H2AZ_PICGU
ID H2AZ_PICGU Reviewed; 133 AA.
AC A5DQL2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Histone H2A.Z;
GN Name=HTZ1; ORFNames=PGUG_05563;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 once deposited into chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; CH408161; EDK41465.1; -; Genomic_DNA.
DR RefSeq; XP_001482543.1; XM_001482493.1.
DR AlphaFoldDB; A5DQL2; -.
DR SMR; A5DQL2; -.
DR STRING; 4929.XP_001482543.1; -.
DR EnsemblFungi; EDK41465; EDK41465; PGUG_05563.
DR GeneID; 5123994; -.
DR KEGG; pgu:PGUG_05563; -.
DR VEuPathDB; FungiDB:PGUG_05563; -.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_1_1; -.
DR InParanoid; A5DQL2; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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 PANTHER; PTHR23430; PTHR23430; 1.
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;
KW Acetylation; Chromosome; DNA-binding; Nucleosome core; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..133
FT /note="Histone H2A.Z"
FT /id="PRO_0000297728"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 133 AA; 14428 MW; B9643ED3D9F69129 CRC64;
MSGKGKVHGG KGKSSDSAKA STSHSARAGL QFPVGRIKRY LKRSAQNKVR VGSKSAIYLT
AVLEYLTAEV LELAGNAAKD LKVKRITPRH LQLAIRGDEE LDNLIKATIA YGGVLPHINK
ALLLKVEKKK QQK
