ID   H4_TETTS                Reviewed;         103 AA.
AC   P69152; P02311; P02312;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Histone H4;
GN   Name=HHF1; ORFNames=TTHERM_00498190;
GN   and
GN   Name=HHF2; ORFNames=TTHERM_00189170;
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHF1 AND HHF2).
RX   PubMed=6322129; DOI=10.1093/nar/12.4.1961;
RA   Bannon G.A., Bowen J.K., Yao M.-C., Gorovsky M.A.;
RT   "Tetrahymena H4 genes: structure, evolution and organization in macro- and
RT   micronuclei.";
RL   Nucleic Acids Res. 12:1961-1975(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHF1 AND HHF2).
RX   PubMed=3822803; DOI=10.1093/nar/15.1.141;
RA   Horowitz S., Bowen J.K., Bannon G.A., Gorovsky M.A.;
RT   "Unusual features of transcribed and translated regions of the histone H4
RT   gene family of Tetrahymena thermophila.";
RL   Nucleic Acids Res. 15:141-160(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF1 AND HHF2).
RC   STRAIN=SB210;
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-54 AND 85-97.
RX   PubMed=284382; DOI=10.1073/pnas.76.2.585;
RA   Glover C.V.C., Gorovsky M.A.;
RT   "Amino-acid sequence of Tetrahymena histone H4 differs from that of higher
RT   eukaryotes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:585-589(1979).
RN   [5]
RP   ACETYLATION AT LYS-8 AND LYS-16.
RX   PubMed=7862667; DOI=10.1073/pnas.92.4.1237;
RA   Sobel R.E., Cook R.G., Perry C.A., Annunziato A.T., Allis C.D.;
RT   "Conservation of deposition-related acetylation sites in newly synthesized
RT   histones H3 and H4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:1237-1241(1995).
RN   [6]
RP   INTERACTION WITH GCN5.
RX   PubMed=14661947; DOI=10.1021/bi035632n;
RA   Poux A.N., Marmorstein R.;
RT   "Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for
RT   histone and nonhistone substrates.";
RL   Biochemistry 42:14366-14374(2003).
RN   [7]
RP   ACETYLATION AT LYS-5; LYS-8; LYS-12 AND LYS-16, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17194708; DOI=10.1074/jbc.m607900200;
RA   Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA   Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT   "Organismal differences in post-translational modifications in histones H3
RT   and H4.";
RL   J. Biol. Chem. 282:7641-7655(2007).
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   -!- PTM: The N-terminus is not acetylated. {ECO:0000269|PubMed:17194708,
CC       ECO:0000269|PubMed:7862667}.
CC   -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR   EMBL; X00417; CAA25121.1; -; Genomic_DNA.
DR   EMBL; X04755; CAA28452.1; -; Genomic_DNA.
DR   EMBL; GG662693; EAR96348.1; -; Genomic_DNA.
DR   EMBL; GG662212; EAS07765.1; -; Genomic_DNA.
DR   PIR; A02650; A02650.
DR   PIR; A25875; A25875.
DR   RefSeq; XP_001016593.1; XM_001016593.3.
DR   RefSeq; XP_001028007.1; XM_001028007.3.
DR   AlphaFoldDB; P69152; -.
DR   SMR; P69152; -.
DR   STRING; 5911.EAR96348; -.
DR   iPTMnet; P69152; -.
DR   EnsemblProtists; EAR96348; EAR96348; TTHERM_00189170.
DR   EnsemblProtists; EAS07765; EAS07765; TTHERM_00498190.
DR   GeneID; 7823613; -.
DR   GeneID; 7845533; -.
DR   KEGG; tet:TTHERM_00189170; -.
DR   KEGG; tet:TTHERM_00498190; -.
DR   eggNOG; KOG3467; Eukaryota.
DR   HOGENOM; CLU_109117_2_3_1; -.
DR   InParanoid; P69152; -.
DR   OMA; QKEHING; -.
DR   OrthoDB; 1594208at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:284382"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158367"
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:17194708"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17194708,
FT                   ECO:0000269|PubMed:7862667"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17194708"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:17194708,
FT                   ECO:0000269|PubMed:7862667"
SQ   SEQUENCE   103 AA;  11328 MW;  253EA334E959BFC9 CRC64;
     MAGGKGGKGM GKVGAKRHSR KSNKASIEGI TKPAIRRLAR RGGVKRISSF IYDDSRQVLK
     SFLENVVRDA VTYTEHARRK TVTAMDVVYA LKRQGRTLYG FGG