ID   H2A1_PEA                Reviewed;         150 AA.
AC   P25470;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Histone H2A.1;
OS   Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Alaska;
RX   PubMed=1841722; DOI=10.2307/3869247;
RA   Koning A.J., Tanimoto E.Y., Kiehne K., Rost T., Comai L.;
RT   "Cell-specific expression of plant histone H2A genes.";
RL   Plant Cell 3:657-665(1991).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12232021; DOI=10.1104/pp.103.4.1291;
RA   Tanimoto E.Y., Rost T.L., Comai L.;
RT   "DNA replication-dependent histone H2A mRNA expression in pea root tips.";
RL   Plant Physiol. 103:1291-1297(1993).
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   -!- TISSUE SPECIFICITY: High expression in root meristematic tissues,
CC       moderate in whole shoot and very low in mature leaves.
CC       {ECO:0000269|PubMed:12232021, ECO:0000269|PubMed:1841722}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the late G1 phase and the major
CC       part of the S phase. {ECO:0000269|PubMed:12232021,
CC       ECO:0000269|PubMed:1841722}.
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   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; M64838; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; JQ1183; JQ1183.
DR   AlphaFoldDB; P25470; -.
DR   SMR; P25470; -.
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   Acetylation; Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   CHAIN           1..150
FT                   /note="Histone H2A.1"
FT                   /id="PRO_0000055263"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           139..142
FT                   /note="SPKK motif 1"
FT   MOTIF           146..149
FT                   /note="SPKK motif 2"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  15880 MW;  0F72BAFE5265F230 CRC64;
     MDASTKTKKG AGGRKGGGPR KKSVTRSVRA GLQFPVGRVG RFLKKGRYAQ RVGTGAPVYL
     AAVLEYLAAE VLELAGNAAR DNKKNRISPR HLLLAVRNDE ELGKLLAGVT IAYGGVLPNI
     NPVLLPKRKE NAAASTPKSP SKAKKSPKKA