Protein information for: OR52A4



MALPITNGTLFMPFVLTFIGIPGFESVQCWIGIPFCATYVIALIGNSLLL
IIIKSEPSLHEPMYIFLATLGATDISLSTSIVPKMLDIFWFHLPEIYFDA
CLFQMWLIHTFQGIESGVLLAMALDRCVAICYPLRRAIVFTRQLVTYIVV
GVTLRPAILVIPCLLLIKCHLKLYRTKLIYHTYCERVALVKLATEDVYIN
KVYGILGAFIVGGLDFIFITLSYIQIFITVFHLPLKEARLKVFNTCIPHI
YVFFQFYLLAFFFIFYSQIWILYPIICTYHLVQSLPTGPTIPQPLYLWVK
DQTH
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 28 54 QCWIGIPFCATYVIALIGNSLLLIIIK
TM2 65 87 IFLATLGATDISLSTSIVPKMLD
TM3 102 122 LFQMWLIHTFQGIESGVLLAM
TM4 145 165 VTYIVVGVTLRPAILVIPCLL
TM5 203 224 YGILGAFIVGGLDFIFITLSYI
TM6 246 270 CIPHIYVFFQFYLLAFFFIFYSQIW
TM7 278 297 TYHLVQSLPTGPTIPQPLYL

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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