Protein information for: OR10AA1P



MDHVSHNWTQSFILAGFTTTGTLQPLAFLGTLCIYLLTLAGNILIIVLVQ
LDSGLFTPMYLFISVLSFVEVWYVSTTVPMLLHTLLQGCSPVSSAVCFIQ
LFFHSLGMTECYLLGVMALDSYLIICHPLHYHALMSRQVQLRLAGASWVA
GFSAALVPATLTATLPFCLKEVAHYFCDLAPLMRLACVDTSWHARAHGTV
IGVATGCNFVLILGLYGGILNAVLKLPSAASSAKAFSTCSSHVTVVALFY
ASAFTVYVGSPGSRPESTDKLVALVYALITPFLNPIIYSLRNKEVKKALR
RVMAGRGGSRL
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 24 50 QPLAFLGTLCIYLLTLAGNILIIVLVQ
TM2 61 83 LFISVLSFVEVWYVSTTVPMLLH
TM3 98 117 FIQLFFHSLGMTECYLLGVM
TM4 140 160 QLRLAGASWVAGFSAALVPAT
TM5 196 217 AHGTVIGVATGCNFVLILGLYG
TM6 239 263 CSSHVTVVALFYASAFTVYVGSPGS
TM7 269 288 DKLVALVYALITPFLNPIIY

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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