| First appeared in release:||Release 1.0 (08/01/2003)|
|SwissProt: ||HSP1_CHICK |
|TrEMBL: || |
|NCBI (GI): ||123705 |
|Source organism:||Gallus gallus (Chicken)|
10 20 30 40 50 60
| | | | | |
MARYRRSRTR SRSPRSRRRR RRSGRRRSPR RRRRYGSARR SRRSVGGRRR RYGSRRRRRR - 60
|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.
|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.
|Location:||1 - 62|
|Modification type: ||Complex |
|PDB: || |
|Structural/functional type: ||Function arises via a disorder to order transition |
|Functional classes: || |
|Functional subclasses: ||Metal 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)
- 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
This record is not able to be completed with the Nakano article which is no longer publicly available.
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