Protein information for: OR10Q1



MPVGKLVFNQSEPTEFVFRAFTTATEFQVLLFLLFLLLYLMILCGNTAII
WVVCTHSTLRTPMYFFLSNLSFLELCYTTVVVPLMLSNILGAQKPISLAG
CGAQMFFFVTLGSTDCFLLAIMAYDRYVAICHPLHYTLIMTRELCTQMLG
GALGLALFPSLQLTALIFTLPFCGHQEINHFLCDVPPVLRLACADIRVHQ
AVLYVVSILVLTIPFLLICVSYVFITCAILSIRSAEGRRRAFSTCSFHLT
VVLLQYGCCSLVYLRPRSSTSEDEDSQIALVYTFVTPLLNPLLYSLRNKD
VKGALRSAIIRKAASDAN
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 28 54 QVLLFLLFLLLYLMILCGNTAIIWVVC
TM2 65 87 FFLSNLSFLELCYTTVVVPLMLS
TM3 102 122 GAQMFFFVTLGSTDCFLLAIM
TM4 145 165 CTQMLGGALGLALFPSLQLTA
TM5 202 223 VLYVVSILVLTIPFLLICVSYV
TM6 245 269 CSFHLTVVLLQYGCCSLVYLRPRSS
TM7 275 294 DSQIALVYTFVTPLLNPLLY

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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