H4_PENVA
ID H4_PENVA Reviewed; 103 AA.
AC P83865;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Histone H4;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-103, MASS SPECTROMETRY, METHYLATION AT LYS-21 AND
RP LYS-32, AND ACETYLATION AT THR-2; LYS-6; LYS-9; LYS-13 AND LYS-17.
RC TISSUE=Hemocyte {ECO:0000269|PubMed:17405180};
RX PubMed=17405180; DOI=10.1002/jms.1200;
RA Ouvry-Patat S.A., Schey K.L.;
RT "Characterization of antimicrobial histone sequences and posttranslational
RT modifications by mass spectrometry.";
RL J. Mass Spectrom. 42:664-674(2007).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 24-38; 47-56; 61-73 AND 82-93, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Hemocyte {ECO:0000269|PubMed:15606770};
RX PubMed=15606770; DOI=10.1111/j.1432-1033.2004.04448.x;
RA Patat S.A., Carnegie R.B., Kingsbury C., Gross P.S., Chapman R.,
RA Schey K.L.;
RT "Antimicrobial activity of histones from hemocytes of the Pacific white
RT shrimp.";
RL Eur. J. Biochem. 271:4825-4833(2004).
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. {ECO:0000269|PubMed:15606770}.
CC -!- FUNCTION: A mixture of histones H2B and H4 has antimicrobial activity
CC against the Gram-positive bacterium M.luteus.
CC {ECO:0000269|PubMed:15606770}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P84040}.
CC Chromosome {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=11323; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15606770};
CC -!- MASS SPECTROMETRY: Mass=11322; Method=MALDI; Note=With 1 dimethylation
CC and 1 acetylation on a lysine residue.;
CC Evidence={ECO:0000269|PubMed:17405180};
CC -!- MASS SPECTROMETRY: Mass=11362; Method=MALDI; Note=With 1 dimethylation
CC and 2 acetylations on lysine residues.;
CC Evidence={ECO:0000269|PubMed:17405180};
CC -!- MASS SPECTROMETRY: Mass=11403; Method=MALDI; Note=With 1 dimethylation
CC and 3 acetylations on lysine residues.;
CC Evidence={ECO:0000269|PubMed:17405180};
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000255}.
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DR iPTMnet; P83865; -.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW Direct protein sequencing; DNA-binding; Methylation; Nucleosome core;
KW Nucleus.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17405180"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158345"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 21
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 32
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:17405180"
SQ SEQUENCE 103 AA; 11374 MW; 4596DF6393BD2082 CRC64;
MTGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRXXXTLYG FGG
