Protein information for: OR2H4P



MIIICNDSHSDFILLGFSNKPHLEKILFVIIFIFYFLTLAGNMVIVLVSL
KDPKLHIPMYFFLSNLSLVDLCLTSSCVPQMLINFWGPEKTISYIGCAIQ
LYVFLWLGATEYVLLVVMAVDCYVAVCHPLQNTMIMHPKLCLQLAILAWG
TGLAQSLIQSPATLRLPFCSQRMVDDVVCEVPALIQLSSTDTTYSEIQMS
IASVVLLVMPLIIILSSSGAIAKAVLRIKSTAGQKKAFGTCISHLLVVSL
FYGTVTGVYLQPKNHYPHEWGKFLTLFYTVVTPTLNPLIYTLRNKEVKGA
LIRLGRRTWDSQNN
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 24 50 EKILFVIIFIFYFLTLAGNMVIVLVSL
TM2 61 83 FFLSNLSLVDLCLTSSCVPQMLI
TM3 98 118 AIQLYVFLWLGATEYVLLVVM
TM4 141 161 CLQLAILAWGTGLAQSLIQSP
TM5 198 219 QMSIASVVLLVMPLIIILSSSG
TM6 241 265 CISHLLVVSLFYGTVTGVYLQPKNH
TM7 271 289 KFLTLFYTVVTPTLNPLIY

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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