ID   H41_TETPY               Reviewed;         103 AA.
AC   P02310; Q27846;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histone H4, major;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC   STRAIN=GL;
RX   PubMed=2129549; DOI=10.1093/nar/18.2.323;
RA   Brunk C.F., Sadler L.A.;
RT   "Characterization of the promoter region of Tetrahymena genes.";
RL   Nucleic Acids Res. 18:323-329(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-103, AND ACETYLATION AT LYS-5; LYS-8; LYS-12 AND
RP   LYS-16.
RX   PubMed=6441804;
RA   Hayashi H., Nomoto M., Iwai K.;
RT   "Tetrahymena histone H4. Complete amino acid sequences of two variants.";
RL   J. Biochem. 96:1449-1456(1984).
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; X17141; CAA35017.1; -; Genomic_DNA.
DR   PIR; A02648; HSTE41.
DR   PIR; S10294; S10294.
DR   AlphaFoldDB; P02310; -.
DR   SMR; P02310; -.
DR   iPTMnet; P02310; -.
DR   PRIDE; P02310; -.
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   Nucleosome core; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6441804"
FT   CHAIN           2..103
FT                   /note="Histone H4, major"
FT                   /id="PRO_0000158365"
FT   DNA_BIND        16..21
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:6441804"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:6441804"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:6441804"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:6441804"
SQ   SEQUENCE   103 AA;  11328 MW;  D4B7B1830BFCF82B CRC64;
     MAGGKGGKGM GKVGAKRHSK RSNKASIEGI TKPAIRRLAR RGGVKRISSF IYDDSRQVLK
     SFLENVVRDA VTYTEHARRK TVTAMDVVYA LKRQGRTLYG FGG