Protein information for: OR52J3



MFYHNKSIFHPVTFFLIGIPGLEDFHMWISGPFCSVYLVALLGNATILLV
IKVEQTLREPMFYFLAILSTIDLALSATSVPRMLGIFWFDAHEINYGACV
AQMFLIHAFTGMEAEVLLAMAFDRYVAICAPLHYATILTSLVLVGISMCI
VIRPVLLTLPMVYLIYRLPFCQAHIIAHSYCEHMGIAKLSCGNIRINGIY
GLFVVSFFVLNLVLIGISYVYILRAVFRLPSHDAQLKALSTCGAHVGVIC
VFYIPSVFSFLTHRFGHQIPGYIHILVANLYLIIPPSLNPIIYGVRTKQI
RERVLYVFTKK
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 HMWISGPFCSVYLVALLGNATILLVIK
TM2 63 85 YFLAILSTIDLALSATSVPRMLG
TM3 100 120 VAQMFLIHAFTGMEAEVLLAM
TM4 143 163 LVGISMCIVIRPVLLTLPMVY
TM5 200 220 YGLFVVSFFVLNLVLIGISYV
TM6 242 266 CGAHVGVICVFYIPSVFSFLTHRFG
TM7 274 293 HILVANLYLIIPPSLNPIIY

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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