Protein information for: OR52I2



MLGPAYNHTMETPASFLLVGIPGLQSSHLWLAISLSAMYIIALLGNTIIV
TAIWMDSTRHEPMYCFLCVLAAVDIVMASSVVPKMVSIFCSGDSSISFSA
CFTQMFFVHLATAVETGLLLTMAFDRYVAICKPLHYKRILTPQVMLGMSM
AITIRAIIAITPLSWMVSHLPFCGSNVVVHSYCEHIALARLACADPVPSS
LYSLIGSSLMVGSDVAFIAASYILILKAVFGLSSKTAQLKALSTCGSHVG
VMALYYLPGMASIYAAWLGQDVVPLHTQVLLADLYVIIPATLNPIIYGMR
TKQLRERIWSYLMHVLFDHSNLGS
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 28 54 HLWLAISLSAMYIIALLGNTIIVTAIW
TM2 65 87 CFLCVLAAVDIVMASSVVPKMVS
TM3 102 122 FTQMFFVHLATAVETGLLLTM
TM4 145 165 MLGMSMAITIRAIIAITPLSW
TM5 202 223 YSLIGSSLMVGSDVAFIAASYI
TM6 245 269 CGSHVGVMALYYLPGMASIYAAWLG
TM7 278 297 QVLLADLYVIIPATLNPIIY

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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