Protein information for: OR13D2P



MERTNWTEIEFILQGLSGYPRAEKFLFVMCLVMYLVILLGNGTLIILTLL
DARLHTPMYFFLGNLSFLDIWYTSSSIPSMLIHFLSEKKTISFTRCVIQM
SVSYTMGSTECVLLAVMAYDRYVAICNPLRYPIIMGKALCIQMVAVSWGL
GFLNSLTETVLAIRLPFCGKNVINHFVCEILAFVKLACTDTSLNEIIIML
GNVIFLFSPLLLICISYIFILSTVLRINSAEGRKKAFSTCSAHMTVVIVF
YGTILFMYMKAKSKDSAFDKLIALFYGIVTPMLNPIIYSLRNTEVHGAMR
KLMSRPWFWRK
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 EKFLFVMCLVMYLVILLGNGTLIILTL
TM2 60 82 FFLGNLSFLDIWYTSSSIPSMLI
TM3 97 117 VIQMSVSYTMGSTECVLLAVM
TM4 140 160 CIQMVAVSWGLGFLNSLTETV
TM5 197 218 IIMLGNVIFLFSPLLLICISYI
TM6 240 264 CSAHMTVVIVFYGTILFMYMKAKSK
TM7 269 287 KLIALFYGIVTPMLNPIIY

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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