Protein information for: OR51E2



MSSCNFTHATFVLIGIPGLEKAHFWVGFPLLSMYVVAMFGNCIVVFIVRT
ERSLHAPMYLFLCMLAAIDLALSTSTMPKILALFWFDSREISFEACLTQM
FFIHALSAIESTILLAMAFDRYVAICHPLRHAAVLNNTVTAQIGIVAVVR
GSLFFFPLPLLIKRLAFCHSNVLSHSYCVHQDVMKLAYADTLPNVVYGLT
AILLVMGVDVMFISLSYFLIIRTVLQLPSKSERAKAFGTCVSHIGVVLAF
YVPLIGLSVVHRFGNSLHPIVRVVMGDIYLLLPPVINPIIYGAKTKQIRT
RVLAMFKISCDKDLQAVGGK
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 23 49 HFWVGFPLLSMYVVAMFGNCIVVFIVR
TM2 60 82 LFLCMLAAIDLALSTSTMPKILA
TM3 97 117 LTQMFFIHALSAIESTILLAM
TM4 140 160 TAQIGIVAVVRGSLFFFPLPL
TM5 197 218 YGLTAILLVMGVDVMFISLSYF
TM6 240 264 CVSHIGVVLAFYVPLIGLSVVHRFG
TM7 272 291 RVVMGDIYLLLPPVINPIIY

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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