H2A1_SOLLC
ID H2A1_SOLLC Reviewed; 146 AA.
AC P25469;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Histone H2A.1;
DE AltName: Full=LeH2A-1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. UC82B;
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).
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 meristematic tissues, in cells
CC of the root pericycle and in shoot cortical cells undergoing
CC endoduplication of their DNA. {ECO:0000269|PubMed:1841722}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit development, showing a
CC maximum at 4 to 10 days postanthesis. {ECO:0000269|PubMed:1841722}.
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 PIR; JQ1182; JQ1182.
DR RefSeq; NP_001296309.1; NM_001309380.1.
DR AlphaFoldDB; P25469; -.
DR SMR; P25469; -.
DR STRING; 4081.Solyc01g099410.2.1; -.
DR PaxDb; P25469; -.
DR PRIDE; P25469; -.
DR EnsemblPlants; Solyc01g099410.3.1; Solyc01g099410.3.1; Solyc01g099410.3.
DR GeneID; 101250163; -.
DR Gramene; Solyc01g099410.3.1; Solyc01g099410.3.1; Solyc01g099410.3.
DR KEGG; sly:101250163; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_1_1_1; -.
DR InParanoid; P25469; -.
DR OMA; ELMLGCV; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P25469; -.
DR Proteomes; UP000004994; Chromosome 1.
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 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Nucleosome core; Nucleus;
KW Reference proteome.
FT CHAIN 1..146
FT /note="Histone H2A.1"
FT /id="PRO_0000055248"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..145
FT /note="SPKK motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 15335 MW; 9281B9A5FE6AB773 CRC64;
MDATKTTKGA GGRKGGPRKK SVTKSIKAGL QFPVGRIGRY LKKGRYAQRV GSGAPIYLAA
VLEYLAAEVL ELAGNAARDN KKSRIIPRHV LLAVRNDEEL GKLLAGVTIA SGGVLPNINP
VLLPKKSAVA EEKSPKAKAG KSPKKA
