H31_TETTH
ID H31_TETTH Reviewed; 136 AA.
AC P69150; P15511; P92147; Q95047;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Histone H3;
DE AltName: Full=H3S;
DE AltName: Full=Histone H3-I/H3-II;
DE AltName: Full=Major histone H3;
DE Contains:
DE RecName: Full=H3F;
GN Name=HHT1; ORFNames=TTHERM_00570560;
GN and
GN Name=HHT2; ORFNames=TTHERM_00189180;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE (HHT1 AND HHT2).
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 [GENOMIC DNA] OF 1-76 (HHT1 AND HHT2).
RX PubMed=3921962; DOI=10.1073/pnas.82.8.2452;
RA Horowitz S., Gorovsky M.A.;
RT "An unusual genetic code in nuclear genes of Tetrahymena.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2452-2455(1985).
RN [3]
RP PROTEIN SEQUENCE OF 2-39, AND METHYLATION AT LYS-5.
RX PubMed=10611321; DOI=10.1073/pnas.96.26.14967;
RA Strahl B.D., Ohba R., Cook R.G., Allis C.D.;
RT "Methylation of histone H3 at lysine 4 is highly conserved and correlates
RT with transcriptionally active nuclei in Tetrahymena.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14967-14972(1999).
RN [4]
RP PROTEIN SEQUENCE OF 2-22, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=6993010; DOI=10.1016/0092-8674(80)90234-2;
RA Allis C.D., Bowen J.K., Abraham G.N., Glover C.V.C., Gorovsky M.A.;
RT "Proteolytic processing of histone H3 in chromatin: a physiologically
RT regulated event in Tetrahymena micronuclei.";
RL Cell 20:55-64(1980).
RN [5]
RP PROTEIN SEQUENCE OF 8-32, PHOSPHORYLATION AT SER-11, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9636175; DOI=10.1073/pnas.95.13.7480;
RA Wei Y., Mizzen C.A., Cook R.G., Gorovsky M.A., Allis C.D.;
RT "Phosphorylation of histone H3 at serine 10 is correlated with chromosome
RT condensation during mitosis and meiosis in Tetrahymena.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7480-7484(1998).
RN [6]
RP ACETYLATION.
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 [7]
RP ACETYLATION AT LYS-10 AND LYS-15.
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 [8]
RP PHOSPHORYLATION AT SER-11, AND MUTAGENESIS OF SER-11.
RX PubMed=10199406; DOI=10.1016/s0092-8674(00)80718-7;
RA Wei Y., Yu L., Bowen J., Gorovsky M.A., Allis C.D.;
RT "Phosphorylation of histone H3 is required for proper chromosome
RT condensation and segregation.";
RL Cell 97:99-109(1999).
RN [9]
RP METHYLATION AT LYS-10, AND SUBCELLULAR LOCATION.
RX PubMed=12297044; DOI=10.1016/s0092-8674(02)00941-8;
RA Taverna S.D., Coyne R.S., Allis C.D.;
RT "Methylation of histone H3 at lysine 9 targets programmed DNA elimination
RT in Tetrahymena.";
RL Cell 110:701-711(2002).
RN [10]
RP INTERACTION WITH GCN5.
RX PubMed=14536085; DOI=10.1016/s1097-2765(03)00288-0;
RA Clements A., Poux A.N., Lo W.-S., Pillus L., Berger S.L., Marmorstein R.;
RT "Structural basis for histone and phosphohistone binding by the GCN5
RT histone acetyltransferase.";
RL Mol. Cell 12:461-473(2003).
RN [11]
RP FUNCTION, METHYLATION AT LYS-10, AND MUTAGENESIS OF LYS-10.
RX PubMed=14755052; DOI=10.1073/pnas.0305421101;
RA Liu Y., Mochizuki K., Gorovsky M.A.;
RT "Histone H3 lysine 9 methylation is required for DNA elimination in
RT developing macronuclei in Tetrahymena.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1679-1684(2004).
RN [12]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
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).
RN [13]
RP ACETYLATION AT LYS-37, AND METHYLATION AT LYS-37.
RX PubMed=17189264; DOI=10.1074/jbc.m607909200;
RA Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J.,
RA Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly conserved
RT histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [14]
RP ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37 AND
RP LYS-57, METHYLATION AT LYS-5; LYS-10; LYS-28; LYS-37; LYS-57 AND LYS-80,
RP AND IDENTIFICATION BY MASS 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. H3 is deposited into chromatin
CC exclusively through a DNA replication-coupled pathway that can be
CC associated with either DNA duplication or DNA repair synthesis during
CC meiotic homologous recombination. {ECO:0000269|PubMed:14755052,
CC 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. Interacts with GCN5, whereby H3S10ph increases histone-protein
CC interactions. Interacts with PDD1 and PDD3.
