Protein information for: OR52T1P



MATLNLSSFNPGLFILLGIPGLEWFCIWMGILSFTSYLVSLVGNVILLYL
ITVEHNLHKPMFSFLSIPASANLILCITYFPKTFGIFXLKAQKIIFPGCF
TRFFFFGSFFCWTCAILLGLAFDHYMTIGFLLRYTSGLTPRHLCKIVVSI
DXRFNNILPIDFLGKHLPFCRTHINSNTYCEHIGVALLSYADISINIWYD
FTILVMTIISDLILTDISYTLTLHAVFHLPSSDALLKALSTGGSHVSVIL
MLYTPAMLSALTHHFGQSISCTFYIMFVGLYRAIPPVLNSIIMEXKQSRL
ELFFLKGMQXYEDENMDKW
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 CIWMGILSFTSYLVSLVGNVILLYLIT
TM2 63 85 SFLSIPASANLILCITYFPKTFG
TM3 100 120 FTRFFFFGSFFCWTCAILLGL
TM4 144 164 CKIVVSIDXRFNNILPIDFLG
TM5 199 220 YDFTILVMTIISDLILTDISYT
TM6 242 266 GGSHVSVILMLYTPAMLSALTHHFG
TM7 274 293 YIMFVGLYRAIPPVLNSIIM

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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