Protein information for: OR52B2



MSHTNVTIFHPAVFVLPGIPGLEAYHIWLSIPLCLIYITAVLGNSILIVV
IVMERNLHVPMYFFLSMLAVMDILLSTTTVPKALAIFWLQAHNIAFDACV
TQGFFVHMMFVGESAILLAMAFDRFVAICAPLRYTTVLTWPVVGRIALAV
ITRSFCIIFPVIFLLKRLPFCLTNIVPHSYCEHIGVARLACADITVNIWY
GFSVPIVMVILDVILIAVSYSLILRAVFRLPSQDARHKALSTCGSHLCVI
LMFYVPSFFTLLTHHFGRNIPQHVHILLANLYVAVPPMLNPIVYGVKTKQ
IREGVAHRFFDIKTWC
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 HIWLSIPLCLIYITAVLGNSILIVVIV
TM2 63 85 FFLSMLAVMDILLSTTTVPKALA
TM3 100 120 VTQGFFVHMMFVGESAILLAM
TM4 143 163 VGRIALAVITRSFCIIFPVIF
TM5 200 221 YGFSVPIVMVILDVILIAVSYS
TM6 243 267 CGSHLCVILMFYVPSFFTLLTHHFG
TM7 275 294 HILLANLYVAVPPMLNPIVY

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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