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Histone H2A [Cleaved into: Acipensin 1 (Ac1); Acipensin 2 (Ac2); Acipensin 3 (Ac3); Acipensin 4 (Ac4); Acipensin 5 (Ac5); Acipensin 6 (Ac6)] (Fragments)

 H2A_ACIGU               Reviewed;          76 AA.
C0HJQ3;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-APR-2015, sequence version 1.
28-MAR-2018, entry version 10.
RecName: Full=Histone H2A {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 1 {ECO:0000303|PubMed:25558400};
Short=Ac1 {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 2 {ECO:0000303|PubMed:25558400};
Short=Ac2 {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 3 {ECO:0000303|PubMed:25558400};
Short=Ac3 {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 4 {ECO:0000303|PubMed:25558400};
Short=Ac4 {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 5 {ECO:0000303|PubMed:25558400};
Short=Ac5 {ECO:0000303|PubMed:25558400};
Contains:
RecName: Full=Acipensin 6 {ECO:0000303|PubMed:25558400};
Short=Ac6 {ECO:0000303|PubMed:25558400};
Flags: Fragments;
Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae;
Acipenser.
NCBI_TaxID=7902 {ECO:0000303|PubMed:25558400};
[1] {ECO:0000305}
PROTEIN SEQUENCE OF 2-76, FUNCTION OF ACIPENSINS, MASS SPECTROMETRY,
AND ACETYLATION AT SER-2.
TISSUE=Leukocyte {ECO:0000303|PubMed:25558400};
PubMed=25558400;
Shamova O.V., Orlov D.S., Balandin S.V., Shramova E.I.,
Tsvetkova E.V., Panteleev P.V., Leonova Y.F., Tagaev A.A.,
Kokryakov V.N., Ovchinnikova T.V.;
"Acipensins - novel antimicrobial peptides from leukocytes of the
Russian sturgeon Acipenser gueldenstaedtii.";
Acta Naturae 6:99-109(2014).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. {ECO:0000305}.
-!- FUNCTION: Acipensins are antimicrobial peptides. Acipensins 1 and
2 have antibacterial activity against Gram-positive bacteria
L.monocytogenes EGD (MIC are 1.1 uM and 1.0 uM, respectively) and
S.aureus ATCC 33591 (MIC are 0.9 uM and 0.6 uM, respectively),
against Gram-negative bacterium E.coli ML-35p (MIC are 0.7 uM and
0.3 uM, respectively) and antifungal activity against C.albicans
820 (MIC are 1.0 uM and 0.9 uM, respectively). Acipensin 6 has
antibacterial activity against Gram-negative bacterium E.coli ML-
35p (MIC=2.5 uM). Antimicrobial activity is reduced by high ionic
strength. Acipensins 1, 2 and 6 have no hemolytic (up to 40 uM) or
cytotoxic (up to 20 uM) effects on human cells in vitro.
{ECO:0000269|PubMed:25558400}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. {ECO:0000250|UniProtKB:P02264}.
-!- SUBCELLULAR LOCATION: Histone H2A: Nucleus
{ECO:0000250|UniProtKB:P02264}. Chromosome
{ECO:0000250|UniProtKB:P02264}.
-!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
Phosphorylation on Ser-2 directly represses transcription.
{ECO:0000250|UniProtKB:P0C0S8}.
-!- MASS SPECTROMETRY: Mass=5336.2; Method=MALDI; Range=2-51;
Note=Acipensin 1.; Evidence={ECO:0000269|PubMed:25558400};
-!- MASS SPECTROMETRY: Mass=3803; Method=MALDI; Range=2-36;
Note=Acipensin 2.; Evidence={ECO:0000269|PubMed:25558400};
-!- MASS SPECTROMETRY: Mass=5173; Method=MALDI; Range=2-50;
Note=Acipensin 3.; Evidence={ECO:0000269|PubMed:25558400};
-!- MASS SPECTROMETRY: Mass=4777.5; Method=MALDI; Range=2-47;
Note=Acipensin 4.; Evidence={ECO:0000269|PubMed:25558400};
-!- MASS SPECTROMETRY: Mass=5449.4; Method=MALDI; Range=2-52;
Note=Acipensin 5.; Evidence={ECO:0000269|PubMed:25558400};
-!- MASS SPECTROMETRY: Mass=2740.2; Method=MALDI; Range=53-76;
Note=Acipensin 6.; Evidence={ECO:0000269|PubMed:25558400};
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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SMR; C0HJQ3; -.
iPTMnet; C0HJQ3; -.
GO; GO:0000786; C:nucleosome; IEA:InterPro.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR032458; Histone_H2A_CS.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
1: Evidence at protein level;
Acetylation; Antibiotic; Antimicrobial; Chromosome;
Direct protein sequencing; Fungicide; Hydroxylation; Immunity;
Isopeptide bond; Nucleus; Phosphoprotein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02264}.
CHAIN 2 >76 Histone H2A.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432406.
PEPTIDE 2 52 Acipensin 5.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432407.
PEPTIDE 2 51 Acipensin 1.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432408.
PEPTIDE 2 50 Acipensin 3.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432409.
PEPTIDE 2 47 Acipensin 4.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432410.
PEPTIDE 2 36 Acipensin 2.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432411.
PEPTIDE 53 76 Acipensin 6.
{ECO:0000269|PubMed:25558400}.
/FTId=PRO_0000432412.
MOD_RES 2 2 N-acetylserine; in acipensins.
{ECO:0000269|PubMed:25558400}.
MOD_RES 2 2 N-acetylserine; in histone H2A.
{ECO:0000250|UniProtKB:P02264}.
MOD_RES 2 2 Phosphoserine; in histone H2A.
{ECO:0000250|UniProtKB:P02264}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 6 6 N6-acetyllysine; in histone H2A.
{ECO:0000250|UniProtKB:P02264}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 65 65 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 66 66 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000250|UniProtKB:P0C0S8}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin); in
histone H2A.
{ECO:0000250|UniProtKB:P04908}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin); in
histone H2A.
{ECO:0000250|UniProtKB:P04908}.
NON_CONS 52 53 {ECO:0000303|PubMed:25558400}.
NON_TER 76 76 {ECO:0000303|PubMed:25558400}.
SEQUENCE 76 AA; 8262 MW; 6B6BF530E14E9666 CRC64;
MSGRGKTGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AQRVGAGAPV YLILELAGNA
ARDNKKTRII PRHLQL


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