Protein information for: OR11H13P



MNVSEPNSSFAFVNEFILQGFSCEWTIQIFLFSLFTTIYALTITGNGAIA
FALWCDRRLHTPMYMFLGDFSFLEIWYVFSTVPKMLVNFLSEKTNISFAG
CFLQFYFFFSLGTSECLLLTVMAFDQYLAICRPLHYPNIMTGHLCAKLVI
LCWVCGFLWFLIPIFLISQMPFCGPNIIDHVVCDPGPLFALDCVSAPRIQ
LFCYTLSSLVIFGNFLFIIGSYTIVLKVVLGTPSSTGRHKAFSTCGSHLA
VVSLCYGSLMVMYVSPGLGHSTGMQKIVTLFYAMVTPLFNPLIYSLQNKE
IKAALRKVLG
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 QIFLFSLFTTIYALTITGNGAIAFALW
TM2 65 87 MFLGDFSFLEIWYVFSTVPKMLV
TM3 102 122 FLQFYFFFSLGTSECLLLTVM
TM4 145 165 CAKLVILCWVCGFLWFLIPIF
TM5 202 223 FCYTLSSLVIFGNFLFIIGSYT
TM6 245 269 CGSHLAVVSLCYGSLMVMYVSPGLG
TM7 275 294 QKIVTLFYAMVTPLFNPLIY

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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