Protein information for: OR2AK2



MKTGNQSFGTDFLLVGLFQYGWINSLLFVVIATLFTVALTGNIMLIHLIR
LNTRLHTPMYFLLSQLSIVDLMYISTTVPKMAVSFLSQSKTIRFLGCEIQ
TYVFLALGGTEALLLGFMSYDRYVAICHPLHYPMLMSKKICCLMVACAWA
SGSINAFIHTLYVFQLPFCRSRLINHFFCEVPALLSLVCQDTSQYEYTVL
LSGLIILLLPFLAILASYARVLIVVFQMSSGKGQAKAVSTCSSHLIVASL
FYATTLFTYTRPHSLRSPSRDKAVAVFYTIVTPLLNPFIYSLRNKEVTGA
VRRLLGYWICCRKYDFRSLY
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 NSLLFVVIATLFTVALTGNIMLIHLIR
TM2 61 83 FLLSQLSIVDLMYISTTVPKMAV
TM3 98 118 EIQTYVFLALGGTEALLLGFM
TM4 141 161 CCLMVACAWASGSINAFIHTL
TM5 198 219 TVLLSGLIILLLPFLAILASYA
TM6 241 265 CSSHLIVASLFYATTLFTYTRPHSL
TM7 271 290 DKAVAVFYTIVTPLLNPFIY

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.
HORDE homepage