Protein information for: OR5AK4P



MEQNNGTEVTEFILLGFAGQHKSWHILSIAFLAIYVVTPVGNIGMILLIK
IDASLHIPMXIFLQHLAFVDLCYTSAITPKMLKNFVETKKSISCIGCMVQ
LLVYGTFATSDCYILAAMAVDRYVAFCNPLHYPGVMSQRLCIKLLVSSYV
MGFLNASINISFTFSLNFCKSKTINHFFCDEPPIIALPCSNIDLNIMLLT
VFVGLNLMCTVMVVIISCIYVLVAILRISSAAGKKKVFSTCASHLTAVTI
FYGVLSYMYLCHRINESQKQEKVASVFYGIIIPMLNPLIYSQRNQDVIEA
IKLTEKKYF
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 24 50 WHILSIAFLAIYVVTPVGNIGMILLIK
TM2 61 83 IFLQHLAFVDLCYTSAITPKMLK
TM3 98 118 MVQLLVYGTFATSDCYILAAM
TM4 141 161 CIKLLVSSYVMGFLNASINIS
TM5 198 219 LLTVFVGLNLMCTVMVVIISCI
TM6 241 265 CASHLTAVTIFYGVLSYMYLCHRIN
TM7 271 290 EKVASVFYGIIIPMLNPLIY

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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