ID U3I5X1_ANAPP Unreviewed; 139 AA.
AC U3I5X1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN Name=H2AZ2 {ECO:0000313|Ensembl:ENSAPLP00000002642.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000002642.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000002642.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037205}.
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:0000256|RuleBase:RU003767}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003767}.
CC -!- SIMILARITY: Belongs to the histone H2A family.
CC {ECO:0000256|ARBA:ARBA00010691, ECO:0000256|RuleBase:RU003767}.
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DR AlphaFoldDB; U3I5X1; -.
DR STRING; 8840.ENSAPLP00000002642; -.
DR Ensembl; ENSAPLT00000003234.2; ENSAPLP00000002642.2; ENSAPLG00000003184.2.
DR GeneTree; ENSGT00900000140979; -.
DR HOGENOM; CLU_062828_2_2_1; -.
DR OMA; ARTQNNM; -.
DR Proteomes; UP000016666; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU003767};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003767};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW ECO:0000256|RuleBase:RU003767};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003767};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 18..104
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT DOMAIN 106..138
FT /note="Histone H2A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16211"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 139 AA; 14487 MW; 15F2F3649F12C125 CRC64;
GGAGLTRALS PQAGGKAGKD SGKAKAKAVS RSQRAGLQFP VGRIHRHLKT RTTSHGRVGA
TAAVYSAAIL EYLTAEVLEL AGNASKDLKV KRITPRHLQL AIRGDEELDS LIKATIAGGG
VIPHIHKSLI GKKGQQKTA
//
