EAF3_SCHPO
ID EAF3_SCHPO Reviewed; 337 AA.
AC O13953;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Chromatin modification-related protein eaf3;
DE AltName: Full=Altered polarity protein 13;
DE AltName: Full=ESA1-associated factor 3;
GN Name=alp13; Synonyms=eaf3; ORFNames=SPAC23H4.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Radcliffe P.A., Toda T.;
RT "Chromo domain protein required for cell polarity.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 105-123; 129-138; 147-169 AND 311-332, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12773392; DOI=10.1093/emboj/cdg248;
RA Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K.,
RA Kobayashi R., Grewal S.I.S.;
RT "Alp13, an MRG family protein, is a component of fission yeast Clr6 histone
RT deacetylase required for genomic integrity.";
RL EMBO J. 22:2776-2787(2003).
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 (By similarity). Also involved in
CC deacetylation of histones, chromatin assembly and chromosome
CC segregation. May act as a transcriptional oscillator, directing histone
CC deacetylases to specific chromosomal domains. {ECO:0000250,
CC ECO:0000269|PubMed:12773392}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex (By
CC similarity). Heterotetramer of alp13, clr6, prw1 and pst2.
CC {ECO:0000250, ECO:0000269|PubMed:12773392}.
CC -!- INTERACTION:
CC O13953; O13919: pst2; NbExp=4; IntAct=EBI-904711, EBI-904686;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972,
CC ECO:0000269|PubMed:12773392}.
CC -!- SIMILARITY: Belongs to the MRG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB015294; BAA28826.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11666.1; -; Genomic_DNA.
DR PIR; T43372; T43372.
DR RefSeq; NP_593394.1; NM_001018826.2.
DR AlphaFoldDB; O13953; -.
DR SMR; O13953; -.
DR BioGRID; 278348; 241.
DR DIP; DIP-29343N; -.
DR IntAct; O13953; 5.
DR STRING; 4896.SPAC23H4.12.1; -.
DR iPTMnet; O13953; -.
DR MaxQB; O13953; -.
DR PaxDb; O13953; -.
DR PRIDE; O13953; -.
DR EnsemblFungi; SPAC23H4.12.1; SPAC23H4.12.1:pep; SPAC23H4.12.
DR GeneID; 2541858; -.
DR KEGG; spo:SPAC23H4.12; -.
DR PomBase; SPAC23H4.12; alp13.
DR VEuPathDB; FungiDB:SPAC23H4.12; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; O13953; -.
DR OMA; GLQTYFD; -.
DR PhylomeDB; O13953; -.
DR PRO; PR:O13953; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:PomBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; ISO:PomBase.
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 PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Direct protein sequencing; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..337
FT /note="Chromatin modification-related protein eaf3"
FT /id="PRO_0000088780"
FT DOMAIN 6..56
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 166..336
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 70..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 39138 MW; 827B85CE12CAE8CC CRC64;
MAVSYKVNER VLCFHGPLLY EAKIVDTEMK GDVTTYLIHY KGWKNSWDEW VEQDRILQWT
EENLKTQKEL KNAAISTRQK PTSKKSASST SKHDSTGVKT SGKRSRESST VTVDGDSHEL
PSRIKTQKSE SPIPQQVKRD GTTDAKNEET TKPENNEKDD FEEEPPLPKH KISVPDVLKL
WLVDDWENIT KNQQLIAIPR NPTVRAAIAA FRESKISHLN NEIDVDVFEQ AMAGLVIYFN
KCLGNMLLYR FERQQYLEIR QQYPDTEMCD LYGVEHLIRL FVSLPELIDR TNMDSQSIEC
LLNYIEEFLK YLVLHKDEYF IKEYQNAPPN YRSLVGV
