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Histone H3 (H3S) (Histone H3-I/H3-II) (Major histone H3) [Cleaved into: H3F]

 H31_TETTH               Reviewed;         136 AA.
P69150; P15511; P92147; Q95047;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 61.
RecName: Full=Histone H3;
AltName: Full=H3S;
AltName: Full=Histone H3-I/H3-II;
AltName: Full=Major histone H3;
Contains:
RecName: Full=H3F;
Name=HHT1; ORFNames=TTHERM_00570560;
and
Name=HHT2; ORFNames=TTHERM_00189180;
Tetrahymena thermophila.
Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
Tetrahymena.
NCBI_TaxID=5911;
[1]
NUCLEOTIDE SEQUENCE (HHT1 AND HHT2).
PubMed=8121802; DOI=10.1093/nar/22.2.180;
Thatcher T.H., MacGaffey J., Bowen J.K., Horowitz S., Shapiro D.L.,
Gorovsky M.A.;
"Independent evolutionary origin of histone H3.3-like variants of
animals and Tetrahymena.";
Nucleic Acids Res. 22:180-186(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76 (HHT1 AND HHT2).
PubMed=3921962; DOI=10.1073/pnas.82.8.2452;
Horowitz S., Gorovsky M.A.;
"An unusual genetic code in nuclear genes of Tetrahymena.";
Proc. Natl. Acad. Sci. U.S.A. 82:2452-2455(1985).
[3]
PROTEIN SEQUENCE OF 2-39, AND METHYLATION AT LYS-5.
PubMed=10611321; DOI=10.1073/pnas.96.26.14967;
Strahl B.D., Ohba R., Cook R.G., Allis C.D.;
"Methylation of histone H3 at lysine 4 is highly conserved and
correlates with transcriptionally active nuclei in Tetrahymena.";
Proc. Natl. Acad. Sci. U.S.A. 96:14967-14972(1999).
[4]
PROTEIN SEQUENCE OF 2-22, AND PROTEOLYTIC CLEAVAGE.
PubMed=6993010; DOI=10.1016/0092-8674(80)90234-2;
Allis C.D., Bowen J.K., Abraham G.N., Glover C.V.C., Gorovsky M.A.;
"Proteolytic processing of histone H3 in chromatin: a physiologically
regulated event in Tetrahymena micronuclei.";
Cell 20:55-64(1980).
[5]
PROTEIN SEQUENCE OF 8-32, PHOSPHORYLATION AT SER-11, AND SUBCELLULAR
LOCATION.
PubMed=9636175; DOI=10.1073/pnas.95.13.7480;
Wei Y., Mizzen C.A., Cook R.G., Gorovsky M.A., Allis C.D.;
"Phosphorylation of histone H3 at serine 10 is correlated with
chromosome condensation during mitosis and meiosis in Tetrahymena.";
Proc. Natl. Acad. Sci. U.S.A. 95:7480-7484(1998).
[6]
ACETYLATION.
PubMed=7061439;
Vavra K.J., Allis C.D., Gorovsky M.A.;
"Regulation of histone acetylation in Tetrahymena macro- and
micronuclei.";
J. Biol. Chem. 257:2591-2598(1982).
[7]
ACETYLATION AT LYS-10 AND LYS-15.
PubMed=7862667; DOI=10.1073/pnas.92.4.1237;
Sobel R.E., Cook R.G., Perry C.A., Annunziato A.T., Allis C.D.;
"Conservation of deposition-related acetylation sites in newly
synthesized histones H3 and H4.";
Proc. Natl. Acad. Sci. U.S.A. 92:1237-1241(1995).
[8]
PHOSPHORYLATION AT SER-11, AND MUTAGENESIS OF SER-11.
PubMed=10199406; DOI=10.1016/S0092-8674(00)80718-7;
Wei Y., Yu L., Bowen J., Gorovsky M.A., Allis C.D.;
"Phosphorylation of histone H3 is required for proper chromosome
condensation and segregation.";
Cell 97:99-109(1999).
[9]
METHYLATION AT LYS-10, AND SUBCELLULAR LOCATION.
PubMed=12297044; DOI=10.1016/S0092-8674(02)00941-8;
Taverna S.D., Coyne R.S., Allis C.D.;
"Methylation of histone H3 at lysine 9 targets programmed DNA
elimination in Tetrahymena.";
Cell 110:701-711(2002).
[10]
INTERACTION WITH GCN5.
PubMed=14536085; DOI=10.1016/S1097-2765(03)00288-0;
Clements A., Poux A.N., Lo W.-S., Pillus L., Berger S.L.,
Marmorstein R.;
"Structural basis for histone and phosphohistone binding by the GCN5
histone acetyltransferase.";
Mol. Cell 12:461-473(2003).
[11]
FUNCTION, METHYLATION AT LYS-10, AND MUTAGENESIS OF LYS-10.
PubMed=14755052; DOI=10.1073/pnas.0305421101;
Liu Y., Mochizuki K., Gorovsky M.A.;
"Histone H3 lysine 9 methylation is required for DNA elimination in
developing macronuclei in Tetrahymena.";
Proc. Natl. Acad. Sci. U.S.A. 101:1679-1684(2004).
[12]
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=16908532; DOI=10.1128/MCB.01139-06;
Cui B., Liu Y., Gorovsky M.A.;
"Deposition and function of histone H3 variants in Tetrahymena
thermophila.";
Mol. Cell. Biol. 26:7719-7730(2006).
[13]
ACETYLATION AT LYS-37, AND METHYLATION AT LYS-37.
