Protein information for: OR51B4



MWYNNSAGPFLLTGFLGSEAVHYRISMSFFVIYFSVLFGNGTLLVLIWND
HSLHEPMYYFLAMLADTDLGMTFTTMPTVLGVLLLDQREIAHAACFTQSF
IHSLAIVESGILLVLAYDCFIAIRTPLRYNCILTNSRVMNIGLGVLMRGF
MSILPIILSLYCYPYCGSRALLHTFCLHQDVIKLACADITFNHIYPIIQT
SLTVFLDALIIIFSYILILKTVMGIASGQEEAKSLNTCVSHISCVLVFHI
TVMGLSFIHRFGKHAPHVVPITMSYVHFLFPPFVNPIIYSIKTKQIQRSI
IRLFSGQSRA
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 HYRISMSFFVIYFSVLFGNGTLLVLIW
TM2 59 81 YFLAMLADTDLGMTFTTMPTVLG
TM3 96 115 FTQSFIHSLAIVESGILLVL
TM4 138 158 VMNIGLGVLMRGFMSILPIIL
TM5 195 216 YPIIQTSLTVFLDALIIIFSYI
TM6 238 262 CVSHISCVLVFHITVMGLSFIHRFG
TM7 270 288 ITMSYVHFLFPPFVNPIIY

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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