Protein information for: OR51G1



MTILLNSSLQRATFFLTGFQGLEGLHGWISIPFCFIYLTVILGNLTILHV
ICTDATLHGPMYYFLGMLAVTDLGLCLSTLPTVLGIFWFDTREIGIPACF
TQLFFIHTLSSMESSVLLSMSIDRYVAVCNPLHDSTVLTPACIVKMGLSS
VLRSALLILPLPFLLKRFQYCHSHVLAHAYCLHLEIMKLACSSIIVNHIY
GLFVVACTVGVDSLLIFLSYALILRTVLSIASHQERLRALNTCVSHICAV
LLFYIPMIGLSLVHRFGEHLPRVVHLFMSYVYLLVPPLMNPIIYSIKTKQ
IRQRIIKKFQFIKSLRCFWKD
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 HGWISIPFCFIYLTVILGNLTILHVIC
TM2 63 85 YFLGMLAVTDLGLCLSTLPTVLG
TM3 100 120 FTQLFFIHTLSSMESSVLLSM
TM4 143 163 IVKMGLSSVLRSALLILPLPF
TM5 200 221 YGLFVVACTVGVDSLLIFLSYA
TM6 243 267 CVSHICAVLLFYIPMIGLSLVHRFG
TM7 275 294 HLFMSYVYLLVPPLMNPIIY

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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