2.A.66.1.52 Detoxification protein 14, DTX14, of 485 aas and 12 TMSs. This MATE family (MOP superfamily) proter extrduces xenobiotics from the cell. It's 3-d structure is known to 2.6 Å resolution (Miyauchi et al. 2017). Its carboxy-terminal lobe (C-lobe) contains an extensive hydrogen-bonding network with well-conserved acidic residues, as demonstrated by structure-based mutational analyses. The analyses suggest that the transport mechanism involves a structural change of transmembrane helix 7, induced by the formation of a hydrogen-bonding network upon the protonation of the conserved acidic residue in the C-lobe (Miyauchi et al. 2017).
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Accession Number: | Q9C994 |
Protein Name: | Protein DETOXIFICATION 14 |
Length: | 485 |
Molecular Weight: | 52425.00 |
Species: | Arabidopsis thaliana (Mouse-ear cress) [3702] |
Number of TMSs: | 12 |
Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
Substrate |
xenobiotic |
---|
1: MDSAEKGLLV VSDREEVNKK DGFLRETKKL SYIAGPMIAV NSSMYVLQVI SIMMVGHLGE
61: LFLSSTAIAV SFCSVTGFSV VFGLASALET LCGQANGAKQ YEKLGVHTYT GIVSLFLVCI
121: PLSLLWTYIG DILSLIGQDA MVAQEAGKFA TWLIPALFGY ATLQPLVRFF QAQSLILPLV
181: MSSVSSLCIH IVLCWSLVFK FGLGSLGAAI AIGVSYWLNV TVLGLYMTFS SSCSKSRATI
241: SMSLFEGMGE FFRFGIPSAS MICLEWWSFE FLVLLSGILP NPKLEASVLS VCLSTQSSLY
301: QIPESLGAAA STRVANELGA GNPKQARMAV YTAMVITGVE SIMVGAIVFG ARNVFGYLFS
361: SETEVVDYVK SMAPLLSLSV IFDALHAALS GVARGSGRQD IGAYVNLAAY YLFGIPTAIL
421: LAFGFKMRGR GLWIGITVGS CVQAVLLGLI VILTNWKKQA RKARERVMGD EYEEKESEEE
481: HEYIS