ID   H2B3_SOLLC              Reviewed;         137 AA.
AC   O65819;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histone H2B.3;
DE   AltName: Full=LeH2B-3;
DE   Flags: Fragment;
GN   Name=H2B-3;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Moneymaker; TISSUE=Anther;
RX   PubMed=10344194; DOI=10.1023/a:1006157718263;
RA   van den Heuvel K.J.P.T., van Esch R.J., Barendse G.W.M., Wullems G.J.;
RT   "Isolation and molecular characterization of gibberellin-regulated H1 and
RT   H2B histone cDNAs in the leaf of the gibberellin-deficient tomato.";
RL   Plant Mol. Biol. 39:883-890(1999).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest level in shoots, fruits and
CC       young flower buds, including petals, anthers and ovules.
CC       {ECO:0000269|PubMed:10344194}.
CC   -!- INDUCTION: By gibberellins GA1, GA3, GA4 and GA9.
CC       {ECO:0000269|PubMed:10344194}.
CC   -!- PTM: Can be acetylated to formH2BK33ac and H2BK34ac. {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated to form H2BK143ub1; may give a specific tag for
CC       epigenetic transcriptional activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2BK33ac =
CC       acetylated Lys-27; H2BK34ac = acetylated Lys-28; H2BK143ub1 =
CC       monoubiquitinated Lys-133. {ECO:0000305}.
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DR   EMBL; AJ224932; CAA12231.1; -; mRNA.
DR   PIR; T06390; T06390.
DR   AlphaFoldDB; O65819; -.
DR   SMR; O65819; -.
DR   STRING; 4081.Solyc05g055440.1.1; -.
DR   PaxDb; O65819; -.
DR   PRIDE; O65819; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   InParanoid; O65819; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; O65819; baseline and differential.
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   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           <1..137
FT                   /note="Histone H2B.3"
FT                   /id="PRO_0000240451"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        133
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  15045 MW;  6DB1D9356CC06B6F CRC64;
     KPAEKKPAEK TPVAEKAPAE KKPKAGKKLP KDAAAGDKKK KRSKKAVETY KIYIFKVLKQ
     VHPDIGISSK AMGIMNSFIN DIFEKLAQEA SRLARYNKKP TITSREIQTA VRLVLPGELA
     KHAVSEGTKA VTKFTSS