Protein information for: OR12D2



MLNTTSVTEFLLLGVTDIQELQPFLFVVFLTIYFISVTGNGAVLMIVISD
PRLHSLMYFFLGNLSYLDICYSTVTLPKMLQNFLSTHKAISFLGCISQLH
FFHFLGSTESMLFAVMAFDLSVAICKPLRYTVIMNPQLCTQMAITIWVIG
FFHALLHSVMTSRLNFCGSNRIHHFLCDIKPLLKLACGNTELNQWLLSTV
TGTIAMGPFFLTLLSYFYIITYLFFKTRSCSMLCKALSTCASHFMVVILF
YAPVLFTYIHPALESFMDQDRIVAIMYTVVTPVLNPLIYTLRNKEVKGAL
GRVIRRL
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 QPFLFVVFLTIYFISVTGNGAVLMIVI
TM2 59 81 FFLGNLSYLDICYSTVTLPKMLQ
TM3 96 116 ISQLHFFHFLGSTESMLFAVM
TM4 139 159 CTQMAITIWVIGFFHALLHSV
TM5 196 217 LLSTVTGTIAMGPFFLTLLSYF
TM6 240 264 CASHFMVVILFYAPVLFTYIHPALE
TM7 270 289 DRIVAIMYTVVTPVLNPLIY

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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