Protein information for: OR52S1P



MSAYNNTNARPSTFILIGIPGLEAAHIWISIPFCVVYLLALLGNGSLLFI
IKTEPSLHEPMYLFLCMLAVVDLVVCSTAVPKLLSLFWFHDGEIRFETCL
TQMFLIHSCSTMESGFFLAMAFDRYVAICNPLRHSAILTRAVIGRVGLAI
VLRGIALLSPHSFLLHWLPYCRTHIISHTYCEFMALIRIACAETKFRRAY
SLIVAFLTGVVDFILIIYSYVLILHTVFQLPSKDARLKSLGTCGSHVCVI
LVSYTPAFFSFLTHRFGHHVAPHFHIFVANIYLLVPPMVNPIIYGVRTKR
IWDRFLKVFSFSKPLSKSFLLVRNI
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 HIWISIPFCVVYLLALLGNGSLLFIIK
TM2 63 85 LFLCMLAVVDLVVCSTAVPKLLS
TM3 100 120 LTQMFLIHSCSTMESGFFLAM
TM4 143 163 IGRVGLAIVLRGIALLSPHSF
TM5 200 221 YSLIVAFLTGVVDFILIIYSYV
TM6 243 267 CGSHVCVILVSYTPAFFSFLTHRFG
TM7 275 294 HIFVANIYLLVPPMVNPIIY

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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