Protein information for: OR2N1P



MPLTNESHPEEFILLGFADRPWLELPLFTSLLIMYPIAVMGNITIILMSR
LDSRLHSPMYFFLTNLSFLDMCYTTSIVPQMLFNLGSSKKTISYMGCAVQ
LYFFHIMGGTECLLLAIMSFDRYVAICRPLHYTLIMNQRVCIHXFPPCWL
IGIIYAVSEATATLQLPLCGLNKLDHLVCEIPVLIKIACGEKGSNELTLS
VVCIFMLAVPLCLILASYASIGSAVFKIKSSKGRKKAFGTCSSHLIVVFL
FYGPAISMYLQPPSSISRDQPKFMALFYGVVTPSLNPFIYTLRNKNVKGA
LRNLVRSIFSFK
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 ELPLFTSLLIMYPIAVMGNITIILMSR
TM2 61 83 FFLTNLSFLDMCYTTSIVPQMLF
TM3 98 118 AVQLYFFHIMGGTECLLLAIM
TM4 141 161 CIHXFPPCWLIGIIYAVSEAT
TM5 198 219 TLSVVCIFMLAVPLCLILASYA
TM6 241 265 CSSHLIVVFLFYGPAISMYLQPPSS
TM7 271 290 PKFMALFYGVVTPSLNPFIY

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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