Protein information for: OR52N3P



MNGANSSSLTPRYFILSGVPGLEAAHIWISLPFCFMYIIVVLGNCGLIYL
ISHEEALHQPTYYFLDLLSLTDVTGCTSFVPNMLCIFWFGLKEIDFNACL
VQMFFIHMLTGMESGALMLMALDRYVAICYPLHYSTIFTNTVITKVGLVT
FIQSVLLMIPFAFLIKCLPYCRGNLIHHTYCXHMSVAKLSCGNVQINAIY
GLIAAILIGGFDMFCISMSYTMIIRAVVNLSSGRCCHKAFSTCTAHICAI
FITYVPAFFNFFTHRFGGHTIPHHVHIFIANLYLMLPPTLNPIVYGVKTK
QIREGVIKLFFREKGILSMT
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 HIWISLPFCFMYIIVVLGNCGLIYLIS
TM2 63 85 YFLDLLSLTDVTGCTSFVPNMLC
TM3 100 120 LVQMFFIHMLTGMESGALMLM
TM4 143 163 ITKVGLVTFIQSVLLMIPFAF
TM5 200 221 YGLIAAILIGGFDMFCISMSYT
TM6 243 267 CTAHICAIFITYVPAFFNFFTHRFG
TM7 276 295 HIFIANLYLMLPPTLNPIVY

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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