Protein information for: OR2B2



MNWVNKSVPQEFILLVFSDQPWLEIPPFVMFLFSYILTIFGNLTIILVSH
VDFKLHTPMYFFLSNLSLLDLCYTTSTVPQMLVNICNTRKVISYGGCVAQ
LFIFLALGSTECLLLAVMCFDRFVAICRPLHYSIIMHQRLCFQLAAASWI
SGFSNSVLQSTWTLKMPLCGHKEVDHFFCEVPALLKLSCVDTTANEAELF
FISVLFLLIPVTLILISYAFIVQAVLRIQSAEGQRKAFGTCGSHLIVVSL
FYGTAISMYLQPPSPSSKDRGKMVSLFCGIIAPMLNPLIYTLRNKEVKEA
FKRLVAKSLLNQEIRNMQMISFAKDTVLTYLTNFSASCPIFVITIENYCN
LPQRKFP
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 24 50 EIPPFVMFLFSYILTIFGNLTIILVSH
TM2 61 83 FFLSNLSLLDLCYTTSTVPQMLV
TM3 98 118 VAQLFIFLALGSTECLLLAVM
TM4 141 161 CFQLAAASWISGFSNSVLQST
TM5 198 219 ELFFISVLFLLIPVTLILISYA
TM6 241 265 CGSHLIVVSLFYGTAISMYLQPPSP
TM7 271 290 GKMVSLFCGIIAPMLNPLIY

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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