Protein information for: OR2L13



MEKWNHTSNDFILLGLLPPNQTGIFLLCLIILIFFLASVGNSAMIHLIHV
DPRLHTPMYFLLSQLSLMDLMYISTTVPKMAYNFLSGQKGISFLGCGVQS
FFFLTMACSEGLLLTSMAYDRYLAICHSLYYPIRMSKMMCVKMIGGSWTL
GSINSLAHTVFALHIPYCRSRAIDHFFCDVPAMLLLACTDTWVYEYMVFV
STSLFLLFPFIGITSSCGRVLFAVYHMHSKEGRKKAFTTISTHLTVVIFY
YAPFVYTYLRPRNLRSPAEDKILAVFYTILTPMLNPIIYSLRNKEVLGAM
RRVFGIFSFLKE
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 23 49 GIFLLCLIILIFFLASVGNSAMIHLIH
TM2 60 82 FLLSQLSLMDLMYISTTVPKMAY
TM3 97 117 GVQSFFFLTMACSEGLLLTSM
TM4 140 160 CVKMIGGSWTLGSINSLAHTV
TM5 197 218 MVFVSTSLFLLFPFIGITSSCG
TM6 240 264 ISTHLTVVIFYYAPFVYTYLRPRNL
TM7 270 289 DKILAVFYTILTPMLNPIIY

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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