ID   H4_APLCA                Reviewed;         103 AA.
AC   Q8MTV8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Histone H4;
GN   Name=His.H4;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12437922; DOI=10.1016/s0092-8674(02)01074-7;
RA   Guan Z., Giustetto M., Lomvardas S., Kim J.H., Miniaci M.C., Schwartz J.H.,
RA   Thanos D., Kandel E.R.;
RT   "Integration of long-term-memory-related synaptic plasticity involves
RT   bidirectional regulation of gene expression and chromatin structure.";
RL   Cell 111:483-493(2002).
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; AY064471; AAL54860.1; -; Genomic_DNA.
DR   RefSeq; NP_001248346.1; NM_001261417.1.
DR   AlphaFoldDB; Q8MTV8; -.
DR   SMR; Q8MTV8; -.
DR   GeneID; 100885793; -.
DR   CTD; 100885793; -.
DR   OrthoDB; 1594208at2759; -.
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; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW   Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158277"
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:0000250"
FT   MOD_RES         21
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   103 AA;  11314 MW;  B9F4DED3F8B97598 CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYTEHAKCK TVTAMDVVYA LKRQGRTLYG FGG