(data stored in ACNUC7421 zone)

SWISSPROT: H2AZ_ASHGO

ID   H2AZ_ASHGO              Reviewed;         133 AA.
AC   Q75CC6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=Histone H2A.Z;
GN   Name=HTZ1; OrderedLocusNames=ACL017C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC       nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC       DNA accessibility to the cellular machineries which require DNA as a
CC       template. Histones thereby play a central role in transcription
CC       regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and nucleosome
CC       remodeling. This variant is enriched at promoters, it may keep them in
CC       a repressed state until the appropriate activation signal is received.
CC       Near telomeres, it may counteract gene silencing caused by the spread
CC       of heterochromatin proteins. Required for the RNA polymerase II and
CC       SPT15/TBP recruitment to the target genes. Involved in chromosome
CC       stability (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA. H2A or its variant H2A.Z forms a heterodimer with H2B. H2A.Z
CC       associates with the VPS72/SWC2 subunit of the SWR1 chromatin remodeling
CC       complex. Interacts also with RBP1/DNA-directed RNA polymerase II
CC       largest subunit (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- PTM: Acetylated by ESA1 and/or GCN5 to form H2A.ZK3Ac, H2A.ZK8Ac,
CC       H2A.ZK10Ac and H2A.ZK14Ac once deposited into chromatin. Acetylation is
CC       required for function at telomeres. H2A.ZK14Ac is acetylated at the
CC       promoters of active genes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2A.ZK3ac =
CC       acetylated Lys-4; H2A.ZK8ac = acetylated Lys-9; H2A.ZK10ac = acetylated
CC       Lys-11; H2A.ZK14ac = acetylated Lys-15. {ECO:0000305}.
DR   EMBL; AE016816; AAS51211.1; -; Genomic_DNA.
DR   RefSeq; NP_983387.1; NM_208740.1.
DR   SMR; Q75CC6; -.
DR   STRING; 33169.AAS51211; -.
DR   PRIDE; Q75CC6; -.
DR   EnsemblFungi; AAS51211; AAS51211; AGOS_ACL017C.
DR   GeneID; 4619512; -.
DR   KEGG; ago:AGOS_ACL017C; -.
DR   HOGENOM; HOG000234652; -.
DR   InParanoid; Q75CC6; -.
DR   KO; K11251; -.
DR   OMA; KQRTQHN; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0005719; C:nuclear euchromatin; IEA:EnsemblFungi.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IEA:EnsemblFungi.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:1903098; P:negative regulation of CENP-A containing nucleosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi.
DR   GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CC6.
DR   SWISS-2DPAGE; Q75CC6.
KW   Acetylation; Activator; Chromatin regulator; Chromosome; DNA-binding;
KW   Nucleosome core; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..133
FT                   /note="Histone H2A.Z"
FT                   /id="PRO_0000055328"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   133 AA;  14099 MW;  45DC432D20E9DBF9 CRC64;
     MSGKVHGGKG KSGAKDGGPL GSQSHSARAG LQFPVGRIKR YLKKNAAGKT RVGSKAAIYL
     TAVLEYLTAE VLELAGNAAK DLKVKRITPR HLQLAIRGDD ELDSLIRATI ASGGVLPHIN
     KALLLKVEKK THK
//

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