Protein information for: OR4K12P



MEGFNYSRVSEFMLLGLTDSPELQIFFFVVFSVFYLMTMLGNCLILLTVL
STSHLHSRTYFLLSNLSLDMCLSSFATPKMIMDFFALRKTISFEGCISQI
FFLHLFNGTEIVLLISMSFDRYIAICKPLRYSTIMSQRVCVELVAVSWTV
GFLHTMSQLVFPYYLPFCVPNVVDSFFCDLPLVIQLACIDIYVLGTSMIS
TSGVTALTSFLLLLTSYIIVLNTIRDYSSTGSSKALSTCTAHFIVVLMFF
GPCIFIYVWPSTNFLVDKILSVFYTIFTPFLNPLIYTLRNQEVKTAMKKK
LNIQYFSLGK
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 QIFFFVVFSVFYLMTMLGNCLILLTVL
TM2 61 82 FLLSNLSLDMCLSSFATPKMIM
TM3 97 117 ISQIFFLHLFNGTEIVLLISM
TM4 140 160 CVELVAVSWTVGFLHTMSQLV
TM5 197 218 SMISTSGVTALTSFLLLLTSYI
TM6 239 263 CTAHFIVVLMFFGPCIFIYVWPSTN
TM7 268 285 ILSVFYTIFTPFLNPLIY

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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