Protein information for: OR51H1P



MTNLNASQANHRNFILTGIPGTPDKNPWLAFPLGFLYTLTLLGNGTILAV
IKVEPSLHEPTYYFLSILALTDVSLSMSTLPSMLSIYWFNAPQIVFDACI
MQMFFIHVFGIVESGVLVSMAFDRFVAIRNPLHYVSILTHDVIRKTGIAV
LTRAVCVVFPVPFLIKCLPFCHSNVLSHSYCLHQNMMRLACASTRINSLY
GLIVVIFTLGLDVLLTLLSYVLTLKTVLGIVSRGERLKTLSTCLSHMSTV
LLFYVPFRLPPXSTDFGMHLSPVVHMVMADIYLLLPPVLNPIVYSVKTKQ
IXRMIFQVFQRQKK
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 NPWLAFPLGFLYTLTLLGNGTILAVIK
TM2 63 85 YFLSILALTDVSLSMSTLPSMLS
TM3 100 120 IMQMFFIHVFGIVESGVLVSM
TM4 143 163 IRKTGIAVLTRAVCVVFPVPF
TM5 200 221 YGLIVVIFTLGLDVLLTLLSYV
TM6 243 267 CLSHMSTVLLFYVPFRLPPXSTDFG
TM7 275 294 HMVMADIYLLLPPVLNPIVY

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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