H33_DROHY
ID H33_DROHY Reviewed; 136 AA.
AC P84250; P06351; P33155; Q9V3W4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Histone H3.3;
DE AltName: Full=H3.A/B;
GN Name=His3.3A;
GN and
GN Name=His3.3B;
OS Drosophila hydei (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7224;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3.3A AND HIS3.3B).
RC STRAIN=Tuebingen;
RX PubMed=7557364; DOI=10.1139/g95-075;
RA Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., Hennig W.;
RT "Structure and expression of histone H3.3 genes in Drosophila melanogaster
RT and Drosophila hydei.";
RL Genome 38:586-600(1995).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes and is specifically enriched in
CC modifications associated with active chromatin. Constitutes the
CC predominant form of histone H3 in non-dividing cells and is
CC incorporated into chromatin independently of DNA synthesis. Deposited
CC at sites of nucleosomal displacement throughout transcribed genes,
CC suggesting that it represents an epigenetic imprint of
CC transcriptionally active chromatin. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC 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 -!- PTM: Phosphorylation at Ser-11 by aurB/ial or JIL-1 is crucial for
CC chromosome condensation and cell-cycle progression during mitosis and
CC meiosis. Phosphorylation at Ser-11 is enriched on male X chromosome
CC compared to the autosome (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylated on
CC Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119'
CC is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is
CC enriched on male X chromosome compared to the autosome (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Methylation at Lys-5 or Lys-80 is generally associated with active
CC chromatin. Methylation at Lys-80 by gpp occurs at low levels in
CC specific developmental stages and tissues undergoing active cell
CC division, and at highest levels in epidermal cells undergoing
CC differentiation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This histone is the predominant form in non-dividing
CC cells.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; X81206; CAA57078.1; -; Genomic_DNA.
DR EMBL; X81208; CAA57081.1; -; Genomic_DNA.
DR PIR; S61218; S61218.
DR AlphaFoldDB; P84250; -.
DR SMR; P84250; -.
DR FlyBase; FBgn0014721; Dhyd\His3.3A.
DR FlyBase; FBgn0014722; Dhyd\His3.3B.
DR OMA; SDCERRK; -.
DR OrthoDB; 1564596at2759; -.
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; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000221303"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
