Protein information for: OR2L9P



MEKYNQTSTDFILLGIFPPSRIGFLLFILLVLILLLALIGNQSVILLIFL
DTHLHTPIYFLLSRLYLIDLNYISTIVPKMFSDFLFGNKSISFIGCGIQS
FFFVTLAGAEMLPLTSMACDHYVAVCFPLHYPIHMSKIVCVWMIIGSWIM
GSIDTCAHISYCPISLLLSQGCDVPAMVTLAFVDTWVYECTVFLSTTLFL
MFTFIGIACSYGEVLLTVYHIKSAEGRKKAYSTCSTHLTVVIFYYAMFAY
TYLYPRYLQSPTEDKVLAVFYTILTSMLNPIIYSLRNREVMGALTRVSQR
IFPVKMKTNFLP
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 23 49 GFLLFILLVLILLLALIGNQSVILLIF
TM2 60 82 FLLSRLYLIDLNYISTIVPKMFS
TM3 97 117 GIQSFFFVTLAGAEMLPLTSM
TM4 140 160 CVWMIIGSWIMGSIDTCAHIS
TM5 191 212 TVFLSTTLFLMFTFIGIACSYG
TM6 234 258 CSTHLTVVIFYYAMFAYTYLYPRYL
TM7 264 283 DKVLAVFYTILTSMLNPIIY

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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