Protein information for: OR51L1



MGDWNNSDAVEPIFILRGFPGLEYVHSWLSILFCLAYLVAFMGNVTILSV
IWIESSLHQPMYYFISILAVNDLGMSLSTLPTMLAVLWLDAPEIQASACY
AQLFFIHTFTFLESSVLLAMAFDRFVAICHPLHYPTILTNSVIGKIGLAC
LLRSLGVVLPTPLLLRHYHYCHGNALSHAFCLHQDVLRLSCTDARTNSIY
GLCVVIATLGVDSIFILLSYVLILNTVLDIASREEQLKALNTCVSHICVV
LIFFVPVIGVSMVHRFGKHLSPIVHILMADIYLLLPPVLNPIVYSVRTKQ
IRLGILHKFVLRRRF
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 26 52 HSWLSILFCLAYLVAFMGNVTILSVIW
TM2 63 85 YFISILAVNDLGMSLSTLPTMLA
TM3 100 120 YAQLFFIHTFTFLESSVLLAM
TM4 143 163 IGKIGLACLLRSLGVVLPTPL
TM5 200 221 YGLCVVIATLGVDSIFILLSYV
TM6 243 267 CVSHICVVLIFFVPVIGVSMVHRFG
TM7 275 294 HILMADIYLLLPPVLNPIVY

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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