Protein information for: OR2H2
MVNQSSTPGFLLLGFSEHPGLERTLFVVVFTSYLLTLVGNTLIILLSALD
PKLHSPMYFFLSNLSFLDLCFTTSCVPQMLVNLWGPKKTISFLDCSVQIF
IFLSLGTTECILLTVMAFDRYVAVCQPLHYATIIHPRLCWQLASVAWVIG
LVESVVQTPSTLHLPFCPDRQVDDFVCEVPALIRLSCEDTSYNEIQVAVA
SVFILVVPLSLILVSYGAITWAVLRINSAKGRRKAFGTCSSHLTVVTLFY
SSVIAVYLQPKNPYAQERGKFFGLFYAVGTPSLNPLIYTLRNKEVTRAFR
RLLGKEMGLTQS
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 | 22 | 48 | ERTLFVVVFTSYLLTLVGNTLIILLSA |
| TM2 | 59 | 81 | FFLSNLSFLDLCFTTSCVPQMLV |
| TM3 | 96 | 116 | SVQIFIFLSLGTTECILLTVM |
| TM4 | 139 | 159 | CWQLASVAWVIGLVESVVQTP |
| TM5 | 196 | 217 | QVAVASVFILVVPLSLILVSYG |
| TM6 | 239 | 263 | CSSHLTVVTLFYSSVIAVYLQPKNP |
| TM7 | 269 | 288 | GKFFGLFYAVGTPSLNPLIY |
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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