ID H2AV_XENTR Reviewed; 128 AA.
AC Q5BJ65; Q28FN8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
GN Name=h2az2; ORFNames=TGas096d24.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC limiting DNA accessibility to the cellular machineries which require
CC DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling. May be involved in the formation of constitutive
CC heterochromatin. May be required for chromosome segregation during cell
CC division (By similarity). {ECO:0000250}.
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. H2A or its variant H2AZ2 forms a heterodimer with H2B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 when associated with the 5'-
CC end of active genes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; CR761860; CAJ81609.1; -; mRNA.
DR EMBL; BC091605; AAH91605.1; -; mRNA.
DR RefSeq; NP_001016178.1; NM_001016178.2.
DR AlphaFoldDB; Q5BJ65; -.
DR SMR; Q5BJ65; -.
DR STRING; 8364.ENSXETP00000013001; -.
DR PaxDb; 8364-ENSXETP00000002709; -.
DR DNASU; 548932; -.
DR GeneID; 548932; -.
DR KEGG; xtr:548932; -.
DR AGR; Xenbase:XB-GENE-964016; -.
DR CTD; 94239; -.
DR Xenbase; XB-GENE-964016; h2az2.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; Q5BJ65; -.
DR OMA; ARTQNNM; -.
DR OrthoDB; 3019669at2759; -.
DR PhylomeDB; Q5BJ65; -.
DR TreeFam; TF354232; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Bgee; ENSXETG00000001258; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; Q5BJ65; baseline.
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 CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 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; HISTONE H2A; 1.
DR PANTHER; PTHR23430:SF280; HISTONE H2A.V; 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; Histone-fold; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..128
FT /note="Histone H2A.V"
FT /id="PRO_0000055307"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 14
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 116
FT /note="N6-lactoyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 128 AA; 13509 MW; 1F3C388F6854041C CRC64;
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTA
//
