ID   H4_PSAMI                Reviewed;         103 AA.
AC   P62781; P02306; P18678;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Histone H4;
OS   Psammechinus miliaris (Green sea urchin) (Echinus miliaris).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Parechinidae;
OC   Psammechinus.
OX   NCBI_TaxID=7660;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7443547; DOI=10.1093/nar/8.5.957;
RA   Busslinger M., Portmann R., Irminger J.C., Birnstiel M.L.;
RT   "Ubiquitous and gene-specific regulatory 5' sequences in a sea urchin
RT   histone DNA clone coding for histone protein variants.";
RL   Nucleic Acids Res. 8:957-977(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9032246; DOI=10.1128/mcb.17.3.1189;
RA   Mandl B., Brandt W.F., Superti-Furga G., Graninger P.G., Birnstiel M.L.,
RA   Busslinger M.;
RT   "The five cleavage-stage (CS) histones of the sea urchin are encoded by a
RT   maternally expressed family of replacement histone genes: functional
RT   equivalence of the CS H1 and frog H1M (B4) proteins.";
RL   Mol. Cell. Biol. 17:1189-1200(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, AND METHYLATION
RP   AT LYS-21.
RX   PubMed=1278426; DOI=10.1016/0014-5793(76)80485-1;
RA   Wouters-Tyrou D., Sautiere P., Biserte G.;
RT   "Covalent structure of the sea urchin histone H4.";
RL   FEBS Lett. 65:225-228(1976).
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; X01343; CAA25630.1; -; Genomic_DNA.
DR   EMBL; M10556; AAA30024.1; -; Genomic_DNA.
DR   EMBL; U84117; AAB48834.1; -; mRNA.
DR   PIR; D93719; HSUR4.
DR   AlphaFoldDB; P62781; -.
DR   SMR; P62781; -.
DR   iPTMnet; P62781; -.
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|PubMed:1278426"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158352"
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:0000269|PubMed:1278426"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:1278426"
FT   MOD_RES         21
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:1278426"
SQ   SEQUENCE   103 AA;  11369 MW;  A9E5DFD3F8AF04FF CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYCEHAKRK TVTAMDVVYA LKRQGRTLYG FGG