Protein information for: OR2M2



MAWENQTFNSDFILLGIFNHSPPHTFLFFLVLGIFLVAFMGNSVMVLLIY
LDTQLHTPMYFLLSQLSLMDLMLICTTVPKMAFNYLSGSKSISMAGCVTQ
IFFYISLSGSECFLLAVMAYDRYIAICHPLRYTNLMNPKICGLMATFSWI
LGSTDGIIDAVATFSFSFCGSREIAHFFCEFPSLLILSCNDTSIFEEVIF
ICCIVMLVFPVAIIIASYARVILAVIHMGSGEGRCKAFTTCSSHLMVVGM
YYGAALFMYIRPTSDHSPTQDKMVSVFYTILTPMLNPLIYSLRNKEVTRA
FMKILGKGKSESELPHKLYVLLFAKFFFLISIFFYDVKILALIMYIA
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 HTFLFFLVLGIFLVAFMGNSVMVLLIY
TM2 61 83 FLLSQLSLMDLMLICTTVPKMAF
TM3 98 118 VTQIFFYISLSGSECFLLAVM
TM4 141 161 CGLMATFSWILGSTDGIIDAV
TM5 198 219 VIFICCIVMLVFPVAIIIASYA
TM6 241 265 CSSHLMVVGMYYGAALFMYIRPTSD
TM7 271 290 DKMVSVFYTILTPMLNPLIY

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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