Protein information for: OR2AP1



MKNKTVLTEFILLGLTDVPELQVAVFTFLFLAYLLSILGNLTILILTLLD
SHLQTPMYFFLRNFSFLEISFTNIFIPRVLISITTGNKSISFAGCFTQYF
FAMFLGATEFYLLAAMSYDRYVAICKPLHYTTIMSSRICIQLIFCSWLGG
LMAIIPTITLMSQQDFCASNRLNHYFCDYEPLLELSCSDTSLIEKVVFLV
ASVTLVVTLVLVILSYAFIIKTILKLPSAQQRTKAFSTCSSHMIVISLSY
GSCMFMYINPSAKEGDTFNKGVALLITSVAPLLNPFIYTLRNQQVKQPFK
DMVKKLLNL
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 22 48 QVAVFTFLFLAYLLSILGNLTILILTL
TM2 59 81 FFLRNFSFLEISFTNIFIPRVLI
TM3 96 116 FTQYFFAMFLGATEFYLLAAM
TM4 139 159 CIQLIFCSWLGGLMAIIPTIT
TM5 196 217 VVFLVASVTLVVTLVLVILSYA
TM6 239 263 CSSHMIVISLSYGSCMFMYINPSAK
TM7 269 287 KGVALLITSVAPLLNPFIY

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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