Protein information for: OR4K2



MDVGNKSTMSEFVLLGLSNSWELQMFFFMVFSLLYVATMVGNSLIVITVI
VDPHLHSPMYFLLTNLSIIDMSLASFATPKMITDYLTGHKTISFDGCLTQ
IFFLHLFTGTEIILLMAMSFDRYIAICKPLHYASVISPQVCVALVVASWI
MGVMHSMSQVIFALTLPFCGPYEVDSFFCDLPVVFQLACVDTYVLGLFMI
STSGIIALSCFIVLFNSYVIVLVTVKHHSSRGSSKALSTCTAHFIVVFLF
FGPCIFIYMWPLSSFLTDKILSVFYTIFTPTLNPIIYTLRNQEVKIAMRK
LKNRFLNFNKAMPS
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 QMFFFMVFSLLYVATMVGNSLIVITVI
TM2 61 83 FLLTNLSIIDMSLASFATPKMIT
TM3 98 118 LTQIFFLHLFTGTEIILLMAM
TM4 141 161 CVALVVASWIMGVMHSMSQVI
TM5 198 219 FMISTSGIIALSCFIVLFNSYV
TM6 240 264 CTAHFIVVFLFFGPCIFIYMWPLSS
TM7 269 286 ILSVFYTIFTPTLNPIIY

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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