Protein information for: OR52R1



MVLASGNSSSHPVSFILLGIPGLESFQLWIAFPFCATYAVAVVGNITLLH
VIRIDHTLHEPMYLFLAMLAITDLVLSSSTQPKMLAIFWFHAHEIQYHAC
LIQVFFIHAFSSVESGVLMAMALDCYVAICFPLRHSSILTPSVVIKLGTI
VMLRGLLWVSPFCFMVSRMPFCQHQAIPQSYCEHMAVLKLVCADTSISRG
NGLFVAFSVAGFDMIVIGMSYVMILRAVLQLPSGEARLKAFSTRSSHICV
ILALYIPALFSFLTYRFGHDVPRVVHILFANLYLLIPPMLNPIIYGVRTK
QIGDRVIQGCCGNIP
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 27 53 QLWIAFPFCATYAVAVVGNITLLHVIR
TM2 64 86 LFLAMLAITDLVLSSSTQPKMLA
TM3 101 121 LIQVFFIHAFSSVESGVLMAM
TM4 144 164 VIKLGTIVMLRGLLWVSPFCF
TM5 201 222 NGLFVAFSVAGFDMIVIGMSYV
TM6 244 268 RSSHICVILALYIPALFSFLTYRFG
TM7 276 295 HILFANLYLLIPPMLNPIIY

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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