Protein information for: OR52D1



MSDSNLSNHLPDTFFLTGIPGLEAAHFWIAIPFCAMYLVALVGNAALILV
IAMDNALHAPMYLFLCLLSLTDLALSSTTVPKMLAILWLHAGEISFGGCL
AQMFCVHSIYALESSILLAMAFDRYVAICNPLRYTTILNHAVIGRIGFVG
LFRSVAIVSPFIFLLRRLPYCGHRVMTHTYCEHMGIARLACANITVNIVY
GLTVALLAMGLDSILIAISYGFILHAVFHLPSHDAQHKALSTCGSHIGII
LVFYIPAFFSFLTHRFGHEVPKHVHIFLANLYVLVPPVLNPILYGARTKE
IRSRLLKLLHLGKTSI
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 HFWIAIPFCAMYLVALVGNAALILVIA
TM2 63 85 LFLCLLSLTDLALSSTTVPKMLA
TM3 100 120 LAQMFCVHSIYALESSILLAM
TM4 143 163 IGRIGFVGLFRSVAIVSPFIF
TM5 200 221 YGLTVALLAMGLDSILIAISYG
TM6 243 267 CGSHIGIILVFYIPAFFSFLTHRFG
TM7 275 294 HIFLANLYVLVPPVLNPILY

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.
HORDE homepage