Protein information for: OR51H2P



MSPLNQTTENHQSFFTLTGIPGMPEKDLWMALPLCLLYSTTILGNVTILV
VIKVEQSLHSPCIFLAMLAATDLSLSLSSMPTMVSVHWFNWRSITFNGCL
IQMFFIHTFGGVESGVLVAMAFDRFVAIRFPLHYATILTHSVISKIAAAI
LLRSVGAVLPVPFLIKRLPFCHSNVLSHAYCLHQDAMRLACADTGVNSIY
GLLAVIFIIVLDALILLASYILILQAVLSIASQEDRLKALNTCLSHIXVL
LFYVPLIGMTLIHRYGKHLSPLIHTFMANIYLLLPPVLNPIVYSVRTKQI
XXQIVQAFCGARVSP
No N-glycosylation site was found.
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 27 53 DLWMALPLCLLYSTTILGNVTILVVIK
TM2 63 85 IFLAMLAATDLSLSLSSMPTMVS
TM3 100 120 LIQMFFIHTFGGVESGVLVAM
TM4 143 163 ISKIAAAILLRSVGAVLPVPF
TM5 200 221 YGLLAVIFIIVLDALILLASYI
TM6 243 266 CLSHIXVLLFYVPLIGMTLIHRYG
TM7 274 293 HTFMANIYLLLPPVLNPIVY

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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