Protein information for: OR2K2



MQGENFTIWSIFFLEGFSQYPGLEVVLFVFSLVMYLTTLLGNSTLILITI
LDSRLKTPMYLFLGNLSFMDICYTSASVPTLLVNLLSSQKTIIFSGCAVQ
MYLSLAMGSTECVLLAVMAYDRYVAICNPLRYSIIMNRCVCARMATVSWV
TGCLTALLETSFALQIPLCGNLIDHFTCEILAVLKLACTSSLLMNTIMLV
VSILLLPIPMLLVCISYIFILSTILRITSAEGRNKAFSTCGAHLTVVILY
YGAALSMYLKPSSSNAQKIDKIISLLYGVLTPMLNPIIYSLRNKEVKDAM
KKLLGKITLHQT
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 24 50 EVVLFVFSLVMYLTTLLGNSTLILITI
TM2 61 83 LFLGNLSFMDICYTSASVPTLLV
TM3 98 118 AVQMYLSLAMGSTECVLLAVM
TM4 141 161 CARMATVSWVTGCLTALLETS
TM5 197 218 IMLVVSILLLPIPMLLVCISYI
TM6 240 264 CGAHLTVVILYYGAALSMYLKPSSS
TM7 270 289 DKIISLLYGVLTPMLNPIIY

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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