Protein information for: OR2A25



MGGNQTSITEFLLLGFPIGPRIQMLLFGLFSLFYIFILLGNGTILGLISL
DSRLHTPMYFFLSHLAVVDIACACSTVPQMLVNLLHPAKPISFAGCMTQM
FLFLSFAHTECLLLVVMSYDRYVAICHPLRYSTIMTWKVCITLALTSWIL
GVLLALVHLVLLLPLSFCGPQKLNHFFCEIMAVLKLACADTHINEVMVLA
GAVSVLVGAFFSTVISYVHILCAILKIQSGEGCQKAFSICSSHLCVVGLF
YGTAIIMYVEPQYESPKEQKKYLLLFHSLFNPMLNPLIYSLRNKEVQGTL
KRMLEKKRTS
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 QMLLFGLFSLFYIFILLGNGTILGLIS
TM2 60 82 FFLSHLAVVDIACACSTVPQMLV
TM3 97 117 MTQMFLFLSFAHTECLLLVVM
TM4 140 160 CITLALTSWILGVLLALVHLV
TM5 197 218 MVLAGAVSVLVGAFFSTVISYV
TM6 240 264 CSSHLCVVGLFYGTAIIMYVEPQYE
TM7 270 289 KKYLLLFHSLFNPMLNPLIY

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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