Protein information for: OR8G7P



MEAVNYSSVTEFILVGLTEEPELQLPLFLAFLGIYMVTVLGNLGMITLIG
LSSHLHTPMYYFLNSLFFIDLCHSTVFTPKMLVNFVTEKNIISYSVCMTQ
LYFFLIFAIAECHVLAAMAYDHCIAICSPVLYIVVMPACFPLLILGVILL
CYIIGPVCSSAYTNYSCMSRVQFCKFDVINHYFCDFPPLLKLSXSSTYVN
KLLILCVHAFNILVPSLTILSSYVFIIASIFYICSTEGNSKVFSIYGSHM
VVDVVFYGSAIFIYQXLSSVSSEXXWKVSSXSACYTTVVPMLNTLIYNLR
NKDVNVSLEKMLQRTLLXTEIKDGLLNLSGXLLHCMNGCLSF
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 24 50 QLPLFLAFLGIYMVTVLGNLGMITLIG
TM2 61 83 YFLNSLFFIDLCHSTVFTPKMLV
TM3 98 118 MTQLYFFLIFAIAECHVLAAM
TM4 144 164 ILGVILLCYIIGPVCSSAYTN
TM5 203 224 LILCVHAFNILVPSLTILSSYV
TM6 246 270 YGSHMVVDVVFYGSAIFIYQXLSSV
TM7 278 297 VSSXSACYTTVVPMLNTLIY

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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