Protein information for: OR2AT2P



METITCNGSGDSSTTFYLMGIPSLPKSLFLPIFFVFLLLYVLILMGNTFI
LVAVVAKPSLHKPMYFFLINLSTLDILVTTTTVPKMLSLFLFGDSFLSFP
ACFLQMYLFHSFSCSEAFILVVMAYDRYVAICRPLHYPVLMTPQTNTVLT
TSAWLTALLLPIPAVVQTSQMAFDIIVHIYHCFCDHLAVVQASCSDTSPQ
TFMGFCIAMVVSFLPLLLVLLSYAHILTSVLCINCQEGRSKAFSTCSSHL
LVVGTYYSSIAIAYVAYRADLPLDFHVMGNVVYAILTPVLNPVIYKLRNK
DVKAAITKIAVPRSQRMLGNPDSK
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 FLPIFFVFLLLYVLILMGNTFILVAVV
TM2 66 88 FFLINLSTLDILVTTTTVPKMLS
TM3 103 123 FLQMYLFHSFSCSEAFILVVM
TM4 146 166 NTVLTTSAWLTALLLPIPAVV
TM5 203 224 MGFCIAMVVSFLPLLLVLLSYA
TM6 246 270 CSSHLLVVGTYYSSIAIAYVAYRAD
TM7 276 295 HVMGNVVYAILTPVLNPVIY

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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