Protein information for: OR2G6



STRANDLENGTHMEETNNSSEKGFLLLGFSDQPQLERFLFAIILYFYVLS
LLGNTALILVCCLDSRLHTPMYFFLSNLSCVDICFTTSVAPQLLVTMNKK
DKTMSYGGCVAQLYVAMGLGSSECILLAVMAYDRYAAVCRPLRYIAIMHP
RFCASLAGGAWLSGLITSLIQCSLTVQLPLCGHRTLDHIFCEVPVLIKLA
CVDTTFNEAELFVASVVFLIVPVLLILVSYGFITQAVLRIKSAAGRQKAF
GTCSSHLVVVIIFYGTIIFMYLQPANRRSKNQGKFVSLFYTIVTPLLNPI
IYTLRNKDVKGALRTLILGSAAGQSHKD
In red: predicted N-glycosylation site.
In magenta: Conserved cysteines that are predicted to form a disulfide bond.
Underlined and bold: TM regions.

Predicted binding site residues (CDRs) are highlighted according to the following amino acid color code:
| | basic (H,R,K)
| | hydrophilic, no charge (Q,N,T,S)
| | aliphatic (M,A,I,L,V)
| | aromatic (F,Y,W)
| | helix breakers (G,P)
| | acidic (D,E)
| | cysteine (C)

Sequences of the TM regions:

TM

Start position

End position

Sequence

TM1 36 62 ERFLFAIILYFYVLSLLGNTALILVCC
TM2 73 95 FFLSNLSCVDICFTTSVAPQLLV
TM3 110 130 VAQLYVAMGLGSSECILLAVM
TM4 153 173 CASLAGGAWLSGLITSLIQCS
TM5 210 231 ELFVASVVFLIVPVLLILVSYG
TM6 253 277 CSSHLVVVIIFYGTIIFMYLQPANR
TM7 283 302 GKFVSLFYTIVTPLLNPIIY

The information was derived from a multiple alignment of ORs, based on the algorithms of Man et al. Protein Sci. 2004 Jan;13(1):240-54.
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