Protein information for: OR2T4



MGLFRQSKHPMANITWMANHTGWSDFILLGLFRQSKHPALLCVVIFVVFL
MALSGNAVLILLIHCDAHLHTPMYFFISQLSLMDMAYISVTVPKMLLDQV
MGVNKISAPECGMQMFFYVTLAGSEFFLLATMAYDRYVAICHPLRYPVLM
NHRVCLFLSSGCWFLGSVDGFTFTPITMTFPFRGSREIHHFFCEVPAVLN
LSCSDTSLYEIFMYLCCVLMLLIPVVIISSSYLLILLTIHGMNSAEGRKK
AFATCSSHLTVVILFYGAAIYTYMLPSSYHTPEKDMMVSVFYTILTPVVN
PLIYSLRNKDVMGALKKMLTVEPAFQKAME
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 38 64 PALLCVVIFVVFLMALSGNAVLILLIH
TM2 75 97 FFISQLSLMDMAYISVTVPKMLL
TM3 112 132 GMQMFFYVTLAGSEFFLLATM
TM4 155 175 CLFLSSGCWFLGSVDGFTFTP
TM5 212 233 FMYLCCVLMLLIPVVIISSSYL
TM6 255 279 CSSHLTVVILFYGAAIYTYMLPSSY
TM7 285 304 DMMVSVFYTILTPVVNPLIY

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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