Protein information for: OR2T11



MTNTSSSDFTLLGLLVNSEAAGIVFTVILAVFLGAVTANLVMIFLIQVDS
RLHTPMYFLLSQLSIMDTLFICTTVPKLLADMVSKEKIISFVACGIQIFL
YLTMIGSEFFLLGLMAYDCYVAVCNPLRYPVLMNRKKCLLLAAGAWFGGS
LDGFLLTPITMNVPYCGSRSINHFFCEIPAVLKLACADTSLYETLMYICC
VLMLLIPISIISTSYSLILLTIHRMPSAEGRKKAFTTCSSHLTVVSIFYG
AAFYTYVLPQSFHTPEQDKVVSAFYTIVTPMLNPLIYSLRNKDVIGAFKK
VFACCSSAQKVATSDA
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 21 47 AGIVFTVILAVFLGAVTANLVMIFLIQ
TM2 58 80 FLLSQLSIMDTLFICTTVPKLLA
TM3 95 115 GIQIFLYLTMIGSEFFLLGLM
TM4 138 158 CLLLAAGAWFGGSLDGFLLTP
TM5 195 216 LMYICCVLMLLIPISIISTSYS
TM6 238 262 CSSHLTVVSIFYGAAFYTYVLPQSF
TM7 268 287 DKVVSAFYTIVTPMLNPLIY

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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