ID   H33_HORVU               Reviewed;          80 AA.
AC   P06353;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histone H3.3;
DE   Flags: Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chojecki J.;
RT   "Identification and characterization of a cDNA clone for histone H3 in
RT   barley.";
RL   Carlsberg Res. Commun. 51:211-217(1986).
CC   -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC       range of nucleosomes in active genes. Constitutes the predominant form
CC       of histone H3 in non-dividing cells and is incorporated into chromatin
CC       independently of DNA synthesis. Deposited at sites of nucleosomal
CC       displacement throughout transcribed genes, suggesting that it
CC       represents an epigenetic imprint of transcriptionally active chromatin.
CC       Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC       accessibility to the cellular machineries which require DNA as a
CC       template. Histones thereby play a central role in transcription
CC       regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and nucleosome
CC       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   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; M34928; AAA32965.1; -; mRNA.
DR   PIR; A02632; HSBH3.
DR   AlphaFoldDB; P06353; -.
DR   SMR; P06353; -.
DR   PRIDE; P06353; -.
DR   EnsemblPlants; HORVU.MOREX.r2.2HG0142380.1.mrna1; HORVU.MOREX.r2.2HG0142380.1.mrna1; HORVU.MOREX.r2.2HG0142380.1.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0548720.1; HORVU.MOREX.r2.7HG0548720.1.CDS.1; HORVU.MOREX.r2.7HG0548720.
DR   Gramene; HORVU.MOREX.r2.2HG0142380.1.mrna1; HORVU.MOREX.r2.2HG0142380.1.mrna1; HORVU.MOREX.r2.2HG0142380.1.
DR   Gramene; HORVU.MOREX.r2.7HG0548720.1; HORVU.MOREX.r2.7HG0548720.1.CDS.1; HORVU.MOREX.r2.7HG0548720.
DR   ExpressionAtlas; P06353; 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; 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   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   CHAIN           <1..80
FT                   /note="Histone H3.3"
FT                   /id="PRO_0000221279"
FT   NON_TER         1
SQ   SEQUENCE   80 AA;  9233 MW;  68DB3E33EF04CE7B CRC64;
     KSTELLIRKL PFQRLVREIA QDFKTDLRFQ SHAVLALQEA AEAYLVGLFE DTNLCAIHAK
     RVTIMPKDIQ LARRIRGERA