ID   H1_SALTR                Reviewed;         194 AA.
AC   P02254;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Histone H1;
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT ALA-1, AND PHOSPHORYLATION AT SER-145;
RP   SER-161 AND SER-182.
RX   PubMed=913397; DOI=10.1111/j.1432-1033.1977.tb11739.x;
RA   McLeod A.R., Wong N.C.W., Dixon G.H.;
RT   "The amino-acid sequence of trout-testis histone H1.";
RL   Eur. J. Biochem. 78:281-291(1977).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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   AlphaFoldDB; P02254; -.
DR   SMR; P02254; -.
DR   iPTMnet; P02254; -.
DR   Proteomes; UP000472277; 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; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..194
FT                   /note="Histone H1"
FT                   /id="PRO_0000195937"
FT   DOMAIN          27..100
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..194
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylalanine; partial"
FT                   /evidence="ECO:0000269|PubMed:913397"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:913397"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:913397"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:913397"
FT   VARIANT         35
FT                   /note="A -> I (in minor component)"
SQ   SEQUENCE   194 AA;  19409 MW;  D288F9F44AF9BE7E CRC64;
     AEVAPAPAAA APAKAPKKKA AAKPKKSGPA VGELAGKAVA ASKERSGVSL AALKKSLAAG
     GYDVEKNNSR VKIAVKSLVT KGTLVETKGT GASGSFKLNK KAVEAKKPAK KAAAPKAKKV
     AAKKPAAAKK PKKVAAKKAV AAKKSPKKAK KPATPKKAAK SPKKATKAAK PKAAKPKKAA
     KSPKKVKKPA AAKK