S47A1_HUMAN
ID S47A1_HUMAN Reviewed; 570 AA.
AC Q96FL8; Q53HF5; Q6PD77; Q86VL4; Q9NVA3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Multidrug and toxin extrusion protein 1;
DE Short=MATE-1;
DE Short=hMATE-1;
DE AltName: Full=Solute carrier family 47 member 1;
GN Name=SLC47A1; Synonyms=MATE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Colon, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLU-273, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16330770; DOI=10.1073/pnas.0506483102;
RA Otsuka M., Matsumoto T., Morimoto R., Arioka S., Omote H., Moriyama Y.;
RT "A human transporter protein that mediates the final excretion step for
RT toxic organic cations.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17923-17928(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16641166; DOI=10.1152/ajpcell.00090.2006;
RA Hiasa M., Matsumoto T., Komatsu T., Moriyama Y.;
RT "Wide variety of locations for rodent MATE1, a transporter protein that
RT mediates the final excretion step for toxic organic cations.";
RL Am. J. Physiol. 291:C678-C686(2006).
RN [7]
RP FUNCTION.
RX PubMed=16996621; DOI=10.1016/j.tips.2006.09.001;
RA Omote H., Hiasa M., Matsumoto T., Otsuka M., Moriyama Y.;
RT "The MATE proteins as fundamental transporters of metabolic and xenobiotic
RT organic cations.";
RL Trends Pharmacol. Sci. 27:587-593(2006).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=17509534; DOI=10.1016/j.bcp.2007.04.010;
RA Tanihara Y., Masuda S., Sato T., Katsura T., Ogawa O., Inui K.;
RT "Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin
RT extrusions/H(+)-organic cation antiporters.";
RL Biochem. Pharmacol. 74:359-371(2007).
RN [9]
RP FUNCTION.
RX PubMed=17582384; DOI=10.1016/j.bcp.2007.03.004;
RA Yokoo S., Yonezawa A., Masuda S., Fukatsu A., Katsura T., Inui K.;
RT "Differential contribution of organic cation transporters, OCT2 and MATE1,
RT in platinum agent-induced nephrotoxicity.";
RL Biochem. Pharmacol. 74:477-487(2007).
RN [10]
RP FUNCTION.
RX PubMed=17495125; DOI=10.1124/jpet.107.123554;
RA Chen Y., Zhang S., Sorani M., Giacomini K.M.;
RT "Transport of paraquat by human organic cation transporters and multidrug
RT and toxic compound extrusion family.";
RL J. Pharmacol. Exp. Ther. 322:695-700(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Solute transporter for tetraethylammonium (TEA), 1-methyl-4-
CC phenylpyridinium (MPP), cimetidine, N-methylnicotinamide (NMN),
CC metformin, creatinine, guanidine, procainamide, topotecan, estrone
CC sulfate, acyclovir, ganciclovir and also the zwitterionic
CC cephalosporin, cephalexin and cephradin. Seems to also play a role in
CC the uptake of oxaliplatin (a new platinum anticancer agent). Able to
CC transport paraquat (PQ or N,N-dimethyl-4-4'-bipiridinium); a widely
CC used herbicid. Responsible for the secretion of cationic drugs across
CC the brush border membranes. {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:16996621, ECO:0000269|PubMed:17495125,
CC ECO:0000269|PubMed:17509534, ECO:0000269|PubMed:17582384}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for TEA {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=0.10 mM for MPP {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=0.17 mM for cimetidine {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=0.78 mM for metformin {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=2.1 mM for guanidine {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=1.23 mM for procainamide {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=0.07 mM for topotecan {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=0.47 mM for estrone sulfate {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=2.64 mM for acyclovir {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC KM=5.12 mM for ganciclovir {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:17509534};
CC Vmax=1.185 nmol/min/mg enzyme toward TEA
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.735 nmol/min/mg enzyme toward MPP
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.135 nmol/min/mg enzyme toward cimetidine
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=2.23 nmol/min/mg enzyme toward metformin
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.89 nmol/min/mg enzyme toward guanidine
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=3.78 nmol/min/mg enzyme toward procainamide
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.21 nmol/min/mg enzyme toward topotecan
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.265 nmol/min/mg enzyme toward estrone sulfate
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=0.62 nmol/min/mg enzyme toward acyclovir
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC Vmax=1.08 nmol/min/mg enzyme toward ganciclovir
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC pH dependence:
CC Optimum pH is 8.5. Active from pH 6 to 8.5.
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534};
CC -!- INTERACTION:
CC Q96FL8; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12887226, EBI-713304;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:16641166}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16641166}.
