Protein information for: OR52X1P



FFSNNSVLFPHTFFLAGIPGLTATHIWISLPFCFMFFLSLTGNGVLLFLI
RTECSLRQPMFLFLAMLSFVDLVLSLSTLPKMLAIFWFGATAISSHSCLS
QMFSIHAFSAMESGVLVAMALDRSVAICNPLRYATILPPVVVAKIGGLVV
LXGVGLTISFPSLAHRLHYHGSHMIAYTFCEHMAVVKLACEATTVDNLYA
FVVAIFLGGGDVVFIAYSYGLIVRTVMHFPSPEERAKAGSTCTAHVCVIL
FFYGLGFLSVVMQRFGAPTASTAKVILANLYLLFPPALDPIVYGMETKQI
XERLLMILSPKQIELT
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 HIWISLPFCFMFFLSLTGNGVLLFLIR
TM2 62 84 LFLAMLSFVDLVLSLSTLPKMLA
TM3 99 119 LSQMFSIHAFSAMESGVLVAM
TM4 142 162 VAKIGGLVVLXGVGLTISFPS
TM5 199 220 YAFVVAIFLGGGDVVFIAYSYG
TM6 242 266 CTAHVCVILFFYGLGFLSVVMQRFG
TM7 274 293 KVILANLYLLFPPALDPIVY

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.
HORDE homepage