H2A_HIPHI
ID H2A_HIPHI Reviewed; 52 AA.
AC P59890;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Histone H2A;
DE Contains:
DE RecName: Full=Hipposin;
DE Flags: Fragment;
OS Hippoglossus hippoglossus (Atlantic halibut) (Pleuronectes hippoglossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Hippoglossus.
OX NCBI_TaxID=8267;
RN [1]
RP PROTEIN SEQUENCE OF 2-52, ACETYLATION AT SER-2, SYNTHESIS, FUNCTION, AND
RP MASS SPECTROMETRY.
RC TISSUE=Skin;
RX PubMed=12637028; DOI=10.1016/s1570-9639(03)00018-9;
RA Birkemo G.A., Lueders T., Andersen O., Nes I.F., Nissen-Meyer J.;
RT "Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut
RT (Hippoglossus hippoglossus L.).";
RL Biochim. Biophys. Acta 1646:207-215(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. {ECO:0000269|PubMed:12637028}.
CC -!- FUNCTION: Hipposin shows strong antimicrobial activity against several
CC Gram-positive and Gram-negative bacteria.
CC {ECO:0000269|PubMed:12637028}.
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 -!- SUBCELLULAR LOCATION: [Hipposin]: Secreted.
CC -!- PTM: Acetylation is not necessary for the antibacterial activity.
CC -!- PTM: Monoubiquitination in 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, leading to the recruitment of repair proteins to
CC sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-
CC linked ubiquitination are distinct events (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
CC Phosphorylation on Ser-2 directly represses transcription (By
CC similarity). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=5459; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12637028};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR AlphaFoldDB; P59890; -.
DR SMR; P59890; -.
DR iPTMnet; P59890; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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 PRINTS; PR00620; HISTONEH2A.
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; Hydroxylation; Isopeptide bond;
KW Nucleosome core; Nucleus; Phosphoprotein; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12637028"
FT CHAIN 2..52
FT /note="Hipposin"
FT /id="PRO_0000013166"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12637028"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT NON_TER 52
SQ SEQUENCE 52 AA; 5547 MW; 07AA7B4302D17D6E CRC64;
MSGRGKTGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AHRVGAGAPV YL
