H32_TETPI
ID H32_TETPI Reviewed; 41 AA.
AC P69124; P17705;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Histone H3.2;
DE Flags: Fragment;
OS Tetrahymena pigmentosa.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2129549; DOI=10.1093/nar/18.2.323;
RA Brunk C.F., Sadler L.A.;
RT "Characterization of the promoter region of Tetrahymena genes.";
RL Nucleic Acids Res. 18:323-329(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2129541; DOI=10.1007/bf02099999;
RA Brunk C.F., Kahn R.W., Sadler L.A.;
RT "Phylogenetic relationships among Tetrahymena species determined using the
RT polymerase chain reaction.";
RL J. Mol. Evol. 30:290-297(1990).
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 -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; X17143; CAA35020.1; -; Genomic_DNA.
DR AlphaFoldDB; P69124; -.
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; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..>41
FT /note="Histone H3.2"
FT /id="PRO_0000221345"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 41
SQ SEQUENCE 41 AA; 4343 MW; FC53DF37507B58D9 CRC64;
MARTKQTARK STGAKAPRKQ LASKAARKSA PATGGIKKPH R