Protein information for: OR52N2



MSGDNSSSLTPGFFILNGVPGLEATHIWISLPFCFMYIIAVVGNCGLICL
ISHEEALHRPMYYFLALLSFTDVTLCTTMVPNMLCIFWFNLKEIDFNACL
AQMFFVHMLTGMESGVLMLMALDRYVAICYPLRYATILTNPVIAKAGLAT
FLRNVMLIIPFTLLTKRLPYCRGNFIPHTYCDHMSVAKVSCGNFKVNAIY
GLMVALLIGVFDICCISVSYTMILQAVMSLSSADARHKAFSTCTSHMCSI
VITYVAAFFTFFTHRFVGHNIPNHIHIIVANLYLLLPPTMNPIVYGVKTK
QIQEGVIKFLLGDKVSFTYDK
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 HIWISLPFCFMYIIAVVGNCGLICLIS
TM2 63 85 YFLALLSFTDVTLCTTMVPNMLC
TM3 100 120 LAQMFFVHMLTGMESGVLMLM
TM4 143 163 IAKAGLATFLRNVMLIIPFTL
TM5 200 221 YGLMVALLIGVFDICCISVSYT
TM6 243 267 CTSHMCSIVITYVAAFFTFFTHRFV
TM7 276 295 HIIVANLYLLLPPTMNPIVY

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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