Protein information for: OR2A14



MEGNKTWITDITLPRFQVGPALEILLCGLFSAFYTLTLLGNGVIFGIICL
DCKLHTPMYFFLSHLAIVDISYASNYVPKMLTNLMNQESTISFFPCIMQT
FLYLAFAHVECLILVVMSYDRYADICHPLRYNSLMSWRVCTVLAVASWVF
SFLLALVPLVLILSLPFCGPHEINHFFCEILSVLKLACADTWLNQVVIFA
ACVFILVGPLCLVLVSYLRILAAILRIQSGEGRRKAFSTCSSHLCVVGLF
FGSAIVTYMAPKSRHPEEQQKVLSLFYSLFNPMLNPLIYSLRNAEVKGAL
RRALRKERLT
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 23 49 EILLCGLFSAFYTLTLLGNGVIFGIIC
TM2 60 82 FFLSHLAIVDISYASNYVPKMLT
TM3 97 117 IMQTFLYLAFAHVECLILVVM
TM4 140 160 CTVLAVASWVFSFLLALVPLV
TM5 197 218 VIFAACVFILVGPLCLVLVSYL
TM6 240 264 CSSHLCVVGLFFGSAIVTYMAPKSR
TM7 270 289 QKVLSLFYSLFNPMLNPLIY

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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