Protein information for: OR4K13



MERANHSVVSEFILLGLSKSQNLQILFFLGFSVVFVGIVLGNLLILVTVT
FDSLLHTPMYFLLSNLSCIDMILASFATPKMIVDFLRERKTISWWGCYSQ
MFFMHLLGGSEMMLLVAMAIDRYVAICKPLHYMTIMSPRVLTGLLLSSYA
VGFVHSSSQMAFMLTLPFCGPNVIDSFFCDLPLVIKLACKDTYILQLLVI
ADSGLLSLVCFLLLLVSYGVIIFSVRYRAASRSSKAFSTLSAHITVVTLF
FAPCVFIYVWPFSRYSVDKILSVFYTIFTPLLNPIIYTLRNQEVKAAIKK
RLCI
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 QILFFLGFSVVFVGIVLGNLLILVTVT
TM2 61 83 FLLSNLSCIDMILASFATPKMIV
TM3 98 118 YSQMFFMHLLGGSEMMLLVAM
TM4 141 161 LTGLLLSSYAVGFVHSSSQMA
TM5 198 219 LVIADSGLLSLVCFLLLLVSYG
TM6 240 264 LSAHITVVTLFFAPCVFIYVWPFSR
TM7 269 286 ILSVFYTIFTPLLNPIIY

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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