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Database: UniProt
Entry: A0A452E3K5_CAPHI
LinkDB: A0A452E3K5_CAPHI
Original site: A0A452E3K5_CAPHI 
ID   A0A452E3K5_CAPHI        Unreviewed;       129 AA.
AC   A0A452E3K5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   Name=H2AC20 {ECO:0000313|Ensembl:ENSCHIP00000006590.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000006590.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000006590.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000006590.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00002001}.
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|ARBA:ARBA00011538, 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   EMBL; LWLT01000004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005677761.1; XM_005677704.3.
DR   AlphaFoldDB; A0A452E3K5; -.
DR   SMR; A0A452E3K5; -.
DR   STRING; 9925.ENSCHIP00000006590; -.
DR   Ensembl; ENSCHIT00000014318.1; ENSCHIP00000006590.1; ENSCHIG00000010392.1.
DR   GeneID; 102171676; -.
DR   KEGG; chx:102171676; -.
DR   GeneTree; ENSGT00940000153118; -.
DR   OMA; CEAWHAE; -.
DR   OrthoDB; 5216419at2759; -.
DR   Proteomes; UP000291000; Chromosome 3.
DR   Bgee; ENSCHIG00000010392; Expressed in thymus and 17 other cell types or tissues.
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:SF42; HISTONE H2A TYPE 2-A; 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:UP000291000};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          5..89
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          92..125
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  13988 MW;  358AE20D1C531724 CRC64;
     MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT
     AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
     TESHKAKSK
//
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