H2A_ACIGU
ID H2A_ACIGU Reviewed; 76 AA.
AC C0HJQ3;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Histone H2A {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 1 {ECO:0000303|PubMed:25558400};
DE Short=Ac1 {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 2 {ECO:0000303|PubMed:25558400};
DE Short=Ac2 {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 3 {ECO:0000303|PubMed:25558400};
DE Short=Ac3 {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 4 {ECO:0000303|PubMed:25558400};
DE Short=Ac4 {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 5 {ECO:0000303|PubMed:25558400};
DE Short=Ac5 {ECO:0000303|PubMed:25558400};
DE Contains:
DE RecName: Full=Acipensin 6 {ECO:0000303|PubMed:25558400};
DE Short=Ac6 {ECO:0000303|PubMed:25558400};
DE Flags: Fragments;
OS Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7902 {ECO:0000303|PubMed:25558400};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-76, FUNCTION OF ACIPENSINS, MASS SPECTROMETRY, AND
RP ACETYLATION AT SER-2.
RC TISSUE=Leukocyte {ECO:0000303|PubMed:25558400};
RX PubMed=25558400;
RA Shamova O.V., Orlov D.S., Balandin S.V., Shramova E.I., Tsvetkova E.V.,
RA Panteleev P.V., Leonova Y.F., Tagaev A.A., Kokryakov V.N.,
RA Ovchinnikova T.V.;
RT "Acipensins - novel antimicrobial peptides from leukocytes of the Russian
RT sturgeon Acipenser gueldenstaedtii.";
RL Acta Naturae 6:99-109(2014).
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:0000305}.
CC -!- FUNCTION: Acipensins are antimicrobial peptides. Acipensins 1 and 2
CC have antibacterial activity against Gram-positive bacteria
CC L.monocytogenes EGD (MIC are 1.1 uM and 1.0 uM, respectively) and
CC S.aureus ATCC 33591 (MIC are 0.9 uM and 0.6 uM, respectively), against
CC Gram-negative bacterium E.coli ML-35p (MIC are 0.7 uM and 0.3 uM,
CC respectively) and antifungal activity against C.albicans 820 (MIC are
CC 1.0 uM and 0.9 uM, respectively). Acipensin 6 has antibacterial
CC activity against Gram-negative bacterium E.coli ML-35p (MIC=2.5 uM).
CC Antimicrobial activity is reduced by high ionic strength. Acipensins 1,
CC 2 and 6 have no hemolytic (up to 40 uM) or cytotoxic (up to 20 uM)
CC effects on human cells in vitro. {ECO:0000269|PubMed:25558400}.
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:0000250|UniProtKB:P02264}.
CC -!- SUBCELLULAR LOCATION: [Histone H2A]: Nucleus
CC {ECO:0000250|UniProtKB:P02264}. Chromosome
CC {ECO:0000250|UniProtKB:P02264}.
CC -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
CC Phosphorylation on Ser-2 directly represses transcription.
CC {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- MASS SPECTROMETRY: [Acipensin 1]: Mass=5336.2; Method=MALDI;
CC Note=Acipensin 1.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- MASS SPECTROMETRY: [Acipensin 2]: Mass=3803; Method=MALDI;
CC Note=Acipensin 2.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- MASS SPECTROMETRY: [Acipensin 3]: Mass=5173; Method=MALDI;
CC Note=Acipensin 3.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- MASS SPECTROMETRY: [Acipensin 4]: Mass=4777.5; Method=MALDI;
CC Note=Acipensin 4.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- MASS SPECTROMETRY: [Acipensin 5]: Mass=5449.4; Method=MALDI;
CC Note=Acipensin 5.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- MASS SPECTROMETRY: [Acipensin 6]: Mass=2740.2; Method=MALDI;
CC Note=Acipensin 6.; Evidence={ECO:0000269|PubMed:25558400};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR AlphaFoldDB; C0HJQ3; -.
DR SMR; C0HJQ3; -.
DR iPTMnet; C0HJQ3; -.
DR PRIDE; C0HJQ3; -.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; 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 SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW Direct protein sequencing; Fungicide; Hydroxylation; Immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02264"
FT CHAIN 2..>76
FT /note="Histone H2A"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432406"
FT PEPTIDE 2..52
FT /note="Acipensin 5"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432407"
FT PEPTIDE 2..51
FT /note="Acipensin 1"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432408"
FT PEPTIDE 2..50
FT /note="Acipensin 3"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432409"
FT PEPTIDE 2..47
FT /note="Acipensin 4"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432410"
FT PEPTIDE 2..36
FT /note="Acipensin 2"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432411"
FT PEPTIDE 53..76
FT /note="Acipensin 6"
FT /evidence="ECO:0000269|PubMed:25558400"
FT /id="PRO_0000432412"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine; in acipensins"
FT /evidence="ECO:0000269|PubMed:25558400"
FT MOD_RES 2
FT /note="N-acetylserine; in histone H2A"
FT /evidence="ECO:0000250|UniProtKB:P02264"
FT MOD_RES 2
FT /note="Phosphoserine; in histone H2A"
FT /evidence="ECO:0000250|UniProtKB:P02264"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 6
FT /note="N6-acetyllysine; in histone H2A"
FT /evidence="ECO:0000250|UniProtKB:P02264"
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 MOD_RES 65
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 66
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); in histone H2A"
FT /evidence="ECO:0000250|UniProtKB:P04908"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); in histone H2A"
FT /evidence="ECO:0000250|UniProtKB:P04908"
FT NON_CONS 52..53
FT /evidence="ECO:0000303|PubMed:25558400"
FT NON_TER 76
FT /evidence="ECO:0000303|PubMed:25558400"
SQ SEQUENCE 76 AA; 8262 MW; 6B6BF530E14E9666 CRC64;
MSGRGKTGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AQRVGAGAPV YLILELAGNA
ARDNKKTRII PRHLQL
