H24_CAEEL
ID H24_CAEEL Reviewed; 208 AA.
AC P10771; Q93901;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histone 24 {ECO:0000312|WormBase:M163.3};
DE AltName: Full=Histone H1.1 {ECO:0000312|WormBase:M163.3};
GN Name=his-24 {ECO:0000312|WormBase:M163.3};
GN Synonyms=H1.1 {ECO:0000312|WormBase:M163.3},
GN HH1 {ECO:0000312|WormBase:M163.3};
GN ORFNames=M163.3 {ECO:0000312|WormBase:M163.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1969492; DOI=10.1016/0022-2836(90)90123-4;
RA Sanicola M., Ward S., Childs G., Emmons S.W.;
RT "Identification of a Caenorhabditis elegans histone H1 gene family.
RT Characterization of a family member containing an intron and encoding a
RT poly(A)+ mRNA.";
RL J. Mol. Biol. 212:259-268(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=him-8;
RX PubMed=11245572; DOI=10.1242/dev.128.7.1069;
RA Jedrusik M.A., Schulze E.;
RT "A single histone H1 isoform (H1.1) is essential for chromatin silencing
RT and germline development in Caenorhabditis elegans.";
RL Development 128:1069-1080(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP PROTEIN SEQUENCE OF 2-208, AND ACETYLATION AT SER-2.
RC STRAIN=Bristol N2;
RX PubMed=3202838;
RA Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
RT "The primary structure of the major isoform (H1.1) of histone H1 from the
RT nematode Caenorhabditis elegans.";
RL Biochem. J. 255:647-652(1988).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, METHYLATION AT LYS-14, AND MUTAGENESIS OF
RP LYS-14.
RX PubMed=22083954; DOI=10.1128/mcb.05229-11;
RA Studencka M., Konzer A., Moneron G., Wenzel D., Opitz L.,
RA Salinas-Riester G., Bedet C., Krueger M., Hell S.W., Wisniewski J.R.,
RA Schmidt H., Palladino F., Schulze E., Jedrusik-Bode M.;
RT "Novel roles of Caenorhabditis elegans heterochromatin protein HP1 and
RT linker histone in the regulation of innate immune gene expression.";
RL Mol. Cell. Biol. 32:251-265(2012).
RN [6]
RP FUNCTION, INTERACTION WITH HPL-1 AND HISTONE H3, AND METHYLATION AT LYS-14.
RX PubMed=23028351; DOI=10.1371/journal.pgen.1002940;
RA Studencka M., Wesolowski R., Opitz L., Salinas-Riester G., Wisniewski J.R.,
RA Jedrusik-Bode M.;
RT "Transcriptional repression of Hox genes by C. elegans HP1/HPL and H1/HIS-
RT 24.";
RL PLoS Genet. 8:e1002940-e1002940(2012).
RN [7]
RP INTERACTION WITH NMAD-1.
RX PubMed=31283754; DOI=10.1371/journal.pgen.1008252;
RA Wang S.Y., Mao H., Shibuya H., Uzawa S., O'Brown Z.K., Wesenberg S.,
RA Shin N., Saito T.T., Gao J., Meyer B.J., Colaiacovo M.P., Greer E.L.;
RT "The demethylase NMAD-1 regulates DNA replication and repair in the
RT Caenorhabditis elegans germline.";
RL PLoS Genet. 15:E1008252-E1008252(2019).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures (Probable) (PubMed:23028351).
CC Probably does not act as global transcriptional repressor
CC (PubMed:23028351). Acting in concert with chromobox protein homologs
CC hpl-1 and hpl-2, involved in reproduction, somatic gonad development,
CC male tail development, and vulval cell fate decisions; perhaps as a
CC result of modulating expression of Hox genes mab-5 and egl-5
CC (PubMed:23028351). Plays a role in linking epigenetic regulation with
CC the innate immune response (PubMed:22083954).
CC {ECO:0000269|PubMed:22083954, ECO:0000269|PubMed:23028351,
CC ECO:0000305|PubMed:3202838}.
CC -!- SUBUNIT: Interacts with nmad-1 (PubMed:31283754). Interacts (when
CC monomethylated at Lys-14) with chromobox protein homolog hpl-1; the
CC interaction is direct (PubMed:23028351). Interacts (when monomethylated
CC at Lys-14) with histone H3 (when trimethylated on 'Lys-27'); the
CC interaction is direct (PubMed:23028351). {ECO:0000269|PubMed:23028351,
CC ECO:0000269|PubMed:31283754}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22083954}. Chromosome
CC {ECO:0000269|PubMed:22083954, ECO:0000305|PubMed:3202838}. Cytoplasm
CC {ECO:0000269|PubMed:22083954}. Note=Cytoplasmic localization is
CC observed after infection with Gram-positive bacterium B.thuringiensis.
CC {ECO:0000269|PubMed:22083954}.
CC -!- PTM: Methylation at lysine 14 is necessary to regulate male tail
CC development. {ECO:0000269|PubMed:23028351}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X53277; CAA37372.1; -; Genomic_DNA.
DR EMBL; AF017810; AAB70665.1; -; mRNA.
DR EMBL; BX284606; CAB01892.1; -; Genomic_DNA.
DR PIR; T23778; T23778.
DR RefSeq; NP_510410.1; NM_078009.4.
DR AlphaFoldDB; P10771; -.
DR SMR; P10771; -.
DR BioGRID; 46444; 18.
DR IntAct; P10771; 1.
DR STRING; 6239.M163.3; -.
DR iPTMnet; P10771; -.
DR EPD; P10771; -.
DR PaxDb; P10771; -.
DR PRIDE; P10771; -.
DR EnsemblMetazoa; M163.3.1; M163.3.1; WBGene00001898.
DR GeneID; 181545; -.
DR KEGG; cel:CELE_M163.3; -.
DR UCSC; M163.3; c. elegans.
DR CTD; 181545; -.
DR WormBase; M163.3; CE12450; WBGene00001898; his-24.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_1_1_1; -.
DR InParanoid; P10771; -.
DR OMA; PRYSEMI; -.
DR OrthoDB; 1565299at2759; -.
DR PRO; PR:P10771; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001898; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3202838"
FT CHAIN 2..208
FT /note="Histone 24"
FT /id="PRO_0000195981"
FT DOMAIN 37..113
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 101..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:3202838"
FT MOD_RES 14
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:22083954"
FT MUTAGEN 14
FT /note="K->A: Reduced survival as a result of infection with
FT Gram-positive bacterium B.thuringiensis."
FT /evidence="ECO:0000269|PubMed:22083954"
FT CONFLICT 44
FT /note="M -> T (in Ref. 1; CAA37372 and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> H (in Ref. 1; CAA37372)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> R (in Ref. 1; CAA37372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 21367 MW; EF6C0D5DE5368CFE CRC64;
MSDSAVVAAA VEPKVPKAKA AKAAKPTKVA KAKAPVAHPP YINMIKEAIK QLKDRKGASK
QAILKFISQN YKLGDNVIQI NAHLRQALKR GVTSKALVQA AGSGANGRFR VPEKAAAAKK
PAAAKKPAAA KKPAAAKKAT GEKKAKKPAA AKPKKAATGD KKVKKAKSPK KVAKPAAKKV
AKSPAKKAAP KKIAKPAAKK AAKPAAKA
