Protein information for: OR2A2



MEGNQTWITDITLLGFQVGPALAILLCGLFSVFYTLTLLGNGVIFGIICL
DSKLHTPMYFFLSHLAIIDMSYASNNVPKMLANLMNQKRTISFVPCIMQT
FLYLAFAVTECLILVVMSYDRYVAICHPFQYTVIMSWRVCTILVLTSWSC
GFALSLVHEILLLRLPFCGPRDVNHLFCEILSVLKLACADTWVNQVVIFA
TCVFVLVGPLSLILVSYMHILGAILKIQTKEGRIKAFSTCSSHLCVVGLF
FGIAMVVYMVPDSNQREEQEKMLSLFHSVFNPMLNPLIYSLRNAQLKGAL
HRALQRKRSMRTVYGLCL
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 23 49 AILLCGLFSVFYTLTLLGNGVIFGIIC
TM2 60 82 FFLSHLAIIDMSYASNNVPKMLA
TM3 97 117 IMQTFLYLAFAVTECLILVVM
TM4 140 160 CTILVLTSWSCGFALSLVHEI
TM5 197 218 VIFATCVFVLVGPLSLILVSYM
TM6 240 264 CSSHLCVVGLFFGIAMVVYMVPDSN
TM7 270 289 EKMLSLFHSVFNPMLNPLIY

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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