Protein information for: OR2J2



MMIKKNASSEDFFILLGFSNWPQLEVVLFVVILIFYLMTLTGNLFIIILS
YVDSHLHTPMYFFLSNLSFLDLCHTTSSIPQLLVNLRGPEKTISYAGCMV
QLYFVLALGIAECVLLVVMSYDRYVAVCRPLHYTVLMHPRFCHLLAAASW
VIGFTISALHSSFTFWVPLCGHRLVDHFFCEVPALLRLSCVDTHANELTL
MVMSSIFVLIPLILILTAYGAIARAVLSMQSTTGLQKVFRTCGAHLMVVS
LFFIPVMCMYLQPPSENSPDQGKFIALFYTVVTPSLNPLIYTLRNKHVKG
AAKRLLGWEWGK
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 25 51 EVVLFVVILIFYLMTLTGNLFIIILSY
TM2 62 84 FFLSNLSFLDLCHTTSSIPQLLV
TM3 99 119 MVQLYFVLALGIAECVLLVVM
TM4 142 162 CHLLAAASWVIGFTISALHSS
TM5 199 220 TLMVMSSIFVLIPLILILTAYG
TM6 242 266 CGAHLMVVSLFFIPVMCMYLQPPSE
TM7 272 291 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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