EAF6_CHICK
ID EAF6_CHICK Reviewed; 182 AA.
AC Q5ZIX3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Chromatin modification-related protein MEAF6;
DE Short=MYST/Esa1-associated factor 6;
DE AltName: Full=Esa1-associated factor 6 homolog;
DE Short=Protein EAF6 homolog;
GN Name=MEAF6; ORFNames=RCJMB04_23a7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of select genes principally
CC by acetylation of nucleosomal histone H4 and H2A. This modification may
CC both alter nucleosome - DNA interactions and promote interaction of the
CC modified histones with other proteins which positively regulate
CC transcription. Component of HBO1 complexes, which specifically mediate
CC acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced
CC activity toward histone H4. Component of the MOZ/MORF complex which has
CC a histone H3 acetyltransferase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9HAF1}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC Component of the hbo1 complex. Component of the moz/morf complex (By
CC similarity). {ECO:0000250|UniProtKB:Q9HAF1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9HAF1}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9HAF1}.
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; AJ720661; CAG32320.1; -; mRNA.
DR RefSeq; NP_001026068.1; NM_001030897.1.
DR AlphaFoldDB; Q5ZIX3; -.
DR SMR; Q5ZIX3; -.
DR STRING; 9031.ENSGALP00000003129; -.
DR PaxDb; Q5ZIX3; -.
DR Ensembl; ENSGALT00000059068; ENSGALP00000050953; ENSGALG00000002013.
DR GeneID; 419617; -.
DR KEGG; gga:419617; -.
DR CTD; 64769; -.
DR VEuPathDB; HostDB:geneid_419617; -.
DR eggNOG; KOG3856; Eukaryota.
DR GeneTree; ENSGT00390000015257; -.
DR InParanoid; Q5ZIX3; -.
DR PhylomeDB; Q5ZIX3; -.
DR PRO; PR:Q5ZIX3; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000002013; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; Q5ZIX3; baseline and differential.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR InterPro; IPR015418; Eaf6.
DR PANTHER; PTHR13476; PTHR13476; 1.
DR Pfam; PF09340; NuA4; 1.
PE 2: Evidence at transcript level;
KW Activator; Centromere; Chromatin regulator; Chromosome; Coiled coil;
KW Kinetochore; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..182
FT /note="Chromatin modification-related protein MEAF6"
FT /id="PRO_0000272611"
FT REGION 107..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..49
FT /evidence="ECO:0000255"
FT COMPBIAS 165..182
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20458 MW; 5DA18114B8997EFA CRC64;
MAALHAKAGG PPQIPDTRRE LAELVKRKQE LAETLANLER QIYAFEGSYL EDTQMYGNII
RGWDRYLTNQ KNSNSKNDRR NRKFKEAERL FSKSSVTSAA AVSALAGVQD QLIEKREPGS
GTESDTSPDF HNQENEPSQE DAEELDGSVQ GVKPQKAASS TSGSHHSSHK KRKNKNRHRY
VY