Protein information for: OR11A1



MEIVSTGNETITEFVLLGFYDIPELHFLFFIVFTAVYVFIIIGNMLIIVA
VVSSQRLHKPMYIFLANLSFLDILYTSAVMPKMLEGFLQEATISVAGCLL
QFFIFGSLATAECLLLAVMAYDRYLAICYPLHYPLLMGPRRYMGLVVTTW
LSGFVVDGLVVALVAQLRFCGPNHIDQFYCDFMLFVGLACSDPRVAQVTT
LILSVFCLTIPFGLILTSYARIVVAVLRVPAGASRRRAFSTCSSHLAVVT
TFYGTLMIFYVAPSAVHSQLLSKVFSLLYTVVTPLFNPVIYTMRNKEVHQ
ALRKILCIKQTETLD
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 HFLFFIVFTAVYVFIIIGNMLIIVAVV
TM2 63 85 IFLANLSFLDILYTSAVMPKMLE
TM3 99 119 LLQFFIFGSLATAECLLLAVM
TM4 142 162 YMGLVVTTWLSGFVVDGLVVA
TM5 199 220 TTLILSVFCLTIPFGLILTSYA
TM6 242 266 CSSHLAVVTTFYGTLMIFYVAPSAV
TM7 272 290 KVFSLLYTVVTPLFNPVIY

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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