ID   H4_DROHY                Reviewed;         103 AA.
AC   P84042; P02307; Q9VFH7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Histone H4;
GN   Name=His4; Synonyms=H4;
GN   and
GN   Name=His4r; Synonyms=H4r;
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] (HIS4).
RX   PubMed=2109309; DOI=10.1093/nar/18.6.1573;
RA   Kremer H., Hennig W.;
RT   "Isolation and characterization of a Drosophila hydei histone DNA repeat
RT   unit.";
RL   Nucleic Acids Res. 18:1573-1580(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS4).
RX   PubMed=8487638; DOI=10.1093/oxfordjournals.molbev.a040011;
RA   Fitch D.H., Strausbaugh L.D.;
RT   "Low codon bias and high rates of synonymous substitution in Drosophila
RT   hydei and D. melanogaster histone genes.";
RL   Mol. Biol. Evol. 10:397-413(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HIS4R).
RC   STRAIN=Tuebingen;
RX   PubMed=8690091; DOI=10.1016/0014-5793(96)00551-0;
RA   Akhmanova A., Miedema K., Hennig W.;
RT   "Identification and characterization of the Drosophila histone H4
RT   replacement gene.";
RL   FEBS Lett. 388:219-222(1996).
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   -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR   EMBL; X17072; CAA34920.1; -; Genomic_DNA.
DR   EMBL; X52576; CAA36806.1; -; Genomic_DNA.
DR   EMBL; X97436; CAA66066.1; -; mRNA.
DR   PIR; S09656; S09656.
DR   AlphaFoldDB; P84042; -.
DR   SMR; P84042; -.
DR   FlyBase; FBgn0012378; Dhyd\His4.
DR   FlyBase; FBgn0016205; Dhyd\His4r.
DR   OrthoDB; 1594208at2759; -.
DR   GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Nucleosome core; Nucleus;
KW   Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158303"
FT   DNA_BIND        17..21
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         32
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         80
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         81
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         83
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
FT   MOD_RES         92
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84040"
SQ   SEQUENCE   103 AA;  11381 MW;  DF3EB26393BD208C CRC64;
     MTGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG