Protein information for: OR8G3P
KIVDPGNHSSVTESILAGLSEQPELQLRLFLLFLGICVVTVVGNLGMITL
IGLSSHLHTPMYYFLSSLSFIDFCHSTVITPKMLVNFATEKNIISYPECM
AQLYLFSIFAIAECHMLAAMAYDCYVAICSPLLYNVIMSYHHCFWLTVGV
YILGILGSTIHTSFMLRLFLCKTNVINHYFCDLFPLLGLSCSSTYINELL
VLVLSAFNILMPALTILASYIFIIASILRIHSTEGRSKAFSTCSSHILAV
AVFFGSAAFMYLQPSSVSSMDQRKVSSVFYTTIVPMLNPLIYSLRNKDVK
LAVKKILHQTAC
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 | QLRLFLLFLGICVVTVVGNLGMITLIG |
| TM2 | 63 | 85 | YFLSSLSFIDFCHSTVITPKMLV |
| TM3 | 100 | 120 | MAQLYLFSIFAIAECHMLAAM |
| TM4 | 143 | 163 | CFWLTVGVYILGILGSTIHTS |
| TM5 | 200 | 221 | LVLVLSAFNILMPALTILASYI |
| TM6 | 243 | 267 | CSSHILAVAVFFGSAAFMYLQPSSV |
| TM7 | 273 | 292 | RKVSSVFYTTIVPMLNPLIY |
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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