ID   H2A_PETCR               Reviewed;         149 AA.
AC   P19177;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Histone H2A;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2216791; DOI=10.1093/nar/18.19.5897;
RA   Spiker S., Weisshaar B., da Costa e Silva O., Halbrock K.;
RT   "Sequence of a histone H2A cDNA from parsley.";
RL   Nucleic Acids Res. 18:5897-5897(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   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; X53831; CAA37828.1; -; mRNA.
DR   PIR; S11498; S11498.
DR   AlphaFoldDB; P19177; -.
DR   SMR; P19177; -.
DR   PRIDE; P19177; -.
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.
FT   CHAIN           1..149
FT                   /note="Histone H2A"
FT                   /id="PRO_0000055266"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           138..141
FT                   /note="SPKK motif 1"
FT   MOTIF           145..148
FT                   /note="SPKK motif 2"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  15833 MW;  054289F69CA48FA0 CRC64;
     METAGKAKKG FGGRKGGPRK KSVTRSVKAG LQFPVGRIGR YLKKGRYAQR VGTGAPVYLA
     AVLEYLAAEV LELAGNAARD NKKTRIIPRH LLLAVRNDEE LGKLLAGVTF AHGGVLPNIN
     PVLLPKKTAE KAAKEPKSPS KAGKSPKKA