Protein information for: OR52N1



MSFLNGTSLTPASFILNGIPGLEDVHLWISFPLCTMYSIAITGNFGLMYL
IYCDEALHRPMYVFLALLSFTDVLMCTSTLPNTLFILWFNLKEIDFKACL
AQMFFVHTFTGMESGVLMLMALDHCVAICFPLRYATILTNSVIAKAGFLT
FLRGVMLVIPSTFLTKRLPYCKGNVIPHTYCDHMSVAKISCGNVRVNAIY
GLIVALLIGGFDILCITISYTMILQAVVSLSSADARQKAFSTCTAHFCAI
VLTYVPAFFTFFTHHFGGHTIPLHIHIIMANLYLLMPPTMNPIVYGVKTR
QVRESVIRFFLKGKDNSHNF
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 HLWISFPLCTMYSIAITGNFGLMYLIY
TM2 63 85 VFLALLSFTDVLMCTSTLPNTLF
TM3 100 120 LAQMFFVHTFTGMESGVLMLM
TM4 143 163 IAKAGFLTFLRGVMLVIPSTF
TM5 200 221 YGLIVALLIGGFDILCITISYT
TM6 243 267 CTAHFCAIVLTYVPAFFTFFTHHFG
TM7 276 295 HIIMANLYLLMPPTMNPIVY

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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