ID   H10_BOVIN               Reviewed;         194 AA.
AC   Q0IIJ2;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Histone H1.0;
DE   AltName: Full=Histone H1(0);
DE   Contains:
DE     RecName: Full=Histone H1.0, N-terminally processed;
GN   Name=H1-0;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures. The histones H1.0 are found in
CC       cells that are in terminal stages of differentiation or that have low
CC       rates of cell division (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC       Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC   -!- PTM: ADP-ribosylated on Ser-104 in response to DNA damage.
CC       {ECO:0000250|UniProtKB:P07305}.
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; BC122613; AAI22614.1; -; mRNA.
DR   RefSeq; NP_001069955.1; NM_001076487.1.
DR   AlphaFoldDB; Q0IIJ2; -.
DR   SMR; Q0IIJ2; -.
DR   BioGRID; 545568; 1.
DR   STRING; 9913.ENSBTAP00000049194; -.
DR   PaxDb; Q0IIJ2; -.
DR   PeptideAtlas; Q0IIJ2; -.
DR   PRIDE; Q0IIJ2; -.
DR   GeneID; 617975; -.
DR   KEGG; bta:617975; -.
DR   CTD; 3005; -.
DR   eggNOG; KOG4012; Eukaryota.
DR   HOGENOM; CLU_052897_1_1_1; -.
DR   InParanoid; Q0IIJ2; -.
DR   OrthoDB; 1565299at2759; -.
DR   TreeFam; TF313664; -.
DR   Proteomes; UP000009136; Unplaced.
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; ADP-ribosylation; Chromosome; Citrullination; DNA-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..194
FT                   /note="Histone H1.0"
FT                   /id="PRO_0000423206"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07305"
FT   CHAIN           2..194
FT                   /note="Histone H1.0, N-terminally processed"
FT                   /id="PRO_0000259963"
FT   DOMAIN          24..97
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..194
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P07305"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine; in Histone H1.0, N-terminally
FT                   processed"
FT                   /evidence="ECO:0000250|UniProtKB:P07305"
FT   MOD_RES         42
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:P43275"
FT   MOD_RES         104
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07305"
SQ   SEQUENCE   194 AA;  20951 MW;  18C94D66DAE17705 CRC64;
     MTENSTSTPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
     GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKRSVAFKKT KKEVKKVATP
     KKAAKPKKAA SKAPSKKPKA TPVKKAKKKP AATPKKTKKP KTVKAKPVKA SKPKKTKPVK
     PKAKSSAKRT GKKK