Protein information for: OR2A13P



MGVNQSWVTEFILVGFQLSAEMEVLLFXIFSLLYIFSLLANGMILGLICL
DHILPTPMYFFLSHLAIIDMSYASNNVPKMLANLMNKKRTISFLPCIMQT
YLHFSFAATECLILVVMSYDRYVAICHPLQYTVIMSWRVCTILALTSWSC
GFALSLVHAILLLRLPFCGPRDVNHLFCEILSVLKLACSDTWVNQVVIFA
TCVFVLVGPLCLMLVSYMHILWAILKIQTKEGRIKAFSTCSSHLCVVGLF
FGIAMVVYIVPDSNQREEQEKMLSLFHSVLNPILNPLIYSLRNAQVKGAL
HRALQRTLSM
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 EVLLFXIFSLLYIFSLLANGMILGLIC
TM2 60 82 FFLSHLAIIDMSYASNNVPKMLA
TM3 97 117 IMQTYLHFSFAATECLILVVM
TM4 140 160 CTILALTSWSCGFALSLVHAI
TM5 197 218 VIFATCVFVLVGPLCLMLVSYM
TM6 240 264 CSSHLCVVGLFFGIAMVVYIVPDSN
TM7 270 289 EKMLSLFHSVLNPILNPLIY

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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