CC Note=Predominantly localized at the plasma membrane but also found in
CC intracellular organelles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96FL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FL8-2; Sequence=VSP_029903, VSP_029904;
CC Name=3;
CC IsoId=Q96FL8-3; Sequence=VSP_029905;
CC -!- TISSUE SPECIFICITY: Expressed in adrenal gland, and to a lower extent
CC in liver, skeletal muscle and kidney (especially found in luminal
CC membranes of the urinary tubules, bile caniculi and brush border
CC membranes). {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50592.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001709; BAA91852.1; -; mRNA.
DR EMBL; AK222625; BAD96345.1; -; mRNA.
DR EMBL; CH471212; EAW50893.1; -; Genomic_DNA.
DR EMBL; CH471212; EAW50894.1; -; Genomic_DNA.
DR EMBL; BC010661; AAH10661.1; -; mRNA.
DR EMBL; BC050592; AAH50592.1; ALT_INIT; mRNA.
DR EMBL; BC058882; AAH58882.1; -; mRNA.
DR CCDS; CCDS11209.1; -. [Q96FL8-1]
DR RefSeq; NP_060712.2; NM_018242.2. [Q96FL8-1]
DR AlphaFoldDB; Q96FL8; -.
DR SMR; Q96FL8; -.
DR BioGRID; 120535; 58.
DR IntAct; Q96FL8; 28.
DR STRING; 9606.ENSP00000270570; -.
DR BindingDB; Q96FL8; -.
DR ChEMBL; CHEMBL1743126; -.
DR DrugBank; DB12001; Abemaciclib.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB11901; Apalutamide.
DR DrugBank; DB16098; Atogepant.
DR DrugBank; DB15233; Avapritinib.
DR DrugBank; DB11799; Bictegravir.
DR DrugBank; DB12267; Brigatinib.
DR DrugBank; DB11791; Capmatinib.
DR DrugBank; DB01333; Cefradine.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB00501; Cimetidine.
DR DrugBank; DB00537; Ciprofloxacin.
DR DrugBank; DB08930; Dolutegravir.
DR DrugBank; DB00879; Emtricitabine.
DR DrugBank; DB04574; Estrone sulfate.
DR DrugBank; DB00927; Famotidine.
DR DrugBank; DB12500; Fedratinib.
DR DrugBank; DB12265; Fexinidazole.
DR DrugBank; DB01195; Flecainide.
DR DrugBank; DB16628; Fosdenopterin.
DR DrugBank; DB01004; Ganciclovir.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB11978; Glasdegib.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB01018; Guanfacine.
DR DrugBank; DB00536; Guanidine.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB11732; Lasmiditan.
DR DrugBank; DB01137; Levofloxacin.
DR DrugBank; DB04948; Lofexidine.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00331; Metformin.
DR DrugBank; DB09241; Methylene blue.
DR DrugBank; DB08840; N-methylnicotinamide.
DR DrugBank; DB01203; Nadolol.
DR DrugBank; DB11837; Osilodrostat.
DR DrugBank; DB15102; Pemigatinib.
DR DrugBank; DB12978; Pexidartinib.
DR DrugBank; DB12615; Plazomicin.
DR DrugBank; DB15822; Pralsetinib.
DR DrugBank; DB01035; Procainamide.
DR DrugBank; DB00205; Pyrimethamine.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB12377; Relebactam.
DR DrugBank; DB14761; Remdesivir.
DR DrugBank; DB11753; Rifamycin.
DR DrugBank; DB12457; Rimegepant.
DR DrugBank; DB14840; Ripretinib.
DR DrugBank; DB15305; Risdiplam.
DR DrugBank; DB12332; Rucaparib.
DR DrugBank; DB15685; Selpercatinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB06608; Tafenoquine.
DR DrugBank; DB12887; Tazemetostat.
DR DrugBank; DB13946; Testosterone undecanoate.
DR DrugBank; DB08837; Tetraethylammonium.
DR DrugBank; DB09343; Tipiracil.
DR DrugBank; DB06137; Tirbanibulin.
DR DrugBank; DB01030; Topotecan.
DR DrugBank; DB15442; Trilaciclib.
DR DrugBank; DB00440; Trimethoprim.
DR DrugBank; DB11652; Tucatinib.
DR DrugBank; DB00661; Verapamil.
DR DrugCentral; Q96FL8; -.
DR GuidetoPHARMACOLOGY; 1216; -.
DR TCDB; 2.A.66.1.14; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q96FL8; -.
DR PhosphoSitePlus; Q96FL8; -.
DR BioMuta; SLC47A1; -.
DR DMDM; 74731723; -.
DR jPOST; Q96FL8; -.
DR MassIVE; Q96FL8; -.
DR MaxQB; Q96FL8; -.
DR PaxDb; Q96FL8; -.
DR PeptideAtlas; Q96FL8; -.
DR PRIDE; Q96FL8; -.
