H33_CHLRE
ID H33_CHLRE Reviewed; 135 AA.
AC P50564;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Histone H3 type 3;
GN Name=ch3-IV;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=7479007; DOI=10.1093/nar/23.18.3756;
RA Walther Z., Hall J.L.;
RT "The uni chromosome of Chlamydomonas: histone genes and nucleosome
RT structure.";
RL Nucleic Acids Res. 23:3756-3763(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, AND METHYLATION AT LYS-5.
RX PubMed=16100335; DOI=10.1105/tpc.105.034165;
RA van Dijk K., Marley K.E., Jeong B.-R., Xu J., Hesson J., Cerny R.L.,
RA Waterborg J.H., Cerutti H.;
RT "Monomethyl histone H3 lysine 4 as an epigenetic mark for silenced
RT euchromatin in Chlamydomonas.";
RL Plant Cell 17:2439-2453(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-49, ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND
RP LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-28; LYS-36 AND LYS-37, AND LACK
RP OF PHOSPHORYLATION.
RX PubMed=7480339; DOI=10.1104/pp.109.2.393;
RA Waterborg J.H., Robertson A.J., Tatar D.L., Borza C.M., Davie J.R.;
RT "Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and
RT methylation.";
RL Plant Physiol. 109:393-407(1995).
RN [4]
RP ACETYLATION.
RX PubMed=9765294; DOI=10.1074/jbc.273.42.27602;
RA Waterborg J.H.;
RT "Dynamics of histone acetylation in Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 273:27602-27609(1998).
RN [5]
RP METHYLATION AT LYS-10.
RX PubMed=17251191; DOI=10.1093/nar/gkl1149;
RA Casas-Mollano J.A., van Dijk K., Eisenhart J., Cerutti H.;
RT "SET3p monomethylates histone H3 on lysine 9 and is required for the
RT silencing of tandemly repeated transgenes in Chlamydomonas.";
RL Nucleic Acids Res. 35:939-950(2007).
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. Acetylated to
CC form H3K9ac (11%), H3K14ac (17%), H3K18ac (11%), H3K23ac (16%) and
CC H3K27ac (7%). H3K4, H3K35 and H3K36 are not acetylated. H3K4me prevents
CC acetylation. 32% of the histone H3 are acetylated with, on average, 2.4
CC acetyl-Lys. They are all continuously deacatylated and re-acetylated
CC with a half-life of approximately 2 min. {ECO:0000269|PubMed:7480339,
CC ECO:0000269|PubMed:9765294}.
CC -!- PTM: Monomethylated to form H3K4me1 (81%), H3K9me1 (16%), H3K27me1
CC (25%), H3K35me1 (25%) and H3K36me1 (5%). No methylation at H3K14, H3K18
CC and H3K23. Methylated by a protein complex that includes Mut11. Set1
CC methylates specifically H3K4. H3K4me1 is associated with silenced
CC euchromatin. Set3 forms H3K9me1, while H3K9me2 is undetected. H3K9me1
CC is specifically associated with silent, multi-copy transgenes.
CC {ECO:0000269|PubMed:16100335, ECO:0000269|PubMed:17251191,
CC ECO:0000269|PubMed:7480339}.
CC -!- PTM: No phosphorylation detected.
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: H3K4 = Lys-5;
CC H3K4me = methylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me =
CC methylated Lys-10; H3S10ph = phosphorylated Ser-11; H3T11ph =
CC phosphorylated Thr-12; H3K14 = Lys-15; H3K14ac = acetylated Lys-15;
CC H3K18 = Lys-19; H3K18ac = acetylated Lys-19; H3K23 = Lys-24; H3K23ac =
CC acetylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me = methylated
CC Lys-28; H3K35 = Lys-36; H3K35me = methylated Lys-36; H3K36 = Lys-37;
CC H3K36me = methylated Lys-37. {ECO:0000305}.
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DR EMBL; L41841; AAA99965.1; -; Genomic_DNA.
DR PIR; S59123; S59123.
DR AlphaFoldDB; P50564; -.
DR SMR; P50564; -.
DR iPTMnet; P50564; -.
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:16100335,
FT ECO:0000269|PubMed:7480339"
FT CHAIN 2..135
FT /note="Histone H3 type 3"
FT /id="PRO_0000221272"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 5
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT SITE 15
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT SITE 19
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT SITE 24
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT SITE 36
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT SITE 37
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:16100335,
FT ECO:0000269|PubMed:7480339"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17251191,
FT ECO:0000269|PubMed:7480339"
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-acetyllysine"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 36
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:7480339"
FT MOD_RES 37
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:7480339"
SQ SEQUENCE 135 AA; 15260 MW; D728F7FEC8FBA81E CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKTP ATGGVKKPHR YRPGTVALRE IRKYQKSTEL
LIRKLPFQRL VREIAQDFKT DLRFQSQAVV ALQEAAEAYL VGLFEDTNLC AITAKRVTIM
PKDIQLARRI RGERA
