DP00186: Late embryogenesis abundant protein 1FASTA viewXML view

General information
DisProt:DP00186
Name:Late embryogenesis abundant protein 1
Synonym(s):LEA1_APHAV
AavLea1
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q95V77
UniGene: 
SwissProt: LEA1_APHAV
TrEMBL:  
NCBI (GI): 24418520
Source organism:Aphelenchus avenae (Mycophagous nematode worm)
Sequence length:143
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSSQQNQNRQ GEQQEQGYME AAKEKVVNAW ESTKETLSST AQAAAEKTAE FRDSAGETIR - 60
DLTGQAQEKG QEFKERAGEK AEETKQRAGE KMDETKQRAG EMRENAGQKM EEYKQQGKGK - 120
AEELRDTAAE KLHQAGEKVK GRD



Functional narrative    

"LEA proteins were first identified 20 years ago in cotton and wheat and are produced in abundance during seed development, comprising up to 4% of cellular protein. Since then, up to five different groups of LEA proteins have been defined on the basis of expression pattern and sequence. Precise functions of the LEA proteins have yet to be elucidated, but expression is linked to water stress and the acquisition of desiccation tolerance in orthodox seeds, pollen, and anhydrobiotic plants. They have been variously proposed to protect cellular structures from the effects of water loss by action as a hydration buffer, by sequestration of ions, by direct protection of other proteins or membranes, or by renaturation of unfolded proteins, although supporting evidence is limited.... Genome sequencing projects have brought to light sequences related to Group 3 LEA proteins in the nematode Caenorhabditis elegans and also in the prokaryotes Haemophilus influenzae and Deinococcus radiodurans, indicating that this type of LEA protein at least is not restricted to plant species.... The function of non-plant LEA proteins may also relate to water stress...." (Goyal et al. 2003)

Region 1: 1-143

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 - 143
Length:143
Region sequence:

MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIR
DLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGK
AEELRDTAAEKLHQAGEKVKGRD

Modification type: Native
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Entropic chain
Functional subclasses: Molecular shield
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (pH: 7; 0.1 and 2 mg/ml of AavLEA1 in 50 mM phosphate buffer; 0.1-cm path length)

  2. Fluorescence polarization/anisotropy (0.1 and 0.5 mg/ml AavLEA1; Excitation wavelength of 280 nm; Scan rate of 60 nm/min; Slit widths of 2.5 nm)

  3. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (298 K; Protein (15 mg/ml))
References:
  1. Chakrabortee S, Tripathi R, Watson M, Schierle GS, Kurniawan DP, Kaminski CF, Wise MJ, Tunnacliffe A. "Intrinsically disordered proteins as molecular shields." Mol Biosyst. 2011; 8(1): 210-9. PubMed: 21909508

  2. Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A. "Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein." J Biol Chem. 2003; 278(15): 12977-84. PubMed: 12569097
Comments:
Chakrabortee et al (2012) discuss a possible new functional subclass for LEA proteins, that of "molecular shield."

Molecular shield: entropic chain that forms a physical barrier around a target protein thereby reducing interactions that lead to aggregation, i.e. dessication tolerance provided by LEA proteins.


References

  1. Chakrabortee S, Tripathi R, Watson M, Schierle GS, Kurniawan DP, Kaminski CF, Wise MJ, Tunnacliffe A. "Intrinsically disordered proteins as molecular shields." Mol Biosyst. 2011; 8(1): 210-9. PubMed: 21909508

  2. Wise MJ, Tunnacliffe A. "POPP the question: what do LEA proteins do?" Trends Plant Sci. 2004; 9(1): 13-7. PubMed: 14729214


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