H3_ACRFO
ID H3_ACRFO Reviewed; 136 AA.
AC P22843;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Histone H3;
OS Acropora formosa (Staghorn coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Acropora.
OX NCBI_TaxID=126732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1977663; DOI=10.1016/0378-1119(90)90243-k;
RA Miller D.J., McMillan J., Miles A., ten Lohuis M., Mahony T.;
RT "Nucleotide sequence of the histone H3-encoding gene from the scleractinian
RT coral Acropora formosa (Cnidaria: Scleractinia).";
RL Gene 93:319-320(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7901422; DOI=10.1007/bf00175501;
RA Miller D.J., Harrison P.L., Mahony T.J., McMillan J.P., Miles A.,
RA Odorico D.M., ten Lohuis M.R.;
RT "Nucleotide sequence of the histone gene cluster in the coral Acropora
RT formosa (Cnidaria; Scleractinia): features of histone gene structure and
RT organization are common to diploblastic and triploblastic metazoans.";
RL J. Mol. Evol. 37:245-253(1993).
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.
CC -!- PTM: Methylation at Lys-5 is linked to gene activation. Methylation at
CC Lys-10 is linked to gene repression (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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 EMBL; M60509; AAA64958.1; -; Genomic_DNA.
DR EMBL; L11067; AAC37352.1; -; Genomic_DNA.
DR EMBL; S67324; AAB28736.1; -; Genomic_DNA.
DR PIR; JQ0757; JQ0757.
DR PDB; 6LSB; X-ray; 2.00 A; B=2-26.
DR PDBsum; 6LSB; -.
DR AlphaFoldDB; P22843; -.
DR BMRB; P22843; -.
DR SMR; P22843; -.
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 Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3"
FT /id="PRO_0000221296"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:6LSB"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:6LSB"
SQ SEQUENCE 136 AA; 15285 MW; F5733D26468DAED0 CRC64;
MARTKQTARK STGGKAPRKQ LATKAAAKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV LALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
