Protein information for: OR51I1



MLGLNGTPFQPATLQLTGIPGIQTGLTWVALIFCILYMISIVGNLSILTL
VFWEPALHQPMYYFLSMLALNDLGVSFSTLPTVISTFCFNYNHVAFNACL
VQMFFIHTFSFMESGILLAMSLDRFVAICYPLRYVTVLTHNRILAMGLGI
LTKSFTTLFPFPFVVKRLPFCKGNVLHHSYCLHPDLMKVACGDIHVNNIY
GLLVIIFTYGMDSTFILLSYALILRAMLVIISQEQRLKALNTCMSHICAV
LAFYVPIIAVSMIHRFWKSAPPVVHVMMSNVYLFVPPMLNPIIYSVKTKE
IRKGILKFFHKSQA
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 LTWVALIFCILYMISIVGNLSILTLVF
TM2 63 85 YFLSMLALNDLGVSFSTLPTVIS
TM3 100 120 LVQMFFIHTFSFMESGILLAM
TM4 143 163 ILAMGLGILTKSFTTLFPFPF
TM5 200 221 YGLLVIIFTYGMDSTFILLSYA
TM6 243 267 CMSHICAVLAFYVPIIAVSMIHRFW
TM7 275 294 HVMMSNVYLFVPPMLNPIIY

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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