ID   H2A2_PEA                Reviewed;         149 AA.
AC   P40281;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Histone H2A.2;
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].
RC   STRAIN=cv. Alaska;
RX   PubMed=7579177; DOI=10.1007/bf00043650;
RA   Devitt M.L., Stafstrom J.P.;
RT   "Cell cycle regulation during growth-dormancy cycles in pea axillary
RT   buds.";
RL   Plant Mol. Biol. 29:255-265(1995).
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 one SPKK motif which may interact with the minor
CC       groove of A/T-rich DNA sites. Phosphorylation of this motif may
CC       regulate DNA binding. This motif is reiterated in both termini of
CC       histone H1 and in the N-terminus of sea urchin histones H2B, but its
CC       presence in the C-terminus seems to be unique to plant H2A.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; U10041; AAA86947.1; -; mRNA.
DR   PIR; S60474; S60474.
DR   AlphaFoldDB; P40281; -.
DR   SMR; P40281; -.
DR   PRIDE; P40281; -.
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..149
FT                   /note="Histone H2A.2"
FT                   /id="PRO_0000055264"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           138..141
FT                   /note="SPKK motif"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   149 AA;  15704 MW;  5ED29866408BCE05 CRC64;
     MDASTKVKKG AGGRKGGGPR KKAVTRSVRA GLQFPVGRIG RFLKKGRYAQ RVGTGAPVYL
     AAVLEYLAAE VLELAGNAAR DNKKNRISPR HLLLAVRNDV ELGKLLAGVT IAYGGVLPNI
     NPVLLPKRTE SAASAPKSPS KAKKTPKKA