ID   H1_ONCMY                Reviewed;         207 AA.
AC   P06350; P83374;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Histone H1;
DE   Contains:
DE     RecName: Full=Oncorhyncin II;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6443128; DOI=10.1007/bf02102355;
RA   Mezquita J., Connor W., Winkfein R.J., Dixon G.H.;
RT   "An H1 histone gene from rainbow trout (Salmo gairdnerii).";
RL   J. Mol. Evol. 21:209-219(1984).
RN   [2]
RP   PROTEIN SEQUENCE OF 139-155, FUNCTION OF ONCORHYNCIN II, AND MASS
RP   SPECTROMETRY OF 139-207.
RC   TISSUE=Skin mucus;
RX   PubMed=12969798; DOI=10.1016/s0145-305x(03)00120-4;
RA   Fernandes J.M.O., Molle G., Kemp G.D., Smith V.J.;
RT   "Isolation and characterisation of oncorhyncin II, a histone H1-derived
RT   antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus
RT   mykiss.";
RL   Dev. Comp. Immunol. 28:127-138(2004).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures. {ECO:0000269|PubMed:12969798}.
CC   -!- FUNCTION: Oncorhyncin II has antibacterial activity against Gram-
CC       positive and Gram-negative bacteria at submicromolar concentrations.
CC       Potentially important role in mucosal defense.
CC       {ECO:0000269|PubMed:12969798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable up to 80 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SUBCELLULAR LOCATION: [Oncorhyncin II]: Secreted.
CC   -!- TISSUE SPECIFICITY: Oncorhyncin II is expressed in skin.
CC   -!- MASS SPECTROMETRY: [Oncorhyncin II]: Mass=7195.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12969798};
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
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DR   EMBL; X02624; CAB37646.1; -; Genomic_DNA.
DR   PIR; A02584; HSTR1R.
DR   AlphaFoldDB; P06350; -.
DR   SMR; P06350; -.
DR   Ensembl; ENSOMYT00000153437; ENSOMYP00000113727; ENSOMYG00000062148.
DR   Ensembl; ENSOMYT00000158950; ENSOMYP00000133133; ENSOMYG00000071152.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Nucleus; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..207
FT                   /note="Histone H1"
FT                   /id="PRO_0000013156"
FT   CHAIN           139..207
FT                   /note="Oncorhyncin II"
FT                   /id="PRO_0000013157"
FT   DOMAIN          28..101
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   REGION          105..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..207
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            138..139
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  20803 MW;  49D80EFF9C28E18B CRC64;
     MAEVAPAPAA AAPAKAPKKK AAAKPKKAGP SVGELIVKAV SASKERSGVS LAALKKSLAA
     GGYDVEKNNS RVKIAVKSLV TKGTLVQTKG TGASGSFKLN KKAVEAKKPA KKAAAPKAKK
     VAAKKPAAAK KPKKVAAKKA VAAKKSPKKA KKPATPKKAA KSPKKVKKPA AAAKKAAKSP
     KKATKAAKPK AAKPKAAKAK KAAPKKK