Protein information for: OR2L1P



MENYNQTSTAFILLGLSPPPKIGHFIFILINFVFLMALIGNLSMILLIFL
DIHLHTPMYFLLSQLSLIDLNYISTIVPKMVYDFLYGNKSISFTGCGIQS
FFFLTLAGAEALLLTSMAYDRYVAICFPLHYPIRMRKRVCALMITGSWMI
GSINSCAHTVYALRIPYCKSRAINHFFCDVPAMLTLACTDTWVYECTVFL
STTIFLVFPFICIACSYGRILLAVYHMHSAEGRKKAYSTCSTHLTVVTFY
YAPFAYTYLRPRSLRSPTEDKVLAVFYTILTPMLNPIIYSLRNKEVMGAL
TRVIQKIF
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 GHFIFILINFVFLMALIGNLSMILLIF
TM2 60 82 FLLSQLSLIDLNYISTIVPKMVY
TM3 97 117 GIQSFFFLTLAGAEALLLTSM
TM4 140 160 CALMITGSWMIGSINSCAHTV
TM5 197 218 TVFLSTTIFLVFPFICIACSYG
TM6 240 264 CSTHLTVVTFYYAPFAYTYLRPRSL
TM7 270 289 DKVLAVFYTILTPMLNPIIY

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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