Protein information for: OR52H2P



MYNMSDHGTGLFILLGIPGLEQYHVWISIPFCLIYLMAVVANSILLYLIV
VEHSLHAPMFFFLSMLAITDLILSTTCVPKTLSIFWFGPQISFPGCLTQL
FFLHYSFVLDSAILLAMAFDRYMAICSPLRYTTILTPKTIVKIAVGICFR
SFCVFVPCVFLVNRLPFCRTHIISHTYCEHIGVAQLACADISINIWCGFC
VPIMTVMTDVILIAVSYTLILCAVFCLPSQDARQKALCSCGSHVCVILIF
YIPAFFSILAHCFGHNVPHTFHIMFANLYVIIPPALNSIVYRIKTKQIQN
RILLLFPKGSQ
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 HVWISIPFCLIYLMAVVANSILLYLIV
TM2 61 83 FFLSMLAITDLILSTTCVPKTLS
TM3 97 117 LTQLFFLHYSFVLDSAILLAM
TM4 140 160 IVKIAVGICFRSFCVFVPCVF
TM5 197 218 CGFCVPIMTVMTDVILIAVSYT
TM6 240 264 CGSHVCVILIFYIPAFFSILAHCFG
TM7 272 291 HIMFANLYVIIPPALNSIVY

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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