H43_MAIZE
ID H43_MAIZE Reviewed; 103 AA.
AC Q41811;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Histone H4.3;
DE AltName: Full=HM4;
GN Name=H4;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B37N;
RA Tacchini P., Walbot W.;
RT "A new member of the histone H4 gene family in Zea mays.";
RL (er) Plant Gene Register PGR95-023(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND METHYLATION AT LYS-21.
RX PubMed=16624902; DOI=10.1534/genetics.106.056853;
RA Shi J., Dawe R.K.;
RT "Partitioning of the maize epigenome by the number of methyl groups on
RT histone H3 lysines 9 and 27.";
RL Genetics 173:1571-1583(2006).
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:0000269|PubMed:16624902}. Chromosome
CC {ECO:0000269|PubMed:16624902}.
CC -!- PTM: Lys-21Me2 and Lys-21Me3 not detected.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X84376; CAA59110.1; -; Genomic_DNA.
DR AlphaFoldDB; Q41811; -.
DR SMR; Q41811; -.
DR iPTMnet; Q41811; -.
DR PRIDE; Q41811; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41811; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR CDD; cd00076; H4; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Histone H4.3"
FT /id="PRO_0000158325"
FT DNA_BIND 17..21
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16624902"
SQ SEQUENCE 103 AA; 11552 MW; 1C8960313676F401 CRC64;
MSGRGKGGKG LGKGARKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVRK
IFLENVIRDA VTYTEHARRK TVTAMDVVYA LKRQGRTLYG FGG
