Protein information for: OR4S2



MEKINNVTEFIFWGLSQSPEIEKVCFVVFSFFYIIILLGNLLIMLTVCLS
NLFKSPMYFFLSFLSFVDICYSSVTAPKMIVDLLAKDKTISYVGCMLQLF
GVHFFGCTEIFILTVMAYDRYVAICKPLHYMTIMNRETCNKMLLGTWVGG
FLHSIIQVALVVQLPFCGPNEIDHYFCDVHPVLKLACTETYIVGVVVTAN
SGTIALGSFVILLISYSIILVSLRKQSAEGRRKALSTCGSHIAMVVIFFG
PCTFMYMRPDTTFSEDKMVAVFYTIITPMLNPLIYTLRNAEVKNAMKKLW
GRNVFLEAKGK
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 22 48 EKVCFVVFSFFYIIILLGNLLIMLTVC
TM2 59 81 FFLSFLSFVDICYSSVTAPKMIV
TM3 96 116 MLQLFGVHFFGCTEIFILTVM
TM4 139 159 CNKMLLGTWVGGFLHSIIQVA
TM5 196 217 VVTANSGTIALGSFVILLISYS
TM6 238 262 CGSHIAMVVIFFGPCTFMYMRPDTT
TM7 267 284 MVAVFYTIITPMLNPLIY

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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