Protein information for: OR2A12



MESNQTWITEVILLGFQVDPALELFLFGFFLLFYSLTLMGNGIILGLIYL
DSRLHTPMYVFLSHLAIVDMSYASSTVPKMLANLVMHKKVISFAPCILQT
FLYLAFAITECLILVMMCYDRYVAICHPLQYTLIMNWRVCTVLASTCWIF
SFLLALVHITLILRLPFCGPQKINHFFCQIMSVFKLACADTRLNQVVLFA
GSAFILVGPLCLVLVSYLHILVAILRIQSGEGRRKAFSTCSSHLCVVGLF
FGSAIVMYMAPKSSHSQERRKILSLFYSLFNPILNPLIYSLRNAEVKGAL
KRVLWKQRSM
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 ELFLFGFFLLFYSLTLMGNGIILGLIY
TM2 60 82 VFLSHLAIVDMSYASSTVPKMLA
TM3 97 117 ILQTFLYLAFAITECLILVMM
TM4 140 160 CTVLASTCWIFSFLLALVHIT
TM5 197 218 VLFAGSAFILVGPLCLVLVSYL
TM6 240 264 CSSHLCVVGLFFGSAIVMYMAPKSS
TM7 270 289 RKILSLFYSLFNPILNPLIY

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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