Protein information for: OR52B4



MPTVNHSGTSHTVFHLLGIPGLQDQHMWISIPFFISYVTALLGNSLLIFI
ILTKRSLHEPMYLFLCMLAGADIVLSTCTIPQALAIFWFRAGDISLDRCI
TQLFFIHSTFISESGILLVMAFDHYIAICYPLRYTTILTNALIKKICVTV
SLRSYGTIFPIIFLLKRLTFCQNNIIPHTFCEHIGLAKYACNDIRINIWY
GFSILMSTVVLDVVLIFISYMLILHAVFHMPSPDACHKALNTFGSHVCII
ILFYGSGIFTILTQRFGRHIPPCIHIPLANVCILAPPMLNPIIYGIKTKQ
IQEQVVQFLFIKQK
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 26 52 HMWISIPFFISYVTALLGNSLLIFIIL
TM2 63 85 LFLCMLAGADIVLSTCTIPQALA
TM3 100 120 ITQLFFIHSTFISESGILLVM
TM4 143 163 IKKICVTVSLRSYGTIFPIIF
TM5 200 221 YGFSILMSTVVLDVVLIFISYM
TM6 243 267 FGSHVCIIILFYGSGIFTILTQRFG
TM7 275 294 HIPLANVCILAPPMLNPIIY

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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