ID   A0A3P9AXE0_9CICH        Unreviewed;       102 AA.
AC   A0A3P9AXE0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Histone H4 {ECO:0000256|RuleBase:RU000528};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005002309.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005002309.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005002309.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00002001, ECO:0000256|RuleBase:RU000528}.
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. {ECO:0000256|RuleBase:RU000528}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone H4 family.
CC       {ECO:0000256|ARBA:ARBA00006564, ECO:0000256|RuleBase:RU000528}.
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DR   AlphaFoldDB; A0A3P9AXE0; -.
DR   STRING; 106582.ENSMZEP00005002309; -.
DR   Ensembl; ENSMZET00005002412.1; ENSMZEP00005002309.1; ENSMZEG00005001785.1.
DR   GeneTree; ENSGT00990000203553; -.
DR   Proteomes; UP000265160; LG6.
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   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   PANTHER; PTHR10484; HISTONE H4; 1.
DR   PANTHER; PTHR10484:SF200; HISTONE H4 TYPE VIII; 1.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU000528};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160}.
FT   DOMAIN          33..95
FT                   /note="CENP-T/Histone H4 histone fold"
FT                   /evidence="ECO:0000259|Pfam:PF15511"
SQ   SEQUENCE   102 AA;  11294 MW;  4E019EE99DC28342 CRC64;
     GSGRRGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLTRR GGVKRISGLI YEETRGVLKV
     FLENVIRDAV TYTEHAKRKT VTAMDVVYAL KRQGRTLYGF GG
//