Protein information for: OR52K2



MSASNITLTHPTAFLLVGIPGLEHLHIWISIPFCLAYTLALLGNCTLLLI
IQADAALHEPMYLFLAMLAAIDLVLSSSALPKMLAIFWFRDREINFFACL
AQMFFLHSFSIMESAVLLAMAFDRYVAICKPLHYTKVLTGSLITKIGMAA
VARAVTLMTPLPFLLRCFHYCRGPVIAHCYCEHMAVVRLACGDTSFNNIY
GIAVAMFIVVLDLLLVILSYIFILQAVLLLASQEARYKAFGTCVSHIGAI
LAFYTTVVISSVMHRVARHAAPHVHILLANFYLLFPPMVNPIIYGVKTKQ
IRESILGVFPRKDM
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 HIWISIPFCLAYTLALLGNCTLLLIIQ
TM2 63 85 LFLAMLAAIDLVLSSSALPKMLA
TM3 100 120 LAQMFFLHSFSIMESAVLLAM
TM4 143 163 ITKIGMAAVARAVTLMTPLPF
TM5 200 221 YGIAVAMFIVVLDLLLVILSYI
TM6 243 267 CVSHIGAILAFYTTVVISSVMHRVA
TM7 275 294 HILLANFYLLFPPMVNPIIY

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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