Protein information for: OR10C1



MSANTSMVTEFLLLGFSHLADLQGLLFSVFLTIYLLTVAGNFLIVVLVST
DAALQSPMYFFLRTLSALEIGYTSVTVPLLLHHLLTGRRHISRSGCALQM
FFFLFFGATECCLLAAMAYDRYAAICEPLRYPLLLSHRVCLQLAGSAWAC
GVLVGLGHTPFIFSLPFCGPNTIPQFFCEIQPVLQLVCGDTSLNELQIIL
ATALLILCPFGLILGSYGRILVTIFRIPSVAGRRKAFSTCSSHLIVVSLF
YGTALFIYIRPKASYDPATDPLVSLFYAVVTPILNPIIYSLRNTEVKAAL
KRTIQKTVPMEI
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 23 49 QGLLFSVFLTIYLLTVAGNFLIVVLVS
TM2 60 82 FFLRTLSALEIGYTSVTVPLLLH
TM3 97 117 ALQMFFFLFFGATECCLLAAM
TM4 140 160 CLQLAGSAWACGVLVGLGHTP
TM5 197 218 QIILATALLILCPFGLILGSYG
TM6 240 264 CSSHLIVVSLFYGTALFIYIRPKAS
TM7 270 289 DPLVSLFYAVVTPILNPIIY

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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