Protein information for: OR2S2



MEKANETSPVMGFVLLRLSAHPELEKTFFVLILLMYLVILLGNGVLILVT
ILDSRLHTPMYFFLGNLSFLDICFTTSSVPLVLDSFLTPQETISFSACAV
QMALSFAMAGTECLLLSMMAFDRYVAICNPLRYSVIMSKAAYMPMAASSW
AIGGAASVVHTSLAIQLPFCGDNVINHFTCEILAVLKLACADISINVISM
EVTNVIFLGVPVLFISFSYVFIITTILRIPSAEGRKKVFSTCSAHLTVVI
VFYGTLFFMYGKPKSKDSMGADKEDLSDKLIPLFYGVVTPMLNPIIYSLR
NKDVKAAVRRLLRPKGFTQ
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 25 51 EKTFFVLILLMYLVILLGNGVLILVTI
TM2 62 84 FFLGNLSFLDICFTTSSVPLVLD
TM3 99 119 AVQMALSFAMAGTECLLLSMM
TM4 142 162 YMPMAASSWAIGGAASVVHTS
TM5 199 220 SMEVTNVIFLGVPVLFISFSYV
TM6 242 266 CSAHLTVVIVFYGTLFFMYGKPKSK
TM7 278 297 DKLIPLFYGVVTPMLNPIIY

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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