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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).

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

Cross database links:

Structure:
5Y50     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
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