ID   H2A3_WHEAT              Reviewed;         151 AA.
AC   P02277;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Histone H2A.2.2;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   TISSUE=Germ;
RX   PubMed=3371346; DOI=10.1111/j.1432-1033.1988.tb14035.x;
RA   Rodrigues J.A., Brandt W.F., von Holt C.;
RT   "The primary structure of the histone H2A(2) type from wheat germ. A core
RT   histone type with both, N-terminal and C-terminal extensions.";
RL   Eur. J. Biochem. 173:555-560(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-37.
RC   TISSUE=Germ;
RX   PubMed=454665; DOI=10.1016/0005-2795(79)90127-2;
RA   Rodrigues J.A., Brandt W.F., von Holt C.;
RT   "Plant histone 2 from wheat germ, a family of histone H2a variants. Partial
RT   amino acid sequences.";
RL   Biochim. Biophys. Acta 578:196-206(1979).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=16667585; DOI=10.1104/pp.93.3.1241;
RA   Green G.R., Gustavsen L.C., Poccia D.L.;
RT   "Phosphorylation of plant H2A histones.";
RL   Plant Physiol. 93:1241-1245(1990).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DOMAIN: Contains 2 SPKK motifs which may interact with the minor groove
CC       of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA
CC       binding. This motif is reiterated in both termini of histone H1 and in
CC       the N-terminus of sea urchin histones H2B, but its presence in the C-
CC       terminus seems to be unique to plant H2A.
CC   -!- PTM: Phosphorylated within its C-terminal part, probably at the SPKK
CC       motifs. {ECO:0000269|PubMed:16667585}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   PIR; A02604; HSWT93.
DR   AlphaFoldDB; P02277; -.
DR   SMR; P02277; -.
DR   STRING; 4565.Traes_1AS_6AA4114A2.1; -.
DR   iPTMnet; P02277; -.
DR   PRIDE; P02277; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P02277; baseline.
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   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   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..151
FT                   /note="Histone H2A.2.2"
FT                   /id="PRO_0000055293"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           140..143
FT                   /note="SPKK motif 1"
FT   MOTIF           147..150
FT                   /note="SPKK motif 2"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:3371346"
SQ   SEQUENCE   151 AA;  16070 MW;  20293977E00029C4 CRC64;
     MDASKLKKVA GKKFGGPRKK SVTRSIKAGL QFPVGRIGRY LKKGRYAQRV GSGAPVYLAA
     VLEYLAAEVL ELAGNAAKDN KKSRIVPRHL LLAVRNDQEL GRLLAGVTIA HGGVIPNINP
     VLLPKKAAEK AEKAGTKAKS PKKATKSPKK A