Protein information for: OR52B3P



MTTHNSTGSSHSLFILLSIPGLEDQHTWMSLPFFISYLVAFLGNSLIIFI
IITECSLHEPMYLFLCMLAVADLILSTTTVPKALAIFWFYAGAISLGGCV
TQIFFIHATFIEESGILLAMALDRYVAICDPLHYTTVLSRAKITKIGLAV
VLRSFCVIMPDVFLVKRLPFCHSNLLPHTYCEHMAVAKFACADIHVNVWY
GLSVLLYTVVLDALLILVSYSFILYTGFHLPSPRSRQKALGTCGSHLRVI
SMFYLPGIFTIITQRFGHHVPLHTHILLANVCVLAPPMLNPIIYGINTRQ
IQECVLSLLSSQRK
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 HTWMSLPFFISYLVAFLGNSLIIFIII
TM2 63 85 LFLCMLAVADLILSTTTVPKALA
TM3 100 120 VTQIFFIHATFIEESGILLAM
TM4 143 163 ITKIGLAVVLRSFCVIMPDVF
TM5 200 221 YGLSVLLYTVVLDALLILVSYS
TM6 243 267 CGSHLRVISMFYLPGIFTIITQRFG
TM7 275 294 HILLANVCVLAPPMLNPIIY

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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