Protein information for: OR52E4



MPSINDTHFYPPFFLLLGIPGLDTLHIWISFPFCIVYLIAIVGNMTILFV
IKTEHSLHQPMFYFLAMLSMIDLGLSTSTIPKMLGIFWFNLQEISFGGCL
LQMFFIHMFTGMETVLLVVMAYDRFVAICNPLQYTMILTNKTISILASVV
VGRNLVLVTPFVFLILRLPFCGHNIVPHTYCEHRGLAGLACAPIKINIIY
GLMVISYIIVDVILIASSYVLILRAVFRLPSQDVRLKAFNTCGSHVCVML
CFYTPAFFSFMTHRFGQNIPHYIHILLANLYVVVPPALNPVIYGVRTKQI
REQIVKIFVQKE
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 HIWISFPFCIVYLIAIVGNMTILFVIK
TM2 63 85 YFLAMLSMIDLGLSTSTIPKMLG
TM3 100 120 LLQMFFIHMFTGMETVLLVVM
TM4 143 163 ISILASVVVGRNLVLVTPFVF
TM5 200 220 YGLMVISYIIVDVILIASSYV
TM6 242 266 CGSHVCVMLCFYTPAFFSFMTHRFG
TM7 274 293 HILLANLYVVVPPALNPVIY

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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