ID   H15_CAEEL               Reviewed;         225 AA.
AC   O01833;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Histone H1.5;
DE   AltName: Full=Histone H1-like protein 5;
GN   Name=hil-5; ORFNames=B0414.3;
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 [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}.
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DR   EMBL; AF005372; AAB81030.1; -; mRNA.
DR   EMBL; FO080197; CCD61899.1; -; Genomic_DNA.
DR   PIR; T15228; T15228.
DR   RefSeq; NP_491678.1; NM_059277.5.
DR   AlphaFoldDB; O01833; -.
DR   SMR; O01833; -.
DR   BioGRID; 37697; 1.
DR   STRING; 6239.B0414.3; -.
DR   iPTMnet; O01833; -.
DR   EPD; O01833; -.
DR   PaxDb; O01833; -.
DR   PeptideAtlas; O01833; -.
DR   PRIDE; O01833; -.
DR   EnsemblMetazoa; B0414.3.1; B0414.3.1; WBGene00001856.
DR   GeneID; 172242; -.
DR   KEGG; cel:CELE_B0414.3; -.
DR   UCSC; B0414.3; c. elegans.
DR   CTD; 172242; -.
DR   WormBase; B0414.3; CE07733; WBGene00001856; hil-5.
DR   eggNOG; KOG4012; Eukaryota.
DR   GeneTree; ENSGT00970000195980; -.
DR   HOGENOM; CLU_052897_1_1_1; -.
DR   InParanoid; O01833; -.
DR   OMA; KVMKTVA; -.
DR   OrthoDB; 1565299at2759; -.
DR   PRO; PR:O01833; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00001856; Expressed in germ line (C elegans) and 4 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..225
FT                   /note="Histone H1.5"
FT                   /id="PRO_0000195985"
FT   DOMAIN          37..113
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..171
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   225 AA;  23390 MW;  5EBC9EF74EA99AD2 CRC64;
     MSDVAVAETP AVKTPTKASK ATKAKATKIP KVKVVAAHPP FINMITEAVS NLKDRKGSSR
     VAIFKFITAK YTLGDQVNKT NAHLRSALKK GVVSKVLVQT NGIGANGRFR LAVAEKPPAV
     KKAATGEQKV MKTVAKKAVS GDKAKKTVAK KTGDKVKKVK SPKRIAKPAV KKVTKKAAAP
     TKSAANETAP KKAAATEAAP KKAAVTKAAT KKTPARKAVG TAPKA