H2A_PENVA
ID H2A_PENVA Reviewed; 123 AA.
AC Q6PV61; P83841; Q6PV62;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Histone H2A;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS91563.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-105, PROTEIN SEQUENCE OF 21-29; 40-64 AND
RP 82-123, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Hemocyte {ECO:0000312|EMBL:AAS91563.1};
RX PubMed=15606770; DOI=10.1111/j.1432-1033.2004.04448.x;
RA Patat S.A., Carnegie R.B., Kingsbury C., Gross P.S., Chapman R.,
RA Schey K.L.;
RT "Antimicrobial activity of histones from hemocytes of the Pacific white
RT shrimp.";
RL Eur. J. Biochem. 271:4825-4833(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-123, MASS SPECTROMETRY, ACETYLATION AT SER-2, AND
RP PHOSPHORYLATION AT SER-2.
RC TISSUE=Hemocyte {ECO:0000269|PubMed:17405180};
RX PubMed=17405180; DOI=10.1002/jms.1200;
RA Ouvry-Patat S.A., Schey K.L.;
RT "Characterization of antimicrobial histone sequences and posttranslational
RT modifications by mass spectrometry.";
RL J. Mass Spectrom. 42:664-674(2007).
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:15606770}.
CC -!- FUNCTION: Has antimicrobial activity against the Gram-positive
CC bacterium M.luteus. {ECO:0000269|PubMed:15606770}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome.
CC -!- PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250|UniProtKB:Q96QV6}.
CC -!- PTM: Phosphorylation of Ser-2 directly represses transcription.
CC {ECO:0000250|UniProtKB:Q96QV6}.
CC -!- MASS SPECTROMETRY: Mass=13193; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15606770};
CC -!- MASS SPECTROMETRY: Mass=13269; Method=MALDI; Note=May be
CC phosphorylated.; Evidence={ECO:0000269|PubMed:15606770};
CC -!- MASS SPECTROMETRY: Mass=13197; Method=MALDI; Note=Acetylation on Ser-
CC 2.; Evidence={ECO:0000269|PubMed:17405180};
CC -!- MASS SPECTROMETRY: Mass=13277; Method=MALDI; Note=Acetylation and
CC phosphorylation on Ser-2.; Evidence={ECO:0000269|PubMed:17405180};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000255}.
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DR EMBL; AY576482; AAS91563.1; -; mRNA.
DR EMBL; AY576483; AAS91564.1; -; mRNA.
DR AlphaFoldDB; Q6PV61; -.
DR SMR; Q6PV61; -.
DR iPTMnet; Q6PV61; -.
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; IDA:UniProtKB.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 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; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17405180"
FT CHAIN 2..123
FT /note="Histone H2A"
FT /evidence="ECO:0000269|PubMed:17405180"
FT /id="PRO_0000055265"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17405180"
FT MOD_RES 104
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96QV6"
FT CONFLICT 79
FT /note="V -> I (in Ref. 1; AAS91564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 13267 MW; 10379EACFF286450 CRC64;
MSGRGKGGKV KGKSKSRSSR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA
EVLELAGNAA RDNKKTRIVP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
EKK
