Protein information for: OR52Q1P



CFKPIXKNSTLFIISKFQGCXRXVFIHSHFICXLSIFIGGNXXKCXLPLT
XACPLLLSYLPVQRQGNSFWCFPCLLQMFMTYLCTGLESGVLIILAIDHY
VVIRNPLRYTMILMNNVVAILGSHDNXIFNLYHLLLSLLILLLSFCAAHI
IPHTKCEHMGIAHLSCASIRANNMFGMVAFLWDLLTLLQLVSPMXRNYTL
FHLPPWNGQFEALNTCGSHVCHAHLLHPSSFCFXYTAWXKHPCYIRIFLA
NVYTVVLPVFNPVIYGIRKKQIPDXGIDLKTF
No N-glycosylation site was found.
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 2 26 FKPIXKNSTLFIISKFQGCXRXVFI
TM2 36 58 IFIGGNXXKCXLPLTXACPLLLS
TM3 75 95 LLQMFMTYLCTGLESGVLIIL
TM4 119 139 AILGSHDNXIFNLYHLLLSLL
TM5 175 196 FGMVAFLWDLLTLLQLVSPMXR
TM6 216 240 CGSHVCHAHLLHPSSFCFXYTAWXK
TM7 246 264 IFLANVYTVVLPVFNPVIY

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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