Protein information for: OR2A1



MGENQTMVTEFLLLGFLLGPRIQMLLFGLFSLFYIFTLLGNGAILGLISL
DSRLHTPMYFFLSHLAVVDIAYTRNTVPQMLANLLHPAKPISFAGCMTQT
FLCLSFGHSECLLLVLMSYDRYVAICHPLRYSVIMTWRVCITLAVTSWTC
GSLLALAHVVLILRLPFSGPHEINHFFCEILSVLRLACADTWLNQVVIFA
ACVFFLVGPPSLVLVSYSHILAAILRIQSGEGRRKAFSTCSSHLCVVGLF
FGSAIIMYMAPKSRHPEEQQKVFFLFYSFFNPTLNPLIYSLRNGEVKGAL
RRALGKESHS
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 QMLLFGLFSLFYIFTLLGNGAILGLIS
TM2 60 82 FFLSHLAVVDIAYTRNTVPQMLA
TM3 97 117 MTQTFLCLSFGHSECLLLVLM
TM4 140 160 CITLAVTSWTCGSLLALAHVV
TM5 197 218 VIFAACVFFLVGPPSLVLVSYS
TM6 240 264 CSSHLCVVGLFFGSAIIMYMAPKSR
TM7 270 289 QKVFFLFYSFFNPTLNPLIY

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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