ID   H2A_BUFGR               Reviewed;          39 AA.
AC   P55897;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histone H2A;
DE   Contains:
DE     RecName: Full=Buforin-1;
DE     AltName: Full=Buforin I;
DE   Contains:
DE     RecName: Full=Buforin-2;
DE     AltName: Full=Buforin II;
DE   Flags: Fragment;
OS   Bufo gargarizans (Asian toad) (Bufo bufo gargarizans).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Bufo.
OX   NCBI_TaxID=30331;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Stomach;
RX   PubMed=8573171; DOI=10.1006/bbrc.1996.0071;
RA   Park C.B., Kim M.S., Kim S.C.;
RT   "A novel antimicrobial peptide from Bufo bufo gargarizans.";
RL   Biochem. Biophys. Res. Commun. 218:408-413(1996).
RN   [2]
RP   STRUCTURE BY NMR OF 16-36.
RX   PubMed=8946958; DOI=10.1016/s0014-5793(96)01193-3;
RA   Yi G.-S., Park C.B., Kim S.C., Cheong C.;
RT   "Solution structure of an antimicrobial peptide buforin II.";
RL   FEBS Lett. 398:87-90(1996).
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   -!- FUNCTION: Buforins are strong antimicrobial activities in vitro against
CC       a broad-spectrum of microorganisms including fungi. Buforin II is more
CC       potent than buforin I.
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: Monoubiquitination of C-terminus gives a specific tag for
CC       epigenetic transcriptional repression. Following DNA double-strand
CC       breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of
CC       ubiquitin moieties (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   AlphaFoldDB; P55897; -.
DR   SMR; P55897; -.
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   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Fungicide; Hydroxylation;
KW   Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT   PEPTIDE         1..39
FT                   /note="Buforin-1"
FT                   /id="PRO_0000013167"
FT   PEPTIDE         16..36
FT                   /note="Buforin-2"
FT                   /id="PRO_0000013168"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         9
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         9
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         36
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   CROSSLNK        13
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         39
SQ   SEQUENCE   39 AA;  4263 MW;  E9F88A21839219AA CRC64;
     AGRGKQGGKV RAKAKTRSSR AGLQFPVGRV HRLLRKGNY