ID   H1_SALSA                Reviewed;          55 AA.
AC   P84408; Q5GMQ6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Histone H1;
DE   Contains:
DE     RecName: Full=SAMP H1;
DE   Flags: Fragment;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION, AND
RP   ACETYLATION AT ALA-2.
RC   TISSUE=Skin mucus;
RX   PubMed=15917539; DOI=10.1128/aac.49.6.2399-2406.2005;
RA   Luders T., Birkemo G.A., Nissen-Meyer J., Andersen O., Nes I.F.;
RT   "Proline conformation-dependent antimicrobial activity of a proline-rich
RT   histone H1 N-terminal peptide fragment isolated from the skin mucus of
RT   Atlantic salmon.";
RL   Antimicrob. Agents Chemother. 49:2399-2406(2005).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures. {ECO:0000269|PubMed:15917539}.
CC   -!- FUNCTION: SAMP H1 has antibacterial activity against Gram-negative
CC       bacteria E.coli, A.salmonicida subsp salmonicida, V.anguillarum and
CC       S.typhimurium and Gram-positive bacteria B.subtilis and L.ivanovii.
CC       {ECO:0000269|PubMed:15917539}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SUBCELLULAR LOCATION: [SAMP H1]: Secreted.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
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DR   EMBL; AJ877042; CAI46350.1; -; Genomic_DNA.
DR   AlphaFoldDB; P84408; -.
DR   SMR; P84408; -.
DR   iPTMnet; P84408; -.
DR   Proteomes; UP000087266; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0042742; P:defense response to bacterium; IDA:AgBase.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005818; Histone_H1/H5_H15.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Nucleus; Reference proteome;
KW   Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15917539"
FT   CHAIN           2..>55
FT                   /note="Histone H1"
FT                   /id="PRO_0000013158"
FT   PEPTIDE         2..31
FT                   /note="SAMP H1"
FT                   /id="PRO_0000013159"
FT   DOMAIN          28..55
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:15917539"
FT   NON_TER         55
SQ   SEQUENCE   55 AA;  5320 MW;  F3E5A9E15C821155 CRC64;
     MAEVAPAPAA AAPAKAPKKK AAAKPKKAGP SVGELIVKAV SASKERSGVS LAALK