Protein information for: OR2G2



MVRHTNESNLAGFILLGFSDYPQLQKVLFVLILILYLLTILGNTTIILVS
RLEPKLHMPMYFFLSHLSFLYRCFTSSVIPQLLVNLWEPMKTIAYGGCLV
HLYNSHALGSTECVLPAVMSCDRYVAVCRPLHYTVLMHIHLCMALASMAW
LSGIATTLVQSTLTLQLPFCGHRQVDHFICEVPVLIKLACVGTTFNEAEL
FVASILFLIVPVSFILVSSGYIAHAVLRIKSATRRQKAFGTCFSHLTVVT
IFYGTIIFMYLQPAKSRSRDQGKFVSLFYTVVTRMLNPLIYTLRIKEVKG
ALKKVLAKALGVNIL
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 25 51 QKVLFVLILILYLLTILGNTTIILVSR
TM2 62 84 FFLSHLSFLYRCFTSSVIPQLLV
TM3 99 119 LVHLYNSHALGSTECVLPAVM
TM4 142 162 CMALASMAWLSGIATTLVQST
TM5 199 220 ELFVASILFLIVPVSFILVSSG
TM6 242 266 CFSHLTVVTIFYGTIIFMYLQPAKS
TM7 272 291 GKFVSLFYTVVTRMLNPLIY

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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