Protein information for: OR9H1P



MVNFTHVSEFVLLGFQGGPGMQAMLFLIFLILYGIAVVGNLGMIVIIWVD
AHLHTPMYAFLQSLSLLDICYSSTIAPRALANSMQEDHTISFGGCAAQFF
FLSLFGITEAFLLAAMAYDRFIAICNPLLYSVSMSHQVCVLLISGSYLWG
VVNAIAQTTMTFRLPFCGSNEINDFFCDVPPLLSLSCSDTFINQLVLLGL
CGSIIVSTFLIVLVSYIYIISTILRIPTMQGRXKAFSTCASHLTGVCLFF
GTVFFMYAQPSAIFFMEQSKIVSIFYTMVIPMLNPLIYSLRNKEVKQALR
RSMQKLSL
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 22 48 QAMLFLIFLILYGIAVVGNLGMIVIIW
TM2 59 81 AFLQSLSLLDICYSSTIAPRALA
TM3 96 116 AAQFFFLSLFGITEAFLLAAM
TM4 139 159 CVLLISGSYLWGVVNAIAQTT
TM5 196 217 VLLGLCGSIIVSTFLIVLVSYI
TM6 239 263 CASHLTGVCLFFGTVFFMYAQPSAI
TM7 269 288 SKIVSIFYTMVIPMLNPLIY

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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