Protein information for: OR52L1



MLLSNSSWRLSQPSFLLVGIPGLEESQHWIALPLGILYLLALVGNVTILF
IIWMDPSLHQSMYLFLSMLAAIDLVLASSTAPKALAVLLVHAHEIGYIVC
LIQMFFIHAFSSMESGVLVAMALDCYVAICHPLHHSTILHPGVIGCIGMV
VLVRGLLLLIPFPILLGKLIFCQATIIGHAYCEHMAVVKLACSETTVNRA
YGLTMALLVIGLDVLAIGVSYAHILQAVLKVPGSEARLKAFSTCGSHICV
ILVFYVPGIFSFLTHRFGHHVPHHVHVLLATWYLLMPPALNPLVYGVKTQ
QIRQRVLRVFTQKD
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 27 53 QHWIALPLGILYLLALVGNVTILFIIW
TM2 64 86 LFLSMLAAIDLVLASSTAPKALA
TM3 101 121 LIQMFFIHAFSSMESGVLVAM
TM4 144 164 IGCIGMVVLVRGLLLLIPFPI
TM5 201 222 YGLTMALLVIGLDVLAIGVSYA
TM6 244 268 CGSHICVILVFYVPGIFSFLTHRFG
TM7 276 295 HVLLATWYLLMPPALNPLVY

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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