ID   H34_TETTS               Reviewed;         136 AA.
AC   Q22RG7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Histone H3.4;
DE   AltName: Full=Minor histone H3 variant;
GN   Name=HHT4; ORFNames=TTHERM_00016200;
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 [LARGE SCALE GENOMIC DNA].
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   [2]
RP   FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=B2086, and CU428;
RX   PubMed=16908532; DOI=10.1128/mcb.01139-06;
RA   Cui B., Liu Y., Gorovsky M.A.;
RT   "Deposition and function of histone H3 variants in Tetrahymena
RT   thermophila.";
RL   Mol. Cell. Biol. 26:7719-7730(2006).
CC   -!- FUNCTION: Macronuclear replacement variant which replaces conventional
CC       H3 in a subset of nucleosomes. Nucleosomes wrap and compact DNA into
CC       chromatin, limiting DNA accessibility to the cellular machineries which
CC       require DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. Functions redundantly to H3.3. H3.4 deposition
CC       is mainly transcription-associated, DNA replication-independent.
CC       Although not essential for vegetative growth, minor H3 variants are
CC       required for producing viable conjugation progeny by affecting late
CC       developmental stages of conjugation. {ECO:0000269|PubMed:16908532}.
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:0000269|PubMed:16908532}. Chromosome
CC       {ECO:0000269|PubMed:16908532}. Note=Localizes mainly to the large,
CC       transcriptionally active, somatic macronucleus (MAC) and only faintly
CC       to the small, transcriptionally inert, germ line micronucleus (MIC).
CC   -!- INDUCTION: Up-regulated in the absence of H3.3.
CC       {ECO:0000269|PubMed:16908532}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; GG662845; EAR88155.1; -; Genomic_DNA.
DR   RefSeq; XP_001008400.1; XM_001008400.1.
DR   AlphaFoldDB; Q22RG7; -.
DR   SMR; Q22RG7; -.
DR   STRING; 5911.EAR88155; -.
DR   EnsemblProtists; EAR88155; EAR88155; TTHERM_00016200.
DR   GeneID; 7826848; -.
DR   KEGG; tet:TTHERM_00016200; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   InParanoid; Q22RG7; -.
DR   OMA; SDCERRK; -.
DR   OrthoDB; 1564596at2759; -.
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   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   CHAIN           1..136
FT                   /note="Histone H3.4"
FT                   /id="PRO_0000385012"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  15525 MW;  E975B88C127FD240 CRC64;
     MARTKQTARK STSIKAPRKQ LAAKAARKSA PISGGIKKPH KFRPGTVALR EIRKYQKTTD
     LLIRKLPFQR LVRDIAMEMK SDIRFQSQAI LALQEAAEAY LVGLFEDTNL CAIHARRVTI
     MTKDLHLARR IRGERF