ID   H13_CAEEL               Reviewed;         208 AA.
AC   Q19743;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Histone H1.3;
DE   AltName: Full=Histone H1-like protein 3;
GN   Name=hil-3; ORFNames=F22F1.1;
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 [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   [2]
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).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC       Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
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; AF012253; AAB66471.1; -; mRNA.
DR   EMBL; FO080273; CCD62510.1; -; Genomic_DNA.
DR   PIR; T16138; T16138.
DR   RefSeq; NP_509375.1; NM_076974.4.
DR   AlphaFoldDB; Q19743; -.
DR   SMR; Q19743; -.
DR   BioGRID; 45995; 2.
DR   STRING; 6239.F22F1.1; -.
DR   iPTMnet; Q19743; -.
DR   EPD; Q19743; -.
DR   PaxDb; Q19743; -.
DR   PeptideAtlas; Q19743; -.
DR   PRIDE; Q19743; -.
DR   EnsemblMetazoa; F22F1.1.1; F22F1.1.1; WBGene00001854.
DR   GeneID; 181073; -.
DR   KEGG; cel:CELE_F22F1.1; -.
DR   UCSC; F22F1.1; c. elegans.
DR   CTD; 181073; -.
DR   WormBase; F22F1.1; CE04443; WBGene00001854; hil-3.
DR   eggNOG; KOG4012; Eukaryota.
DR   GeneTree; ENSGT00970000195980; -.
DR   HOGENOM; CLU_052897_1_1_1; -.
DR   InParanoid; Q19743; -.
DR   OMA; VENNTQF; -.
DR   OrthoDB; 1565299at2759; -.
DR   PhylomeDB; Q19743; -.
DR   PRO; PR:Q19743; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001854; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P10771"
FT   CHAIN           2..208
FT                   /note="Histone H1.3"
FT                   /id="PRO_0000195983"
FT   DOMAIN          37..113
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          113..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..187
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10771"
SQ   SEQUENCE   208 AA;  21707 MW;  CCB20FBE08A3E250 CRC64;
     MSDTVVASAA VQAPAKTVKS PKAAKTTKVP KAKKPVAHPP YINMVTAAIN GLKERKGSSK
     IAILKYITKN YNVGDQIIKI NARLRDTLNK GVVSKALVQS VGTGASGRFR VTEKKAAAAK
     KPVAKKAATG EKKAKKPVAQ KAATGEKKAK KTTATKTKKT ADKVKKVKSP KKIAKPTAKK
     VAKSPAKKSA PKKAAAAKPA KKAVAPKT