ID   H2AZ_DICDI              Reviewed;         143 AA.
AC   Q54LA5;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Histone H2A.z;
GN   Name=H2AZ; ORFNames=DDB_G0286747;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Core component of nucleosome which plays a central role in
CC       DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC       into chromatin, limiting DNA accessibility to the cellular machineries
CC       which require DNA as a template. Histones thereby play a central role
CC       in transcription regulation, DNA repair, DNA replication and
CC       chromosomal stability. DNA accessibility is regulated via a complex set
CC       of post-translational modifications of histones, also called histone
CC       code, and nucleosome remodeling (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 DNA
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AAFI02000089; EAL64129.1; -; Genomic_DNA.
DR   RefSeq; XP_637656.1; XM_632564.1.
DR   AlphaFoldDB; Q54LA5; -.
DR   SMR; Q54LA5; -.
DR   STRING; 44689.DDB0216302; -.
DR   PaxDb; Q54LA5; -.
DR   EnsemblProtists; EAL64129; EAL64129; DDB_G0286747.
DR   GeneID; 8625796; -.
DR   KEGG; ddi:DDB_G0286747; -.
DR   dictyBase; DDB_G0286747; H2AZ.
DR   eggNOG; KOG1757; Eukaryota.
DR   HOGENOM; CLU_062828_2_2_1; -.
DR   InParanoid; Q54LA5; -.
DR   OMA; WHCQAGG; -.
DR   PhylomeDB; Q54LA5; -.
DR   Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-DDI-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q54LA5; -.
DR   Proteomes; UP000002195; Chromosome 4.
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; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; PTHR23430; 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   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..143
FT                   /note="Histone H2A.z"
FT                   /id="PRO_0000389154"
SQ   SEQUENCE   143 AA;  16114 MW;  DB7770E8CAF43729 CRC64;
     MTESETTSKK VNKRVKPVPK STKAGLIFPV GRIHRMLKNK VPLKRVSILS SVYLAAILEY
     LASEVLELTI SQVSIQSKEY HNVRRISPRH LLLAIKTDEE LDNLIRVSTT IAGGGVIPYI
     HEVLKKVEQK PTHPQQKQTI KSI