ID   H2AXA_ORYSI             Reviewed;         137 AA.
AC   A2XLI0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable histone H2AXa;
GN   ORFNames=OsI_012923;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC       limiting DNA accessibility to the cellular machineries which require
CC       DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. Required for checkpoint-mediated arrest of cell
CC       cycle progression in response to low doses of ionizing radiation and
CC       for efficient repair of DNA double strand breaks (DSBs) specifically
CC       when modified by C-terminal phosphorylation (By similarity).
CC       {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. Interacts with numerous proteins required for DNA damage signaling
CC       and repair when phosphorylated on Ser-134 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC       from the PI3/PI4-kinase family.
CC   -!- PTM: Phosphorylated to form H2AXS139ph (gamma-H2AX) in response to DNA
CC       double strand breaks (DSBs) generated by exogenous genotoxic agents and
CC       by stalled replication forks, and may also occur during meiotic
CC       recombination events. Phosphorylation can extend up to several thousand
CC       nucleosomes from the actual site of the DSB and may mark the
CC       surrounding chromatin for recruitment of proteins required for DNA
CC       damage signaling and repair. Widespread phosphorylation may also serve
CC       to amplify the damage signal or aid repair of persistent lesions.
CC       H2AXS139ph in response to ionizing radiation is mediated by ATM while
CC       defects in DNA replication induce H2AXS139ph subsequent to activation
CC       of ATR. Dephosphorylation of H2AXS139ph by PP2A is required for DNA DSB
CC       repair (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: H2AXS139ph =
CC       phosphorylated Ser-134. {ECO:0000305}.
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DR   EMBL; CM000128; EAY91690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XLI0; -.
DR   SMR; A2XLI0; -.
DR   STRING; 39946.A2XLI0; -.
DR   iPTMnet; A2XLI0; -.
DR   EnsemblPlants; BGIOSGA013476-TA; BGIOSGA013476-PA; BGIOSGA013476.
DR   Gramene; BGIOSGA013476-TA; BGIOSGA013476-PA; BGIOSGA013476.
DR   HOGENOM; CLU_062828_3_0_1; -.
DR   OMA; MPNIHQT; -.
DR   Proteomes; UP000007015; Chromosome 3.
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   Chromosome; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..137
FT                   /note="Probable histone H2AXa"
FT                   /id="PRO_0000296127"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           134..135
FT                   /note="[ST]-Q motif"
FT   MOD_RES         134
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   137 AA;  14271 MW;  933F5005D19436A3 CRC64;
     MSSSQGGGGR GKAKTTKAVS RSSKAGLQFP VGRIARYLKA GKYAERVGAG APVYLSAVLE
     YLAAEVLELA GNAARDNKKN RIVPRHIQLA VRNDEELSRL LGTVTIAAGG VLPNIQQVLL
     PKKGGGKGDI GSASQEF