Protein information for: OR51F1



MEILSNSTSKFPTFLLTGIPGLESAHVWISIPFCCFYAIALSGNSVILFV
IITQQSLHEPMYYFLFRLSATDLGLTVSSLSTTLGILWFEAREISLYSCI
VQMFFLHGFTFMESGVLVATAFDRYVAICDPLRYTTILTNSRIIQMGLLM
ITRAIVLILPLLLLLKPLYFCRMNALSHSYCYHPDVIQLACSDIRANSIC
GLIDLILTTGIDTPCIVLSYILIIHSVLRIASPEEWHKVFSTCVSHVGAV
AFFYIHMLSLSLVYRYGRSAPRVVHSVMANVYLLLPPVLNPIIDSVKTKQ
IRKAMLSLLLTK
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 HVWISIPFCCFYAIALSGNSVILFVII
TM2 63 85 YFLFRLSATDLGLTVSSLSTTLG
TM3 100 120 IVQMFFLHGFTFMESGVLVAT
TM4 143 163 IIQMGLLMITRAIVLILPLLL
TM5 200 221 CGLIDLILTTGIDTPCIVLSYI
TM6 243 267 CVSHVGAVAFFYIHMLSLSLVYRYG
TM7 275 294 HSVMANVYLLLPPVLNPIID

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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