Protein information for: OR51A4



MSIINTSYVEITTFFLVGMPGLEYAHIWISIPICSMYLIAILGNGTILFI
IKTEPSLHEPMYYFLSMLAMSDLGLSLSSLPTVLSIFLFNAPEISSNACF
AQEFFIHGFSVLESSVLLIMSFDRFLAIHNPLRYTSILTTVRVAQIGIVF
SFKSMLLVLPFPFTLRNLRYCKKNQLSHSYCLHQDVMKLACSDNRIDVIY
GFFGALCLMVDFILIAVSYTLILKTVPGIASKKEQLKALNTCVSHICAVI
IFYLPIINLAVVHRFARHVSPLINVLMANVLLLVPPLTNPIVYCVKTKQI
RVRVVAKLCQRKI
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 HIWISIPICSMYLIAILGNGTILFIIK
TM2 63 85 YFLSMLAMSDLGLSLSSLPTVLS
TM3 100 120 FAQEFFIHGFSVLESSVLLIM
TM4 143 163 VAQIGIVFSFKSMLLVLPFPF
TM5 200 220 YGFFGALCLMVDFILIAVSYT
TM6 242 266 CVSHICAVIIFYLPIINLAVVHRFA
TM7 274 293 NVLMANVLLLVPPLTNPIVY

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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