Protein information for: OR10H2



MLGLNHTSMSEFILVGFSAFPHLQLMLFLLFLLMYLFTLLGNLLIMATVW
SERSLHTPMYLFLCVLSVSEILYTVAIIPRMLADLLSTQRSIAFLACASQ
MFFSFSFGFTHSFLLTVMGYDRYVAICHPLRYNVLMSPRGCACLVGCSWA
GGSVMGMVVTSAIFQLTFCGSHEIQHFLCHVPPLLKLACGNNPAVALGVG
LVCIMALLGCFLLILLSYAFIVADILKIPSAEGRNKAFSTCASHLIVVIV
HYGFASVIYLKPKGPHSQEGDTLMATTYAVLTPFLSPIIFSLRNKELKVA
MKRTFLSTLYSSGT
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 24 50 QLMLFLLFLLMYLFTLLGNLLIMATVW
TM2 61 83 LFLCVLSVSEILYTVAIIPRMLA
TM3 98 118 ASQMFFSFSFGFTHSFLLTVM
TM4 141 161 CACLVGCSWAGGSVMGMVVTS
TM5 198 219 GVGLVCIMALLGCFLLILLSYA
TM6 241 265 CASHLIVVIVHYGFASVIYLKPKGP
TM7 271 290 DTLMATTYAVLTPFLSPIIF

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.
HORDE homepage