Protein information for: OR2AT4



MDATACNESVDGSPVFYLLGIPSLPETFFLPVFFIFLLFYLLILMGNALI
LVAVVAEPSLHKPMYFFLINLSTLDILFTTTTVPKMLSLFLLGDRFLSFS
SCLLQMYLFQSFTCSEAFILVVMAYDRYVAICHPLHYPVLMNPQTNATLA
ASAWLTALLLPIPAVVRTSQMAYNSIAYIYHCFCDHLAVVQASCSDTTPQ
TLMGFCIAMVVSFLPLLLVLLSYVHILASVLRISSLEGRAKAFSTCSSHL
LVVGTYYSSIAIAYVAYRADLPLDFHIMGNVVYAILTPILNPLIYTLRNR
DVKAAITKIMSQDPGCDRSI
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 29 55 FLPVFFIFLLFYLLILMGNALILVAVV
TM2 66 88 FFLINLSTLDILFTTTTVPKMLS
TM3 103 123 LLQMYLFQSFTCSEAFILVVM
TM4 146 166 NATLAASAWLTALLLPIPAVV
TM5 203 224 MGFCIAMVVSFLPLLLVLLSYV
TM6 246 270 CSSHLLVVGTYYSSIAIAYVAYRAD
TM7 276 295 HIMGNVVYAILTPILNPLIY

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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