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


DP00276: Membrane fusion protein p14FASTA viewXML view

General information
DisProt:DP00276
Name:Membrane fusion protein p14
Synonym(s):Q80FJ1_9REOV
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q80FJ1
UniGene: 
SwissProt: Q80FJ1_9REOV
TrEMBL:  
NCBI (GI): 75564240
Source organism:Reptilian orthoreovirus
Sequence length:125
Percent disordered:24%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MGSGPSNFVN HAPGEAIVTG LEKGADKVAG TISHTIWEVI AGLVALLTFL AFGFWLFKYL - 60
QKRRERRRQL TEFQKRYLRN SYRLSEIQRP ISQHEYEDPY EPPSRRKPPP PPYSTYVNID - 120
NVSAI

Region 1: 2-14 Region 2: 15-31

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:2 - 14
Length:13
Region sequence:

GSGPSNFVNHAPG

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; protein (10-80 uM in water))

  2. Nuclear magnetic resonance (NMR) (278 K; pH: 7.2; 1H2O 90 %; 2H2O 10 %; lyophilized acetyl-p14 peptide 5 mg; potassium phosphate (buffer) 50 mM)

  3. Nuclear magnetic resonance (NMR) (278 K; pH: 7.2; 1H2O 90 %; 2H2O 10 %; myristoylated p14 peptide 0.5 mg; potassium phosphate (buffer) 50 mM)
References:
  1. Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. "Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif." J Biol Chem. 2004; 279(49): 51386-94. PubMed: 15448165
Comments:
This region contains an extended "loop structure" comprising residues Pro5 to Pro13.


Region 2
Type:Disordered
Name: 
Location:15 - 31
Length:17
Region sequence:

EAIVTGLEKGADKVAGT

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Entropic chain
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; protein (10-80 uM in water))

  2. Nuclear magnetic resonance (NMR) (278 K; pH: 7.2; 1H2O 90 %; 2H2O 10 %; lyophilized acetyl-p14 peptide 5 mg; potassium phosphate (buffer) 50 mM)

  3. Nuclear magnetic resonance (NMR) (278 K; pH: 7.2; 1H2O 90 %; 2H2O 10 %; myristoylated p14 peptide 0.5 mg; potassium phosphate (buffer) 50 mM)
References:
  1. Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. "Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif." J Biol Chem. 2004; 279(49): 51386-94. PubMed: 15448165
Comments:
 


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