Protein information for: OR2A20P



MVKNQTMVTEFLLLGFLLGPRIQMLLFGLFSLFYVFTLLGNGTILGLISL
DSRLHTPMYFFLSHLAVVNIAYACNTVPQMLVNLLHPAKPISFAGCMTXT
FLFLSFAHTECLLLVLMSYDRYVAICHPLRYFIIMTWKVCITLAITSWTC
GSLLAMVHVSLILRLPFCGPREINHFFCEILSVLRLACADTWLNQVVIFA
ACMFILVGPLCLVLVSYSHILAAILRIQSGEGRRKAFSTCSSHLCVVGLF
FGSAIVMYMAPKSRHPEEQQKVLFLFYSSFNPMLNPLIYNLRNVEVKGAL
RRALCKESHS
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 QMLLFGLFSLFYVFTLLGNGTILGLIS
TM2 60 82 FFLSHLAVVNIAYACNTVPQMLV
TM3 97 117 MTXTFLFLSFAHTECLLLVLM
TM4 140 160 CITLAITSWTCGSLLAMVHVS
TM5 197 218 VIFAACMFILVGPLCLVLVSYS
TM6 240 264 CSSHLCVVGLFFGSAIVMYMAPKSR
TM7 270 289 QKVLFLFYSSFNPMLNPLIY

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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