Protein information for: OR52A1



MSISNITVYMPSVLTLVGIPGLESVQCWIGIPFCAIYLIAMIGNSLLLSI
IKSERSLHEPLYIFLGMLGATDIALASSIMPKMLGIFWFNVPEIYFDSCL
LQMWFIHTLQGIESGILVAMALDRYVAICYPLRHANIFTHQLVIQIGTMV
VLRAAILVAPCLVLIKCRFQFYHTTVISHSYCEHMAIVKLAAANVQVNKI
YGLFVAFTVAGFDLTFITLSYIQIFITVFRLPQKEARFKAFNTCIAHICV
FLQFYLLAFFSFFTHRFGSHISPYIHILFSSIYLLVPPFLNPLVYGAKTT
QIRIHVVKMFCS
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 26 52 QCWIGIPFCAIYLIAMIGNSLLLSIIK
TM2 63 85 IFLGMLGATDIALASSIMPKMLG
TM3 100 120 LLQMWFIHTLQGIESGILVAM
TM4 143 163 VIQIGTMVVLRAAILVAPCLV
TM5 201 222 YGLFVAFTVAGFDLTFITLSYI
TM6 244 268 CIAHICVFLQFYLLAFFSFFTHRFG
TM7 276 295 HILFSSIYLLVPPFLNPLVY

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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