ID   H13_RABIT               Reviewed;         213 AA.
AC   P02251;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Histone H1.3;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Cole R.D.;
RL   (In) Ts'o P.O.P. (eds.);
RL   The molecular biology of the mammalian genetic apparatus, pp.1:93-104,
RL   Elsevier, Amsterdam (1977).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-72, AND ACETYLATION AT SER-1.
RX   PubMed=5167020; DOI=10.1016/s0021-9258(19)45870-5;
RA   Rall S.C., Cole R.D.;
RT   "Amino acid sequence and sequence variability of the amino-terminal regions
RT   of lysine-rich histones.";
RL   J. Biol. Chem. 246:7175-7190(1971).
RN   [3]
RP   PROTEIN SEQUENCE OF 73-107.
RX   PubMed=4822503; DOI=10.1016/s0021-9258(19)42764-6;
RA   Jones G.M.T., Rall S.C., Cole R.D.;
RT   "Extension of the amino acid sequence of a lysine-rich histone.";
RL   J. Biol. Chem. 249:2548-2553(1974).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: H1 histones are progressively phosphorylated during the cell
CC       cycle, becoming maximally phosphorylated during late G2 phase and M
CC       phase, and being dephosphorylated sharply thereafter.
CC       {ECO:0000250|UniProtKB:P43275}.
CC   -!- PTM: Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the
CC       DNA-binding site of H1 and results in its displacement from chromatin
CC       and global chromatin decondensation, thereby promoting pluripotency and
CC       stem cell maintenance. {ECO:0000250|UniProtKB:P43277}.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
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DR   PIR; A94467; HSRB13.
DR   AlphaFoldDB; P02251; -.
DR   SMR; P02251; -.
DR   STRING; 9986.ENSOCUP00000012397; -.
DR   iPTMnet; P02251; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; Citrullination; Direct protein sequencing;
KW   DNA-binding; Hydroxylation; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..213
FT                   /note="Histone H1.3"
FT                   /id="PRO_0000195921"
FT   DOMAIN          37..110
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..166
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..213
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:5167020"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         35
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         53
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         55
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         65
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         86
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         91
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7MAZ5"
FT   MOD_RES         107
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
SQ   SEQUENCE   213 AA;  21423 MW;  21DE34BBD10D894E CRC64;
     SEAPAETAAP APAEKSPAKK KKAAKKPGAG AAKRKAAGPP VSELITKAVA ASKERNGLSL
     AALKKALAAG GYDVEKNNSR IKLGLKSLVS KGTLVETKGT GASGSFKLDK KAASGEAKPK
     PKKAGAAKPK KPAGATPKKP KKAAGAKKAV KKTPKKAPKP KAAAKPKVAK PKSPAKVAKS
     PKKAKAVKPK AAKPKAPKPK AAKAKKTAAK KKK