Protein information for: OR51I2



MGLFNVTHPAFFLLTGIPGLESSHSWLSGPLCVMYAVALGGNTVILQAVR
VEPSLHEPMYYFLSMLSFSDVAISMATLPTVLRTFCLNARNITFDACLIQ
MFLIHFFSMMESGILLAMSFDRYVAICDPLRYATVLTTEVIAAMGLGAAA
RSFITLFPLPFLIKRLPICRSNVLSHSYCLHPDMMRLACADISINSIYGL
FVLVSTFGMDLFFIFLSYVLILRSVMATASREERLKALNTCVSHILAVLA
FYVPMIGVSTVHRFGKHVPCYIHVLMSNVYLFVPPVLNPLIYSAKTKEIR
RAIFRMFHHIKI
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 HSWLSGPLCVMYAVALGGNTVILQAVR
TM2 61 83 YFLSMLSFSDVAISMATLPTVLR
TM3 98 118 LIQMFLIHFFSMMESGILLAM
TM4 141 161 IAAMGLGAAARSFITLFPLPF
TM5 198 219 YGLFVLVSTFGMDLFFIFLSYV
TM6 241 265 CVSHILAVLAFYVPMIGVSTVHRFG
TM7 273 292 HVLMSNVYLFVPPVLNPLIY

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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