Protein information for: OR9A3P



MLGNYSSATEFFLLGFPGSQEVRRILFVNFFFLYAVTVMGNTVIIVTVCV
DKHLQSPMYFFLGHLCVLEILITSTAAPFMLAGLLLPSTQIMSLTCLCCT
AIYLSLGTSELALMGVMAVDHYVAVCNPLRYNIIMNSSTCVWMVIVSWVF
GFLFQIWPVYATFQLTFCKSNVLDHFYCDXGQLLKVSCEDTLFTEFILFL
MAVFIIIGSLIPTIVSYTYIISTILKIPLASGWRKSFSTCASHFTCVVIG
YSSCLFLYTKPKQTQAAKYNRIASLLVLVVTPFLNPFIFTLRNDKFIQAF
GEAXNTAINSSEFSSVLGTI
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 RRILFVNFFFLYAVTVMGNTVIIVTVC
TM2 60 82 FFLGHLCVLEILITSTAAPFMLA
TM3 97 117 LCCTAIYLSLGTSELALMGVM
TM4 140 160 CVWMVIVSWVFGFLFQIWPVY
TM5 197 218 ILFLMAVFIIIGSLIPTIVSYT
TM6 240 264 CASHFTCVVIGYSSCLFLYTKPKQT
TM7 270 289 NRIASLLVLVVTPFLNPFIF

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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