDVLD GIVEYFNVML GSQLLYKFER TQYADVMQKH PDTPLSELYG
SFHLLRLFVR LGSMLSYSAL DQQSMQNLLT HVQDFLKFLV KNSSIFFSMS NFINVDPEYV
RNAQ
