ID   H4_OLILU                Reviewed;         103 AA.
AC   P82888;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Histone H4;
OS   Olisthodiscus luteus (Marine phytoflagellate).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Olisthodiscophyceae;
OC   Olisthodiscaceae; Olisthodiscus.
OX   NCBI_TaxID=83000;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-103, ACETYLATION AT LYS-17, AND METHYLATION AT
RP   LYS-80.
RA   Rodrigues J.A., Spit A., Brandt W.F.;
RL   Submitted (DEC-2000) to UniProtKB.
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   AlphaFoldDB; P82888; -.
DR   SMR; P82888; -.
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   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   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Methylation; Nucleosome core; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158337"
FT   DNA_BIND        17..21
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|Ref.1"
FT   MOD_RES         80
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   103 AA;  11423 MW;  30FD5CFFBF5BD0DF CRC64;
     MSGRGKGGKG LGKGGAKRHR RVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYTEHARRK TVTAMDVVYA LKRQGRTLYG FGG