H3_PSAMI
ID H3_PSAMI Reviewed; 136 AA.
AC P69076; P02298; P05320; P05321; P05322;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Histone H3, embryonic;
OS Psammechinus miliaris (Green sea urchin) (Echinus miliaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Parechinidae;
OC Psammechinus.
OX NCBI_TaxID=7660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H22).
RX PubMed=688387; DOI=10.1016/0092-8674(78)90249-0;
RA Schaffner W., Kunz G., Daetwyler H., Telford J., Smith H.O.,
RA Birnstiel M.L.;
RT "Genes and spacers of cloned sea urchin histone DNA analyzed by
RT sequencing.";
RL Cell 14:655-671(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H22).
RA Birnstiel M.L., Portmann R., Busslinger M., Schaffner W., Probst E.,
RA Kressmann A.;
RT "Functional organization of the histone genes in the sea urchin
RT Psammechinus: a progress report.";
RL Proc. Alfred Benzon Symp. 13:117-132(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H19).
RX PubMed=7443547; DOI=10.1093/nar/8.5.957;
RA Busslinger M., Portmann R., Irminger J.C., Birnstiel M.L.;
RT "Ubiquitous and gene-specific regulatory 5' sequences in a sea urchin
RT histone DNA clone coding for histone protein variants.";
RL Nucleic Acids Res. 8:957-977(1980).
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 -!- DEVELOPMENTAL STAGE: This histone is expressed during late embryonic
CC development.
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}.
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DR EMBL; J01181; AAB59206.1; -; Genomic_DNA.
DR EMBL; X01345; CAA25632.1; -; Genomic_DNA.
DR EMBL; V01143; CAA24375.1; -; Genomic_DNA.
DR EMBL; V01144; CAA24382.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M10558; AAA30026.1; -; Genomic_DNA.
DR PIR; C90776; HSUR3M.
DR AlphaFoldDB; P69076; -.
DR SMR; P69076; -.
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 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3, embryonic"
FT /id="PRO_0000221316"
FT REGION 1..43
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"
SQ SEQUENCE 136 AA; 15402 MW; CFD9518EA50A0F2A CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TELRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
