Annotation for this protein is in progress - please check future releases for more complete information



DP00057: Sperm histoneFASTA viewXML view

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



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.

Region 1: 1-62

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.


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:
  1. 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:
  1. 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

  2. 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:
 



Comments


This record is not able to be completed with the Nakano article which is no longer publicly available.


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