ID A0A1S3WQL1_ERIEU Unreviewed; 384 AA.
AC A0A1S3WQL1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Histone H3.1 {ECO:0000256|ARBA:ARBA00040190};
GN Name=LOC103123927 {ECO:0000313|RefSeq:XP_016048653.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016048653.1};
RN [1] {ECO:0000313|RefSeq:XP_016048653.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_016048653.1; XM_016193167.1.
DR AlphaFoldDB; A0A1S3WQL1; -.
DR STRING; 9365.ENSEEUP00000002495; -.
DR InParanoid; A0A1S3WQL1; -.
DR OrthoDB; 5319100at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 1.10.20.10; Histone, subunit A; 2.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; HISTONE H3; 1.
DR PANTHER; PTHR11426:SF242; HISTONE H3.1; 1.
DR Pfam; PF00125; Histone; 2.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 2.
DR SUPFAM; SSF47113; Histone-fold; 2.
DR PROSITE; PS00322; HISTONE_H3_1; 2.
DR PROSITE; PS00959; HISTONE_H3_2; 2.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT DOMAIN 1..132
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT DOMAIN 249..380
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43570 MW; 8E26696D97549FE7 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERGYRWV SSNINPIPEK DQYSLVINDS LVSCYCVRDQ EMFRKDRKIC
QITKATCHDT ELTFRAEELI SCLSVIYLEL VYLVTALVPS DTACLASSPG SSRRTAVWIS
LENPRLYVMA RTKQTARKST GGKAPRKQLA TKAARKSAPA TGGVKKPHRY RPGTVALREI
RRYQKSTELL IRKLPFQRLV REIAQDFKTD LRFQSSAVMA LQEACEAYLV GLFEDTNLCA
IHAKRVTIMP KDIQLARRIR GERA
//
