Protein information for: OR51Q1



MSQVTNTTQEGIYFILTDIPGFEASHIWISIPVCCLYTISIMGNTTILTV
IRTEPSVHQRMYLFLSMLALTDLGLTLTTLPTVMQLLWFNVRRISSEACF
AQFFFLHGFSFMESSVLLAMSVDCYVAICCPLHYASILTNEVIGRTGLAI
ICCCVLAVLPSLFLLKRLPFCHSHLLSRSYCLHQDMIRLVCADIRLNSWY
GFALALLIIIVDPLLIVISYTLILKNILGTATWAERLRALNNCLSHILAV
LVLYIPMVGVSMTHRFAKHASPLVHVIMANIYLLAPPVMNPIIYSVKNKQ
IQWGMLNFLSLKNMHSR
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 26 52 HIWISIPVCCLYTISIMGNTTILTVIR
TM2 63 85 LFLSMLALTDLGLTLTTLPTVMQ
TM3 100 120 FAQFFFLHGFSFMESSVLLAM
TM4 143 163 IGRTGLAIICCCVLAVLPSLF
TM5 200 221 YGFALALLIIIVDPLLIVISYT
TM6 243 267 CLSHILAVLVLYIPMVGVSMTHRFA
TM7 275 294 HVIMANIYLLAPPVMNPIIY

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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