Protein information for: OR52E3P



MFLPNNTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYIIALIGRFTILLV
IKTDSSLYQPMFYFLAMLATIDLGLSTATIPKMLGIFWFSLREIICDACL
IQMFFIHNFTGMESAALVGMAYDHFVAICNPLRYSIILTKKAVSVIGLGV
LVRSFMSVIPFVFLILRLPFCGDHVIPHTNCEHMGLAHLSCSSIKINIIY
GLGAISILVFDIIAIALSYVQILHAVFHLPSCKAXLKSLSTCGSHVCVIL
AFYTPALFSFVTHRFGQNVPRYIHILLANLYVVVPPMLNPVIYGVRTKQI
YDCVKKIFLQK
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 26 52 HIWIGFPFCAVYIIALIGRFTILLVIK
TM2 63 85 YFLAMLATIDLGLSTATIPKMLG
TM3 100 120 LIQMFFIHNFTGMESAALVGM
TM4 143 163 VSVIGLGVLVRSFMSVIPFVF
TM5 200 220 YGLGAISILVFDIIAIALSYV
TM6 242 266 CGSHVCVILAFYTPALFSFVTHRFG
TM7 274 293 HILLANLYVVVPPMLNPVIY

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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