Protein information for: OR51G2



MTLLGNSSSSVSATFLLSGIPGLERMHIWISIPLCFMYLVSIPGNCTILF
IIKTERSLHEPMYLFLSMLALIDLGLSLCTLPTVLGIFWVGAREISHDAC
FAQLFFIHCFSFLESSVLLSMAFDRFVAICHPLHYVSILTNTVIGRIGLV
SLGRSVALIFPLPFMLKRFPYCGSPVLSHSYCLHQEVMKLACADMKANSI
YGMFVIVSTVGIDSLLILFSYALILRTVLSIASRAERFKALNTCVSHICA
VLLFYTPMIGLSVIHRFGKQAPHLVQVVMGFMYLLFPPVMNPIVYSVKTK
QIRDRVTHAFCY
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 27 53 HIWISIPLCFMYLVSIPGNCTILFIIK
TM2 64 86 LFLSMLALIDLGLSLCTLPTVLG
TM3 101 121 FAQLFFIHCFSFLESSVLLSM
TM4 144 164 IGRIGLVSLGRSVALIFPLPF
TM5 201 222 YGMFVIVSTVGIDSLLILFSYA
TM6 244 268 CVSHICAVLLFYTPMIGLSVIHRFG
TM7 276 295 QVVMGFMYLLFPPVMNPIVY

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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