Protein information for: OR2S1P



MNRSNEASPVLGFVLLGLSAHPXLEKTFFVFILLVYLVILLGNGVLILVT
ILDSRLHTPMYFFLGNLSFLDICYTTSSSLISFLTPRKTISFSACAVQMF
LSFAMGATECVLLSMMAFDHYLDMCNPLRYPVVMSKAAYMPMAVGSWAAG
ITNSVVQISLAMXLPFCGDNVINHFTCEILAVLKLACADICINVISMVVT
NMIFLALPVLFIFVSYVFIIATILRIPSAEGRKKAFSTCSAHLTVVIVFY
GMILFMYGKPKSKDPMGADKQDLADKLISIFYGVVTPILNPIIYSPRNKD
LKAAMRNLVAQKHLTE
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 25 51 EKTFFVFILLVYLVILLGNGVLILVTI
TM2 62 81 FFLGNLSFLDICYTTSSSLI
TM3 96 116 AVQMFLSFAMGATECVLLSMM
TM4 139 159 YMPMAVGSWAAGITNSVVQIS
TM5 196 217 SMVVTNMIFLALPVLFIFVSYV
TM6 239 263 CSAHLTVVIVFYGMILFMYGKPKSK
TM7 275 294 DKLISIFYGVVTPILNPIIY

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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