Protein information for: OR10Q2P



LAWXPVFNQSSPTEFVFRVFTTVPEFQVLLFLLFLLFYLMILCGNTAIIW
VVCTYSVLRTPMYFFLSNLSFVEICYTTVVVPLMLSNIFGAQKPIPLAGC
GAQMFFFLTLGGADCFLLAIVAYDRYVAICHPLHYTLIMTCNLCVQMLGG
AVGLALFLSLQLTALIFTLPFCGRQEINHFLCDVPPVLRLACAAIRVHQA
VLYVVSILVLTVPFLLICVSYVFITCAILSIRSAEGRHQAFSTCSSHLTV
VLLQYGCCALAYLHPQSSSSADEDRQFALVYTFITPLLNPLIYTLRNKDV
KGALEKSAQYQRDT
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 27 53 QVLLFLLFLLFYLMILCGNTAIIWVVC
TM2 64 86 FFLSNLSFVEICYTTVVVPLMLS
TM3 101 121 GAQMFFFLTLGGADCFLLAIV
TM4 144 164 CVQMLGGAVGLALFLSLQLTA
TM5 201 222 VLYVVSILVLTVPFLLICVSYV
TM6 244 268 CSSHLTVVLLQYGCCALAYLHPQSS
TM7 274 293 DRQFALVYTFITPLLNPLIY

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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