Protein information for: OR51B2



MWPNITAAPFLLTGFPGLEAAHHWISIPFFAVYVCILLGNGMLLYLIKHD
HSLHEPMYYFLTMLAGTDLMVTLTTMPTVMGILWVNHREISSVGCFLQAY
FIHSLSVVESGSLLAMAYDRFIAIRNPLRYASIFTNTRVIALGVGVFLRG
FVSILPVILRLFSFSYCKSHVITRAFCLHQEIMRLACADITFNRLYPVIL
ISLTIFLDSLIILFSYILILNTVIGIASGEERAKALNTCISHISCVLIFY
VTVMGLTFIYRFGKNVPEVVHIIMSYIYFLFPPLMNPVIYSIKTKQIQYG
IIRLLSKHRFSR
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 22 48 HHWISIPFFAVYVCILLGNGMLLYLIK
TM2 59 81 YFLTMLAGTDLMVTLTTMPTVMG
TM3 96 116 FLQAYFIHSLSVVESGSLLAM
TM4 139 159 VIALGVGVFLRGFVSILPVIL
TM5 196 217 YPVILISLTIFLDSLIILFSYI
TM6 239 263 CISHISCVLIFYVTVMGLTFIYRFG
TM7 271 290 HIIMSYIYFLFPPLMNPVIY

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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