ID   H2AX_CICAR              Reviewed;         139 AA.
AC   O65759;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Histone H2AX;
GN   Name=HIS2A;
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Castellana; TISSUE=Etiolated epicotyl;
RA   Dopico B., Esteban R., Labrador E.;
RT   "cDNA sequence encoding an histone H2A from Cicer arietinum.";
RL   (er) Plant Gene Register PGR98-215(1998).
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-136 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC       from the PI3/PI4-kinase family.
CC   -!- PTM: Phosphorylated on Ser-136 (to form 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       Phosphorylation of Ser-136 in response to ionizing radiation is
CC       mediated by ATM while defects in DNA replication induce Ser-136
CC       phosphorylation subsequent to activation of ATR. Dephosphorylation of
CC       Ser-136 by PP2A is required for DNA DSB repair (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AJ006768; CAA07234.1; -; mRNA.
DR   RefSeq; NP_001296591.1; NM_001309662.1.
DR   AlphaFoldDB; O65759; -.
DR   SMR; O65759; -.
DR   STRING; 3827.XP_004494649.1; -.
DR   GeneID; 101514555; -.
DR   KEGG; cam:101514555; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   Proteomes; UP000087171; Chromosome Ca3.
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   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..139
FT                   /note="Histone H2AX"
FT                   /id="PRO_0000055219"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           136..137
FT                   /note="[ST]-Q motif"
FT   MOD_RES         136
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   139 AA;  14609 MW;  3920843DF1C9B05B CRC64;
     MSSTATTKGG RGKPKASKSV SRSSKAGLQF PVGRIARFLK AGKYAERVGA GAPVYLSAVL
     EYLAAEVLEL AGNAARDNKN NRIVPRHIQL AVRNDEELSK LLGSVTIANG GVLPNIHQTL
     LPKKVGKGKG EIGSASQEF