CC {ECO:0000269|PubMed:14536085}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to both the
CC large, transcriptionally active, somatic macronucleus (MAC) and the
CC small, transcriptionally inert, germ line micronucleus (MIC).
CC -!- INDUCTION: Highly expressed in growing cells, but only at low levels in
CC starved cells. {ECO:0000269|PubMed:16908532}.
CC -!- PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent
CC H3K14ac formation by GCN5. H3S10ph is only found in the mitotically
CC dividing MIC, but not in the amitotically dividing MAC. H3S10ph is
CC correlated with chromosome condensation during mitotic or meiotic
CC micronuclear divisions. {ECO:0000269|PubMed:10199406,
CC ECO:0000269|PubMed:9636175}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC H3K14ac formation by GCN5 is promoted by H3S10ph. H3K9acK14ac is the
CC preferred acetylated form of newly synthesized H3. Acetylation occurs
CC almost exclusively in the MAC. {ECO:0000269|PubMed:17189264,
CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7061439,
CC ECO:0000269|PubMed:7862667}.
CC -!- PTM: Methylated to form H3K4me. H3K4me is only found in the
CC transcriptionally active MAC. Methylated to form H3K9me in developing
CC MACs during conjugation, when genome-wide DNA elimination occurs. At
CC this stage, H3K9me specifically occurs on DNA sequences being
CC eliminated (IES), probably targeted by small scan RNAs (scnRNAs) bound
CC to IES, and is required for efficient IES elimination. H3K9me is
CC required for the interaction with the chromodomains of PDD1 and PDD3.
CC {ECO:0000269|PubMed:10611321, ECO:0000269|PubMed:12297044,
CC ECO:0000269|PubMed:14755052, ECO:0000269|PubMed:17189264,
CC ECO:0000269|PubMed:17194708}.
CC -!- PTM: The full-length protein H3S (slow migrating) is converted to H3F
CC (fast migrating) by proteolytic removal of the first 6 residues. H3F is
CC unique to MIC, and processing seems to occur regularly each generation
CC at a specific point in the cell cycle. {ECO:0000269|PubMed:6993010}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H3K4ac =
CC acetylated Lys-5; H3K4me1/2/3 = mono-, di- and trimethylated Lys-5;
CC H3K9ac = acetylated Lys-10; H3K9me3 = trimethylated Lys-10; H3S10ph =
CC phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K18ac =
CC acetylated Lys-19; H3K23ac = acetylated Lys-24; H3K27ac = acetylated
CC Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac =
CC acetylated Lys-37; H3K36me1/3/3 = mono-, di- and trimethylated Lys-37;
CC H3K56ac = acetylated Lys-57; H3K56me1 = monomethylated Lys-57; H3K79me1
CC = monomethylated Lys-80. {ECO:0000305}.
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DR EMBL; M87304; AAC37190.1; -; Unassigned_DNA.
DR EMBL; M87504; AAC37189.1; -; Unassigned_DNA.
DR EMBL; M11142; AAA30115.1; -; Genomic_DNA.
DR EMBL; M11143; AAA30116.1; -; Genomic_DNA.
DR PIR; S41499; S41499.
DR PIR; S42521; S42521.
DR PIR; S42522; S42522.
DR AlphaFoldDB; P69150; -.
DR SMR; P69150; -.
DR iPTMnet; P69150; -.
DR OMA; HIVMART; -.
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 Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10611321,
FT ECO:0000269|PubMed:6993010"
FT CHAIN 2..136
FT /note="Histone H3"
FT /id="PRO_0000221330"
FT CHAIN 8..136
FT /note="H3F"
FT /id="PRO_0000385010"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:10611321,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:10611321,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:10611321,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12297044,
FT ECO:0000269|PubMed:14755052, ECO:0000269|PubMed:17194708"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7862667"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10199406,
FT ECO:0000269|PubMed:9636175"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:7862667"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 57
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MUTAGEN 10
FT /note="K->Q: Reduces greatly IES elimination."
FT /evidence="ECO:0000269|PubMed:14755052"
FT MUTAGEN 11
FT /note="S->A: Causes abnormal chromosome condensation and
FT segregation in MIC nuclear divisions."
FT /evidence="ECO:0000269|PubMed:10199406"
FT CONFLICT 6
FT /note="Q -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="F -> S (in Ref. 2; AAA30115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15429 MW; 1358B0734220CF74 CRC64;
MARTKQTARK STGAKAPRKQ LASKAARKSA PATGGIKKPH RFRPGTVALR EIRKYQKSTD
LLIRKLPFQR LVRDIAHEFK AELRFQSSAV LALQEAAEAY LVGLFEDTNL CAIHARRVTI
MTKDMQLARR IRGERF
