Protein information for: OR52B1P



MFGANLTTFHPTLFILLGIPGLEQYHIWLSIPFYLMYITAVLGNGALILV
VLSEHTLHVFLSMLAGTDILLSTTTVPKALAIFWVHAGEIAFDACITQMF
FIHVAFVAESGILLAMAFDSYVAICTPLRYTTILTSMVNGKMTLTIWGQS
IGTIFPVIFLLKRLPYCQTNIIPHSYCEHIGVAQLACADITVNIWYGFSV
PMASVLVDVAFIGFSYTLILQAVFRLPSQESQHKALNTCGSTLVVVLLFF
IPSFFTFLTHRFGKNIPHHVHILLANLYLLVPPMLNPIIYGEKTKQIRDS
MAHMLSVVGKSXDIMVSSQ
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 HIWLSIPFYLMYITAVLGNGALILVVL
TM2 59 80 FLSMLAGTDILLSTTTVPKALA
TM3 96 116 ITQMFFIHVAFVAESGILLAM
TM4 139 159 NGKMTLTIWGQSIGTIFPVIF
TM5 196 217 YGFSVPMASVLVDVAFIGFSYT
TM6 239 263 CGSTLVVVLLFFIPSFFTFLTHRFG
TM7 271 290 HILLANLYLLVPPMLNPIIY

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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