H6_ONCMY
ID H6_ONCMY Reviewed; 70 AA.
AC P02315; P83338;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Non-histone chromosomal protein H6;
DE Short=Histone T;
DE Contains:
DE RecName: Full=Oncorhyncin-3;
DE AltName: Full=Oncorhyncin III;
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 PROTEIN SEQUENCE OF 2-70.
RC TISSUE=Testis;
RX PubMed=456349; DOI=10.1111/j.1432-1033.1979.tb12953.x;
RA Watson D.C., Wong N.C.W., Dixon G.H.;
RT "The complete amino-acid sequence of a trout-testis non-histone protein,
RT H6, localized in a subset of nucleosomes and its similarity to calf-thymus
RT non-histone proteins HMG-14 and HMG-17.";
RL Eur. J. Biochem. 95:193-202(1979).
RN [2]
RP PROTEIN SEQUENCE OF 2-14, FUNCTION OF ONCORHYNCIN III, AND MASS
RP SPECTROMETRY OF 2-67.
RC TISSUE=Skin mucus;
RX PubMed=12713443; DOI=10.1042/bj20030259;
RA Fernandes J.M.O., Saint N., Kemp G.D., Smith V.J.;
RT "Oncorhyncin III: a potent antimicrobial peptide derived from the non-
RT histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss.";
RL Biochem. J. 373:621-628(2003).
CC -!- FUNCTION: Non-histone protein that probably binds to the inner side of
CC nucleosomal DNA, altering the association between the DNA and the
CC nucleosome octamer. {ECO:0000269|PubMed:12713443}.
CC -!- FUNCTION: Oncorhyncin III has antibacterial activity against Gram-
CC positive and Gram-negative bacteria at submicromolar concentrations.
CC {ECO:0000269|PubMed:12713443}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Oncorhyncin-3]: Secreted {ECO:0000305}.
CC -!- MASS SPECTROMETRY: [Oncorhyncin-3]: Mass=6671; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12713443};
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR PIR; A02653; NSTR6.
DR AlphaFoldDB; P02315; -.
DR GO; GO:0000785; C:chromatin; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:CAFA.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:AgBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:AgBase.
DR DisProt; DP00042; -.
DR InterPro; IPR000079; HMGN_fam.
DR Pfam; PF01101; HMG14_17; 1.
DR PRINTS; PR00925; NONHISHMG17.
DR SMART; SM00527; HMG17; 1.
DR PROSITE; PS00355; HMG14_17; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; DNA-binding; Nucleus;
KW Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12713443,
FT ECO:0000269|PubMed:456349"
FT CHAIN 2..70
FT /note="Non-histone chromosomal protein H6"
FT /id="PRO_0000013468"
FT CHAIN 2..67
FT /note="Oncorhyncin-3"
FT /id="PRO_0000013469"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 67..68
FT /note="Cleavage"
FT /evidence="ECO:0000305"
SQ SEQUENCE 70 AA; 7087 MW; 722FE4E829EC3D61 CRC64;
MPKRKSATKG DEPARRSARL SARPVPKPAA KPKKAAAPKK AVKGKKAAEN GDAKAEAKVQ
AAGDGAGNAK
