H4_PEA
ID H4_PEA Reviewed; 103 AA.
AC P62788; P02308; P59258;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Histone H4;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Alaska;
RX PubMed=7579177; DOI=10.1007/bf00043650;
RA Devitt M.L., Stafstrom J.P.;
RT "Cell cycle regulation during growth-dormancy cycles in pea axillary
RT buds.";
RL Plant Mol. Biol. 29:255-265(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-103, AND ACETYLATION AT SER-2; LYS-9 AND LYS-17.
RC TISSUE=Seedling;
RX PubMed=5388597; DOI=10.1016/s0021-9258(18)63612-9;
RA Delange R.J., Fambrough D.M., Smith E.L., Bonner J.;
RT "Calf and pea histone IV. 3. Complete amino acid sequence of pea seedling
RT histone IV; comparison with the homologous calf thymus histone.";
RL J. Biol. Chem. 244:5669-5679(1969).
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 H4 family. {ECO:0000305}.
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DR EMBL; U10042; AAA86948.1; -; mRNA.
DR PIR; S60475; HSPM4.
DR AlphaFoldDB; P62788; -.
DR SMR; P62788; -.
DR iPTMnet; P62788; -.
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; -; 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 Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Nucleosome core; Nucleus.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5388597"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158342"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:5388597"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:5388597"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:5388597"
SQ SEQUENCE 103 AA; 11409 MW; A9FD57725A2A7598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
IFLENVIRDA VTYTEHARRK TVTAMDVVYA LKRQGRTLYG FGG
