Protein information for: OR11H12



MCPLTLQVTGLMNVSEPNSSFAFVNEFILQGFTCEWTIQIFLFSLFTTTY
ALTITGNGAIAFVLWCDWRLHTPMYMFLGNFSFLEIWYVSSTVPKMLVNF
LSEKKNISFAGCFLQFYFFFSLGTSECLLLTVMAFDQYLAICRPLLYPNI
MTGHLCAKLVILCWVCGFLWFLIPIVLISQMPFCGPNIIDHVVCDPGPRF
ALDCVSAPRIQLFCYTLSSLVIFGNFLFIIGSYTLVLKAVLGMPSSTGRH
KAFSTCGSHLAVVSLCYSSLMVMYVSPGLGHSTGMQKIETLFYAMVTPLF
NPLIYSLQNKEIKAALRKVLGSSNII
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 39 65 QIFLFSLFTTTYALTITGNGAIAFVLW
TM2 76 98 MFLGNFSFLEIWYVSSTVPKMLV
TM3 113 133 FLQFYFFFSLGTSECLLLTVM
TM4 156 176 CAKLVILCWVCGFLWFLIPIV
TM5 213 234 FCYTLSSLVIFGNFLFIIGSYT
TM6 256 280 CGSHLAVVSLCYSSLMVMYVSPGLG
TM7 286 305 QKIETLFYAMVTPLFNPLIY

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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