ID   H4_NEUCR                Reviewed;         103 AA.
AC   P04914; Q7RV47; Q7RV56;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Histone H4;
GN   Name=hH4-1; Synonyms=hhf1; ORFNames=B7K22.020, NCU01634;
GN   and
GN   Name=hH4-2; Synonyms=hhf2; ORFNames=NCU00212;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HH4-1).
RX   PubMed=6310494; DOI=10.1093/nar/11.16.5347;
RA   Woudt L.P., Pastink A., Kempers-Veenstra A.E., Jansen A.E.M., Mager W.H.,
RA   Planta R.J.;
RT   "The genes coding for histone H3 and H4 in Neurospora crassa are unique and
RT   contain intervening sequences.";
RL   Nucleic Acids Res. 11:5347-5360(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HH4-1 AND HH4-2).
RX   PubMed=11901114; DOI=10.1093/genetics/160.3.961;
RA   Hays S.M., Swanson J., Selker E.U.;
RT   "Identification and characterization of the genes encoding the core
RT   histones and histone variants of Neurospora crassa.";
RL   Genetics 160:961-973(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HH4-1).
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HH4-1 AND HH4-2).
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC       promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC       {ECO:0000250|UniProtKB:P02309}.
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; X01611; CAA25760.1; -; Genomic_DNA.
DR   EMBL; AY062172; AAL38972.1; -; Genomic_DNA.
DR   EMBL; AY062173; AAL38974.1; -; Genomic_DNA.
DR   EMBL; AL670543; CAD21509.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA26766.2; -; Genomic_DNA.
DR   EMBL; CM002238; EAA27361.1; -; Genomic_DNA.
DR   PIR; S07913; S07913.
DR   RefSeq; XP_956002.2; XM_950909.3.
DR   RefSeq; XP_956597.1; XM_951504.3.
DR   AlphaFoldDB; P04914; -.
DR   BMRB; P04914; -.
DR   SMR; P04914; -.
DR   DIP; DIP-59937N; -.
DR   IntAct; P04914; 1.
DR   STRING; 5141.EFNCRP00000000141; -.
DR   EnsemblFungi; EAA26766; EAA26766; NCU01634.
DR   EnsemblFungi; EAA27361; EAA27361; NCU00212.
DR   GeneID; 3872149; -.
DR   GeneID; 3872744; -.
DR   KEGG; ncr:NCU00212; -.
DR   KEGG; ncr:NCU01634; -.
DR   VEuPathDB; FungiDB:NCU00212; -.
DR   VEuPathDB; FungiDB:NCU01634; -.
DR   HOGENOM; CLU_109117_2_3_1; -.
DR   InParanoid; P04914; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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   InterPro; IPR019809; Histone_H4_CS.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000158336"
FT   DNA_BIND        17..21
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         92
FT                   /note="N6-glutaryllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02309"
SQ   SEQUENCE   103 AA;  11370 MW;  9392CDB8AE0C52E2 CRC64;
     MTGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISAM IYEETRGVLK
     TFLEGVIRDA VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG FGG