DR ProteomicsDB; 76538; -. [Q96FL8-1]
DR ProteomicsDB; 76539; -. [Q96FL8-2]
DR ProteomicsDB; 76540; -. [Q96FL8-3]
DR Antibodypedia; 13691; 146 antibodies from 30 providers.
DR DNASU; 55244; -.
DR Ensembl; ENST00000270570.8; ENSP00000270570.4; ENSG00000142494.13. [Q96FL8-1]
DR Ensembl; ENST00000395585.5; ENSP00000378951.1; ENSG00000142494.13. [Q96FL8-3]
DR GeneID; 55244; -.
DR KEGG; hsa:55244; -.
DR MANE-Select; ENST00000270570.8; ENSP00000270570.4; NM_018242.3; NP_060712.2.
DR UCSC; uc002gvx.4; human. [Q96FL8-1]
DR CTD; 55244; -.
DR DisGeNET; 55244; -.
DR GeneCards; SLC47A1; -.
DR HGNC; HGNC:25588; SLC47A1.
DR HPA; ENSG00000142494; Tissue enhanced (adrenal gland, kidney, liver).
DR MIM; 609832; gene.
DR neXtProt; NX_Q96FL8; -.
DR OpenTargets; ENSG00000142494; -.
DR PharmGKB; PA162403808; -.
DR VEuPathDB; HostDB:ENSG00000142494; -.
DR eggNOG; KOG1347; Eukaryota.
DR GeneTree; ENSGT00940000161644; -.
DR InParanoid; Q96FL8; -.
DR OMA; TGNQKVG; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q96FL8; -.
DR TreeFam; TF324441; -.
DR PathwayCommons; Q96FL8; -.
DR Reactome; R-HSA-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR SignaLink; Q96FL8; -.
DR BioGRID-ORCS; 55244; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; SLC47A1; human.
DR GeneWiki; SLC47A1; -.
DR GenomeRNAi; 55244; -.
DR Pharos; Q96FL8; Tchem.
DR PRO; PR:Q96FL8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96FL8; protein.
DR Bgee; ENSG00000142494; Expressed in right adrenal gland cortex and 150 other tissues.
DR ExpressionAtlas; Q96FL8; baseline and differential.
DR Genevisible; Q96FL8; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0042887; F:amide transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015299; F:solute:proton antiporter activity; TAS:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR GO; GO:0042908; P:xenobiotic transport; IMP:ARUK-UCL.
DR CDD; cd13132; MATE_eukaryotic; 1.
DR InterPro; IPR045069; MATE_euk.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..570
FT /note="Multidrug and toxin extrusion protein 1"
FT /id="PRO_0000312845"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 508..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 286..290
FT /note="ILGMV -> LYEDG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029903"
FT VAR_SEQ 291..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029904"
FT VAR_SEQ 559..570
FT /note="VGILVRFYVRIQ -> AGVRWCDHSSLQPRTLGLQAILLCQPPE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029905"
FT VARIANT 338
FT /note="V -> I (in dbSNP:rs35790011)"
FT /id="VAR_037587"
FT MUTAGEN 273
FT /note="E->Q: No change in subcellular location and
FT abolition of MATE1-dependent TEA transport activity."
FT /evidence="ECO:0000269|PubMed:16330770"
FT CONFLICT 50
FT /note="L -> R (in Ref. 2; BAD96345)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="P -> L (in Ref. 1; BAA91852)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="F -> L (in Ref. 2; BAD96345)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="N -> D (in Ref. 2; BAD96345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 61922 MW; CA940CBC2F6F5CC4 CRC64;
MEAPEEPAPV RGGPEATLEV RGSRCLRLSA FREELRALLV LAGPAFLVQL MVFLISFISS
VFCGHLGKLE LDAVTLAIAV INVTGVSVGF GLSSACDTLI SQTYGSQNLK HVGVILQRSA
LVLLLCCFPC WALFLNTQHI LLLFRQDPDV SRLTQTYVTI FIPALPATFL YMLQVKYLLN
QGIVLPQIVT GVAANLVNAL ANYLFLHQLH LGVIGSALAN LISQYTLALL LFLYILGKKL
HQATWGGWSL ECLQDWASFL RLAIPSMLML CMEWWAYEVG SFLSGILGMV ELGAQSIVYE
LAIIVYMVPA GFSVAASVRV GNALGAGDME QARKSSTVSL LITVLFAVAF SVLLLSCKDH
VGYIFTTDRD IINLVAQVVP IYAVSHLFEA LACTSGGVLR GSGNQKVGAI VNTIGYYVVG
LPIGIALMFA TTLGVMGLWS GIIICTVFQA VCFLGFIIQL NWKKACQQAQ VHANLKVNNV
PRSGNSALPQ DPLHPGCPEN LEGILTNDVG KTGEPQSDQQ MRQEEPLPEH PQDGAKLSRK
QLVLRRGLLL LGVFLILLVG ILVRFYVRIQ
