Protein information for: OR2V2



METWVNQSYTDGFFLLGIFSHSTADLVLFSVVMAVFTVALCGNVLLIFLI
YMDPHLHTPMYFFLSQLSLMDLMLVCTNVPKMAANFLSGRKSISFVGCGI
QIGLFVCLVGSEGLLLGLMAYDRYVAISHPLHYPILMNQRVCLQITGSSW
AFGIIDGLIQMVVVMNFPYCGLRKVNHFFCEMLSLLKLACVDTSLFEKVI
FACCVFMLLFPFSIIVASYAHILGTVLQMHSAQAWKKALATCSSHLTAVT
LFYGAAMFIYLRPRHYRAPSHDKVASIFYTVLTPMLNPLIYSLRNREVMG
ALRKGLDRCRIGSQH
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 DLVLFSVVMAVFTVALCGNVLLIFLIY
TM2 62 84 FFLSQLSLMDLMLVCTNVPKMAA
TM3 99 119 GIQIGLFVCLVGSEGLLLGLM
TM4 142 162 CLQITGSSWAFGIIDGLIQMV
TM5 199 220 VIFACCVFMLLFPFSIIVASYA
TM6 242 266 CSSHLTAVTLFYGAAMFIYLRPRHY
TM7 272 291 DKVASIFYTVLTPMLNPLIY

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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