PubMed=17189264; DOI=10.1074/jbc.M607909200;
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
"Identification of histone H3 lysine 36 acetylation as a highly
conserved histone modification.";
J. Biol. Chem. 282:7632-7640(2007).
[14]
ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37
AND LYS-57, METHYLATION AT LYS-5; LYS-10; LYS-28; LYS-37; LYS-57 AND
LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17194708; DOI=10.1074/jbc.M607900200;
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
"Organismal differences in post-translational modifications in
histones H3 and H4.";
J. Biol. Chem. 282:7641-7655(2007).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. H3 is deposited into chromatin exclusively
through a DNA replication-coupled pathway that can be associated
with either DNA duplication or DNA repair synthesis during meiotic
homologous recombination. {ECO:0000269|PubMed:14755052,
ECO:0000269|PubMed:16908532}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. Interacts with GCN5, whereby H3S10ph
increases histone-protein interactions. Interacts with PDD1 and
PDD3. {ECO:0000269|PubMed:14536085}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to both
the large, transcriptionally active, somatic macronucleus (MAC)
and the small, transcriptionally inert, germ line micronucleus
(MIC).
-!- INDUCTION: Highly expressed in growing cells, but only at low
levels in starved cells. {ECO:0000269|PubMed:16908532}.
-!- PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent
H3K14ac formation by GCN5. H3S10ph is only found in the
mitotically dividing MIC, but not in the amitotically dividing
MAC. H3S10ph is correlated with chromosome condensation during
mitotic or meiotic micronuclear divisions.
{ECO:0000269|PubMed:10199406, ECO:0000269|PubMed:9636175}.
-!- PTM: Acetylation of histone H3 leads to transcriptional
activation. H3K14ac formation by GCN5 is promoted by H3S10ph.
H3K9acK14ac is the preferred acetylated form of newly synthesized
H3. Acetylation occurs almost exclusively in the MAC.
{ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:7061439, ECO:0000269|PubMed:7862667}.
-!- PTM: Methylated to form H3K4me. H3K4me is only found in the
transcriptionally active MAC. Methylated to form H3K9me in
developing MACs during conjugation, when genome-wide DNA
elimination occurs. At this stage, H3K9me specifically occurs on
DNA sequences being eliminated (IES), probably targeted by small
scan RNAs (scnRNAs) bound to IES, and is required for efficient
IES elimination. H3K9me is required for the interaction with the
chromodomains of PDD1 and PDD3. {ECO:0000269|PubMed:10611321,
ECO:0000269|PubMed:12297044, ECO:0000269|PubMed:14755052,
ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708}.
-!- PTM: The full-length protein H3S (slow migrating) is converted to
H3F (fast migrating) by proteolytic removal of the first 6
residues. H3F is unique to MIC, and processing seems to occur
regularly each generation at a specific point in the cell cycle.
{ECO:0000269|PubMed:6993010}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-!- CAUTION: To ensure consistency between histone entries, we follow
the 'Brno' nomenclature for histone modifications, with positions
referring to those used in the literature for the 'closest' model
organism. Due to slight variations in histone sequences between
organisms and to the presence of initiator methionine in
UniProtKB/Swiss-Prot sequences, the actual positions of modified
amino acids in the sequence generally differ. In this entry the
following conventions are used: H3K4ac = acetylated Lys-5;
H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac =
acetylated Lys-10; H3K9me3 = trimethylated Lys-10; H3S10ph =
phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K18ac =
acetylated Lys-19; H3K23ac = acetylated Lys-24; H3K27ac =
acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated
Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/3/3 = mono-, di- and
trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K56me1 =
monomethylated Lys-57; H3K79me1 = monomethylated Lys-80.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M87304; AAC37190.1; -; Unassigned_DNA.
EMBL; M87504; AAC37189.1; -; Unassigned_DNA.
EMBL; M11142; AAA30115.1; -; Genomic_DNA.
EMBL; M11143; AAA30116.1; -; Genomic_DNA.
PIR; S41499; S41499.
PIR; S42521; S42521.
PIR; S42522; S42522.
ProteinModelPortal; P69150; -.
SMR; P69150; -.
iPTMnet; P69150; -.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
Methylation; Nucleosome core; Nucleus; Phosphoprotein.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10611321,
ECO:0000269|PubMed:6993010}.
CHAIN 2 136 Histone H3.
/FTId=PRO_0000221330.
CHAIN 8 136 H3F.
/FTId=PRO_0000385010.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:10611321,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:10611321,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:10611321,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:12297044,
ECO:0000269|PubMed:14755052,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:7862667}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:10199406,
ECO:0000269|PubMed:9636175}.
MOD_RES 15 15 N6-acetyllysine.
{ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:7862667}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 57 57 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-methyllysine.
{ECO:0000269|PubMed:17194708}.
MUTAGEN 10 10 K->Q: Reduces greatly IES elimination.
{ECO:0000269|PubMed:14755052}.
MUTAGEN 11 11 S->A: Causes abnormal chromosome
condensation and segregation in MIC
nuclear divisions.
{ECO:0000269|PubMed:10199406}.
CONFLICT 6 6 Q -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 F -> S (in Ref. 2; AAA30115).
{ECO:0000305}.
SEQUENCE 136 AA; 15429 MW; 1358B0734220CF74 CRC64;
MARTKQTARK STGAKAPRKQ LASKAARKSA PATGGIKKPH RFRPGTVALR EIRKYQKSTD
LLIRKLPFQR LVRDIAHEFK AELRFQSSAV LALQEAAEAY LVGLFEDTNL CAIHARRVTI
MTKDMQLARR IRGERF


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