Protein information for: OR2F2



MEIDNQTWVREFILLGLSSDWCTQISLFSLFLVTYLMTVLGNCLIVLLIR
LDSRLHTPMYFFLTNLSLVDVSYATSVVPQLLAHFLAEHKAIPFQSCAAQ
LFFSLALGGIEFVLLAVMAYDRHVAVSDRLRYSAIMHGGLCARLAITSWV
SGSINSLVQTAITFQLPMCTNKFIDHISCELLAVVRLACVDTSSNEAAIM
VSSIVLLMTPFCLVLLSYIRIISTILKIQSREGRKKAFHTCASHLTVVAL
CYGTTIFTYIQPHSGPSVLQEKLISVFYAIVMPLLNPVIYSLRNKEVKGA
WHKLLEKFSGLTSKLGT
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 24 50 QISLFSLFLVTYLMTVLGNCLIVLLIR
TM2 61 83 FFLTNLSLVDVSYATSVVPQLLA
TM3 98 118 AAQLFFSLALGGIEFVLLAVM
TM4 141 161 CARLAITSWVSGSINSLVQTA
TM5 198 219 AIMVSSIVLLMTPFCLVLLSYI
TM6 241 265 CASHLTVVALCYGTTIFTYIQPHSG
TM7 271 290 EKLISVFYAIVMPLLNPVIY

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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