Protein information for: OR1L3



MGMSNLTRLSEFILLGLSSRSEDQRPLFALFLIIYLVTLMGNLLIILAIH
SDPRLQNPMYFFLSILSFADICYTTVIVPKMLVNFLSEKKTISYAECLAQ
MYFFLVFGNIDSYLLAAMAINRCVAICNPFHYVTVMNRRCCVLLLAFPIT
FSYFHSLLHVLLVNRLTFCTSNVIHHFFCDVNPVLKLSCSSTFVNEIVAM
TEGLASVMAPFVCIIISYLRILIAVLKIPSAAGKHKAFSTCSSHLTVVIL
FYGSISYVYLQPLSSYTVKDRIATINYTVLTSVLNPFIYSLRNKDMKRGL
QKLINKIKSQMSRFSTKTNKICGP
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 QRPLFALFLIIYLVTLMGNLLIILAIH
TM2 61 83 FFLSILSFADICYTTVIVPKMLV
TM3 98 118 LAQMYFFLVFGNIDSYLLAAM
TM4 141 161 CVLLLAFPITFSYFHSLLHVL
TM5 198 219 VAMTEGLASVMAPFVCIIISYL
TM6 241 265 CSSHLTVVILFYGSISYVYLQPLSS
TM7 270 288 RIATINYTVLTSVLNPFIY

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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