H33_TETTS
ID H33_TETTS Reviewed; 136 AA.
AC P41353; Q22RH0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histone H3.3;
DE AltName: Full=Minor histone H3 variant;
DE AltName: Full=hv2;
GN Name=HHT3; ORFNames=TTHERM_00016170;
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.
RX PubMed=8121802; DOI=10.1093/nar/22.2.180;
RA Thatcher T.H., MacGaffey J., Bowen J.K., Horowitz S., Shapiro D.L.,
RA Gorovsky M.A.;
RT "Independent evolutionary origin of histone H3.3-like variants of animals
RT and Tetrahymena.";
RL Nucleic Acids Res. 22:180-186(1994).
RN [2]
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 [3]
RP ACETYLATION.
RC STRAIN=B;
RX PubMed=7061439; DOI=10.1016/s0021-9258(18)34965-2;
RA Vavra K.J., Allis C.D., Gorovsky M.A.;
RT "Regulation of histone acetylation in Tetrahymena macro- and micronuclei.";
RL J. Biol. Chem. 257:2591-2598(1982).
RN [4]
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 H3.4. H3.3 deposition
CC into chromatin is mainly transcription-associated and DNA replication-
CC independent, but it can also enter a replication-coupled pathway.
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: In contrast to major H3, constitutively expressed in both
CC growing and non-growing, starved cells. {ECO:0000269|PubMed:16908532}.
CC -!- PTM: Acetylated. Acetylation occurs almost exclusively in the MAC.
CC {ECO:0000269|PubMed:7061439}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; M87305; AAC37188.1; -; Unassigned_DNA.
DR EMBL; GG662845; EAR88152.1; -; Genomic_DNA.
DR PIR; S41501; S41501.
DR RefSeq; XP_001008397.1; XM_001008397.3.
DR AlphaFoldDB; P41353; -.
DR SMR; P41353; -.
DR STRING; 5911.EAR88152; -.
DR EnsemblProtists; EAR88152; EAR88152; TTHERM_00016170.
DR GeneID; 7826846; -.
DR KEGG; tet:TTHERM_00016170; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P41353; -.
DR OMA; ASHPKKN; -.
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 1: Evidence at protein level;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000221351"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 136 AA; 15483 MW; 204C641E7C4A6071 CRC64;
MARTKQTARK STGVKAPRKQ LATKAARKSA PVSGGVKKPH KFRPGTVALR EIRKYQKTTD
LLIRKLPFQR LVRDIAMEMK SDIRFQSQAI LALQEAAEAY LVGLFEDTNL CAIHARRVTI
MTKDLHLARR IRGERF