Protein information for: OR4K16P



ILIIFSSLXITSAAQIQLXGWSNKSVVTEFNLLGLSSSWELQVFFFFIFS
VFYGAAVLGNILIIITVIIDSHLHSPMYFLLSNLSSIDVCQATFATPKMI
ADFLNEHKTTTFQGCMSQIFFLHVFGGSEMVLLVAMAYDRYIAICKPLHY
MTIMNRRVXTVLVGVSWAIGISHSATHLAFKVNLPFCGPNRVDNFFCDLL
LVIKLACLDTYGFEILVLTNSGLLSLMCFLLLLISDTIILATVHRQASDG
MSKALSTLSAHITVVLLFFGPLIFIYIWPFESFPIDKFISVFFTVFTPLL
NPMIYTLRNKDIKEAMRKLRRXHVGSKQGFXTTTKK
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 42 68 QVFFFFIFSVFYGAAVLGNILIIITVI
TM2 79 101 FLLSNLSSIDVCQATFATPKMIA
TM3 116 136 MSQIFFLHVFGGSEMVLLVAM
TM4 159 179 XTVLVGVSWAIGISHSATHLA
TM5 216 237 LVLTNSGLLSLMCFLLLLISDT
TM6 258 282 LSAHITVVLLFFGPLIFIYIWPFES
TM7 287 304 FISVFFTVFTPLLNPMIY

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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