Protein information for: OR9Q2



MAERNYTVVTEFFLTAFTEHLQWRVPLFLIFLSFYLATMLGNTGMILLIR
GDRRLHTPMYFFLSHLSLVDICYSSAIIPQMLAVLWEHGTTISQARCAAQ
FFLFTFFASIDCYLLAIMAYDRYTAVCQPLLYVTIITEKARWGLVTGAYV
AGFFSAFVRTVTAFTLSFCGNNEINFIFCDLPPLLKLSCGDSYTQEVVII
VFALFVMPACILVILVSYLFIIVAILQIHSAGGRAKTFSTCASHLTAVAL
FFGTLIFMYLRDNTGQSSEGDRVVSVLYTVVTPMLNPLIYSLRNKEVKEA
TRKALSKSKPARRP
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 RVPLFLIFLSFYLATMLGNTGMILLIR
TM2 61 83 FFLSHLSLVDICYSSAIIPQMLA
TM3 98 118 AAQFFLFTFFASIDCYLLAIM
TM4 141 161 RWGLVTGAYVAGFFSAFVRTV
TM5 198 219 VIIVFALFVMPACILVILVSYL
TM6 241 265 CASHLTAVALFFGTLIFMYLRDNTG
TM7 271 290 DRVVSVLYTVVTPMLNPLIY

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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