Protein information for: OR2T32P



MEMRNTTPDFILLGLFNHTRAHQVLFMMVLSIVLTSLFGNSLMILLIHRD
GRLHTPMYFLLSQLSLMDVMLVSTTVPKMAADYLTGNKAISRAGCGVQIF
FLPTLGGGECFLLAAMAYDRYAAVCHPLRYPTLMSWQLCLRMTMSSWLLG
AADGLLQAVATLSFPYCGAHEIDHFFCEAPVLVRLACADTSVFENAMYIC
CVLMLLVPFSLILSSYGLILAAVLHMRSTEARKKAFATCSSHVAVVGLFY
GAAIFTYMRPKSHRSTNHDKVVSAFYSMFTPLLNPLIYSVRNSEVKEALK
RWLGTCVNLKHQQNEAHRSR
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 22 48 HQVLFMMVLSIVLTSLFGNSLMILLIH
TM2 59 81 FLLSQLSLMDVMLVSTTVPKMAA
TM3 96 116 GVQIFFLPTLGGGECFLLAAM
TM4 139 159 CLRMTMSSWLLGAADGLLQAV
TM5 196 217 AMYICCVLMLLVPFSLILSSYG
TM6 239 263 CSSHVAVVGLFYGAAIFTYMRPKSH
TM7 269 288 DKVVSAFYSMFTPLLNPLIY

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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