Protein information for: OR52N4



MLTLNKTDLIPASFILNGVPGLEDTQLWISFPFCSMYVVAMVGNCGLLYL
IHYEDALHKPMYYFLAMLSFTDLVMCSSTIPKALCIFWFHLKDIGFDECL
VQMFFTHTFTGMESGVLMLMALDRYVAICYPLRYSTILTNPVIAKVGTAT
FLRGVLLIIPFTFLTKLLPYCRGNILPHTYCDHMSVAKLSCGNVKVNAIY
GLMVALLIWGFDILCITNSYTMILRAVVSLSSADARQKAFNTCTAHICAI
VFSYTPAFFSFFSHRFGEHIIPPSCHIIVANIYLLLPPTMNPIVYGVKTK
QIRDCVIRILSGSKDTKSYSM
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 26 52 QLWISFPFCSMYVVAMVGNCGLLYLIH
TM2 63 85 YFLAMLSFTDLVMCSSTIPKALC
TM3 100 120 LVQMFFTHTFTGMESGVLMLM
TM4 143 163 IAKVGTATFLRGVLLIIPFTF
TM5 200 221 YGLMVALLIWGFDILCITNSYT
TM6 243 267 CTAHICAIVFSYTPAFFSFFSHRFG
TM7 276 295 HIIVANIYLLLPPTMNPIVY

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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