General information | DisProt: | DP00057 | Name: | Sperm histone | Synonym(s): | HSP1_CHICK
Protamine
Galline
| First appeared in release: | Release 1.0 (08/01/2003) | UniProt: | P15340 | UniGene: | | SwissProt: | HSP1_CHICK | TrEMBL: | | NCBI (GI): | 123705 | Source organism: | Gallus gallus (Chicken) | Sequence length: | 62 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MARYRRSRTR SRSPRSRRRR RRSGRRRSPR RRRRYGSARR SRRSVGGRRR RYGSRRRRRR - 60 RY
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Functional narrative |
Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
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Map of ordered and disordered regions |


Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 62 | Length: | 62 | Region sequence: |
MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRR RY | Modification type: | Complex
Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | | Functional subclasses: | Metal binding
Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (DTT 0.1 mM; Jasco 500 (spectropolarimeter); scan speed 0.2 cm/min; sensitivity 0.5 m/cm; time constant 8 sec; Tris-HF (buffer) 10 mM; wavelength expansion 10 nm/cm)
| References:
- Gatewood JM, Schroth GP, Schmid CW, Bradbury EM. "Zinc-induced secondary structure transitions in human sperm protamines." J Biol Chem. 1990; 265(33): 20667-72. PubMed: 2243113
- Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T. "Conformation of the fowl protamine, galline, and its binding properties to DNA." J Biochem (Tokyo). 1989; 105(1): 133-7. PubMed: 2738040
| Comments:
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Comments |
This record is not able to be completed with the Nakano article which is no longer publicly available.
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