ID   H4_MEDSA                Reviewed;          25 AA.
AC   P62789; P02308; P59258;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Histone H4;
DE   Flags: Fragment;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-25, AND ACETYLATION AT SER-2; LYS-6; LYS-9; LYS-13;
RP   LYS-17 AND LYS-21.
RC   STRAIN=cv. R4;
RX   PubMed=1627562; DOI=10.1021/bi00142a006;
RA   Waterborg J.H.;
RT   "Identification of five sites of acetylation in alfalfa histone H4.";
RL   Biochemistry 31:6211-6219(1992).
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. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR   PIR; B43295; B43295.
DR   AlphaFoldDB; P62789; -.
DR   iPTMnet; P62789; -.
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; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   PRINTS; PR00623; HISTONEH4.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Nucleosome core; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   CHAIN           2..>25
FT                   /note="Histone H4"
FT                   /id="PRO_0000158327"
FT   DNA_BIND        17..21
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1627562"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2607 MW;  E5BD770849703A8A CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRD