ID   H2B3_ICTPU              Reviewed;          18 AA.
AC   P81904;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Histone H2B 3;
DE   AltName: Full=Antibacterial histone-like protein 3;
DE            Short=HLP-3;
DE   Flags: Fragment;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-18, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin;
RX   PubMed=9645227; DOI=10.1007/s000180050175;
RA   Robinette D., Wada S., Arroll T., Levy M.G., Miller W.L., Noga E.J.;
RT   "Antimicrobial activity in the skin of the channel catfish Ictalurus
RT   punctatus: characterization of broad-spectrum histone-like antimicrobial
RT   proteins.";
RL   Cell. Mol. Life Sci. 54:467-475(1998).
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:9645227}.
CC   -!- FUNCTION: Has antimicrobial activity. Possesses strong activity against
CC       saprolegnia, the most common fungal infection in fish.
CC       {ECO:0000269|PubMed:9645227}.
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. Chromosome.
CC   -!- PTM: Phosphorylated during apoptosis; which facilitates apoptotic
CC       chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC   -!- MASS SPECTROMETRY: Mass=13506; Method=MALDI; Note=The measured range is
CC       2-18.; Evidence={ECO:0000269|PubMed:9645227};
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   AlphaFoldDB; P81904; -.
DR   Proteomes; UP000221080; Genome assembly.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Fungicide; Nucleosome core;
KW   Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9645227"
FT   CHAIN           2..>18
FT                   /note="Histone H2B 3"
FT                   /id="PRO_0000071850"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06900"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   NON_TER         18
SQ   SEQUENCE   18 AA;  1926 MW;  44853CA66FD2F377 CRC64;
     MPDPAKTAPK KKSKKAVT