Protein information for: OR11J2P



VRTLETTNITGFVNEFILLGFPCRWEIQILLFVVFSLIYLLTLLGNTSII
CAVWSSQKLHTPMYILLANFSFLEICCVSSDVPIMAANLISQTQSISCAG
CLLRFYFFSMCAAECLFLSVMSFDRFPAICRPLHYPTLMTHHVCVIFVIF
CWVGGCLWLLTPLTLISQVLFCGPNTIDHFFCDLAPLLALSCAPIPGITL
TCGIISALIIFLTFLYILGTYFCVLSTVLQVPSGLGRHKAFSTCGCHLAV
VSLFYGSLMVMYVSPGSGDYHGIKKFATLFYTLSTPFFNPLIYSFRNKDM
KEALKKFLRNRHTVD
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 28 54 QILLFVVFSLIYLLTLLGNTSIICAVW
TM2 65 87 ILLANFSFLEICCVSSDVPIMAA
TM3 102 121 LLRFYFFSMCAAECLFLSVM
TM4 144 164 CVIFVIFCWVGGCLWLLTPLT
TM5 201 222 TCGIISALIIFLTFLYILGTYF
TM6 244 268 CGCHLAVVSLFYGSLMVMYVSPGSG
TM7 274 293 KKFATLFYTLSTPFFNPLIY

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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