H33_MEDSA
ID H33_MEDSA Reviewed; 136 AA.
AC P69244; P11105;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Histone H3.3;
DE AltName: Full=Histone H3.2;
DE AltName: Full=Minor histone H3;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Chief, and cv. Regen S;
RA Robertson A.J.;
RT "Histone H3 genes in alfalfa.";
RL Thesis (1994), University of Missouri / Kansas City, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-136.
RC STRAIN=cv. Regen S;
RX PubMed=2471147; DOI=10.1093/nar/17.8.3057;
RA Wu S.C., Gyoergyey J., Dudits D.;
RT "Polyadenylated H3 histone transcripts and H3 histone variants in
RT alfalfa.";
RL Nucleic Acids Res. 17:3057-3063(1989).
RN [3]
RP ACETYLATION.
RX PubMed=3606121; DOI=10.1016/0003-9861(87)90435-8;
RA Waterborg J.H., Winicov I., Harrington R.E.;
RT "Histone variants and acetylated species from the alfalfa plant Medicago
RT sativa.";
RL Arch. Biochem. Biophys. 256:167-178(1987).
RN [4]
RP ACETYLATION, AND LACK OF PHOSPHORYLATION.
RX PubMed=16666742; DOI=10.1104/pp.90.1.237;
RA Waterborg J.H., Harrington R.E., Winicov I.;
RT "Differential histone acetylation in alfalfa (Medicago sativa) due to
RT growth in NaCl: responses in salt stressed and salt tolerant callus
RT cultures.";
RL Plant Physiol. 90:237-245(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-52 AND 85-95, ACETYLATION AT LYS-10; LYS-15; LYS-19;
RP LYS-24 AND LYS-28, LACK OF ACETYLATION AT LYS-37 AND LYS-38, METHYLATION AT
RP LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, AND LACK OF METHYLATION
RP AT LYS-37 AND LYS-38.
RC STRAIN=cv. R4;
RX PubMed=2211618; DOI=10.1016/s0021-9258(17)44882-4;
RA Waterborg J.H.;
RT "Sequence analysis of acetylation and methylation in two histone H3
RT variants of alfalfa.";
RL J. Biol. Chem. 265:17157-17161(1990).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes. Constitutes the predominant form
CC of histone H3 in non-dividing cells and is incorporated into chromatin
CC independently of DNA synthesis. Deposited at sites of nucleosomal
CC displacement throughout transcribed genes, suggesting that it
CC represents an epigenetic imprint of transcriptionally active chromatin.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC 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. Chromosome.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylated to
CC form H3K9ac (2%), H3K14 (37%), H3K18 (25%) and H3K23 (9%). Pre-existing
CC H3K9me or H3K27me limit the possibility for histone acetylation. H3.2
CC shows a much higher level of steady-state acetylation than H3.1.
CC Increased multiacetylation after exposure to NaCl.
CC -!- PTM: 24% of H3K4 is found under the form of H3K4me1, 6% of H3K4me2 and
CC 19% of H3K4me3. When not under the form of H3K9ac, H3K9 is found as
CC H3K9me1 (43%), H3K9me2 (9%) or H3K9me3 (15%). When not acetylated,
CC H3K14, H3K18 and H3K23 are only under the form of H3K14me3 (18%),
CC H3K18me3 (16%), and H3K23me3 (33%). 31% of H3K27 is found under the
CC form of H3K27me1, 24% of H3K27me2 and 38% of H3K27me3.
CC {ECO:0000269|PubMed:2211618}.
CC -!- PTM: Can be phosphorylated to form H3S10ph, H3T11ph and H3S28ph (By
CC similarity). No phosphorylation detected during salt stress.
CC {ECO:0000250}.
CC -!- PTM: No modifications detected on H3K36 and H3K37.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10;
CC H3K9me1/2/3 = mono-, di- and trimethylated Lys-10; H3S10ph =
CC phosphorylated Ser-11; H3T11ph = phosphorylated Thr-12; H3K14ac =
CC acetylated Lys-15; H3K14me3 = trimethylated Lys-15; H3K18ac =
CC acetylated Lys-19; H3K18me3 = trimethylated Lys-19; H3K23ac =
CC acetylated Lys-24; H3K23me3 = trimethylated Lys-24; H3K27me1/2/3 =
CC mono-, di- and trimethylated Lys-28; H3S28ph = phosphorylated Ser-29;
CC H3K36 = Lys-37; H3K37 = Lys-38. {ECO:0000305}.
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DR EMBL; U09458; AAB49538.1; -; Unassigned_DNA.
DR EMBL; U09460; AAB36493.1; -; mRNA.
DR EMBL; U09461; AAB36494.1; -; mRNA.
DR EMBL; U09464; AAB36497.1; -; mRNA.
DR EMBL; U09465; AAB36498.1; -; mRNA.
DR EMBL; X13676; CAA31967.1; -; mRNA.
DR PIR; B38309; B38309.
DR PIR; S04521; S04521.
DR AlphaFoldDB; P69244; -.
DR SMR; P69244; -.
DR iPTMnet; P69244; -.
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 Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211618"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000221285"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 37
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 37
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 38
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 38
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 19
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 24
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 15406 MW; 6D72383BF2E9EBE6 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PTTGGVKKPH RYRPGTVALR EIRKYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSHAV LALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
