Protein information for: OR2J3



MNDDGKVNASSEGYFILVGFSNWPHLEVVIFVVVLIFYLMTLIGNLFIII
LSYLDSHLHTPMYFFLSNLSFLDLCYTTSSIPQLLVNLWGPEKTISYAGC
MIQLYFVLALGTTECVLLVVMSYDRYAAVCRPLHYTVLMHPRFCHLLAVA
SWVSGFTNSALHSSFTFWVPLCGHRQVDHFFCEVPALLRLSCVDTHVNEL
TLMITSSIFVLIPLILILTSYGAIVRAVLRMQSTTGLQKVFGTCGAHLMA
VSLFFIPAMCIYLQPPSGNSQDQGKFIALFYTVVTPSLNPLIYTLRNKVV
RGAVKRLMGWE
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 27 53 EVVIFVVVLIFYLMTLIGNLFIIILSY
TM2 64 86 FFLSNLSFLDLCYTTSSIPQLLV
TM3 101 121 MIQLYFVLALGTTECVLLVVM
TM4 144 164 CHLLAVASWVSGFTNSALHSS
TM5 201 222 TLMITSSIFVLIPLILILTSYG
TM6 244 268 CGAHLMAVSLFFIPAMCIYLQPPSG
TM7 274 293 GKFIALFYTVVTPSLNPLIY

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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