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 24-JAN-2024, entry version 162. DE RecName: Full=Multidrug and toxin extrusion protein 1 {ECO:0000303|PubMed:16330770}; DE Short=MATE-1; DE Short=hMATE-1; DE AltName: Full=Solute carrier family 47 member 1; GN Name=SLC47A1 {ECO:0000312|HGNC:HGNC:25588}; GN Synonyms=MATE1 {ECO:0000303|PubMed:16330770}; 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, TRANSPORTER ACTIVITY, MUTAGENESIS OF GLU-273, TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MISCELLANEOUS. 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 MISCELLANEOUS. RX PubMed=16914559; DOI=10.1124/jpet.106.110346; RA Yonezawa A., Masuda S., Yokoo S., Katsura T., Inui K.; RT "Cisplatin and oxaliplatin, but not carboplatin and nedaplatin, are RT substrates for human organic cation transporters (SLC22A1-3 and multidrug RT and toxin extrusion family)."; RL J. Pharmacol. Exp. Ther. 319:879-886(2006). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE RP SPECIFICITY, SUBSTRATE SPECIFICITY, AND MISCELLANEOUS. 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, TRANSPORTER ACTIVITY, AND MISCELLANEOUS. 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, TRANSPORTER ACTIVITY, AND MISCELLANEOUS. 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 FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, MISCELLANEOUS, AND RP MUTAGENESIS OF GLU-273; GLU-278; GLU-300 AND GLU-389. RX PubMed=18305230; DOI=10.1152/ajpcell.00504.2007; RA Matsumoto T., Kanamoto T., Otsuka M., Omote H., Moriyama Y.; RT "Role of glutamate residues in substrate recognition by human MATE1 RT polyspecific H+/organic cation exporter."; RL Am. J. Physiol. 294:C1074-C1078(2008). RN [12] RP VARIANTS LEU-10; ASP-64; VAL-310; ALA-328 AND SER-474, CHARACTERIZATION OF RP VARIANTS LEU-10; ASP-64; VAL-310; ALA-328 AND SER-474, FUNCTION, RP TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND MISCELLANEOUS. RX PubMed=19158817; DOI=10.1038/jhg.2008.1; RA Kajiwara M., Terada T., Ogasawara K., Iwano J., Katsura T., Fukatsu A., RA Doi T., Inui K.; RT "Identification of multidrug and toxin extrusion (MATE1 and MATE2-K) RT variants with complete loss of transport activity."; RL J. Hum. Genet. 54:40-46(2009). RN [13] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MISCELLANEOUS. RX PubMed=21128598; DOI=10.1021/mp100180a; RA Winter T.N., Elmquist W.F., Fairbanks C.A.; RT "OCT2 and MATE1 provide bidirectional agmatine transport."; RL Mol. Pharm. 8:133-142(2011). RN [14] 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). RN [15] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=24961373; DOI=10.1073/pnas.1314939111; RA Chen L., Shu Y., Liang X., Chen E.C., Yee S.W., Zur A.A., Li S., Xu L., RA Keshari K.R., Lin M.J., Chien H.C., Zhang Y., Morrissey K.M., Liu J., RA Ostrem J., Younger N.S., Kurhanewicz J., Shokat K.M., Ashrafi K., RA Giacomini K.M.; RT "OCT1 is a high-capacity thiamine transporter that regulates hepatic RT steatosis and is a target of metformin."; RL Proc. Natl. Acad. Sci. U.S.A. 111:9983-9988(2014). RN [16] RP MUTAGENESIS OF TYR-299, AND MISCELLANEOUS. RX PubMed=26979622; DOI=10.1038/ncomms10880; RA Sprowl J.A., Ong S.S., Gibson A.A., Hu S., Du G., Lin W., Li L., RA Bharill S., Ness R.A., Stecula A., Offer S.M., Diasio R.B., Nies A.T., RA Schwab M., Cavaletti G., Schlatter E., Ciarimboli G., Schellens J.H.M., RA Isacoff E.Y., Sali A., Chen T., Baker S.D., Sparreboom A., Pabla N.; RT "A phosphotyrosine switch regulates organic cation transporters."; RL Nat. Commun. 7:10880-10880(2016). RN [17] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=35307651; DOI=10.1124/dmd.121.000748; RA Hau R.K., Klein R.R., Wright S.H., Cherrington N.J.; RT "Localization of Xenobiotic Transporters Expressed at the Human Blood- RT Testis Barrier."; RL Drug Metab. Dispos. 50:770-780(2022). CC -!- FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation CC antiporter (PubMed:16330770, PubMed:17509534). Plays a physiological CC role in the excretion of cationic compounds including endogenous CC metabolites, drugs, toxins through the kidney and liver, into urine and CC bile respectively (PubMed:16330770, PubMed:17495125, PubMed:17509534, CC PubMed:17582384, PubMed:18305230, PubMed:19158817, PubMed:21128598, CC PubMed:24961373). Mediates the efflux of endogenous compounds such as CC creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate CC (PubMed:16330770, PubMed:17495125, PubMed:17509534, PubMed:17582384, CC PubMed:18305230, PubMed:19158817, PubMed:21128598, PubMed:24961373). CC May also contribute to regulate the transport of cationic compounds in CC testis across the blood-testis-barrier (Probable). CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17495125, CC ECO:0000269|PubMed:17509534, ECO:0000269|PubMed:17582384, CC ECO:0000269|PubMed:18305230, ECO:0000269|PubMed:19158817, CC ECO:0000269|PubMed:21128598, ECO:0000269|PubMed:24961373, CC ECO:0000305|PubMed:35307651}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in); CC Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385; CC Evidence={ECO:0000269|PubMed:17509534, ECO:0000305|PubMed:24961373}; CC -!- CATALYTIC ACTIVITY: CC Reaction=estrone 3-sulfate(in) + H(+)(out) = estrone 3-sulfate(out) + CC H(+)(in); Xref=Rhea:RHEA:72139, ChEBI:CHEBI:15378, ChEBI:CHEBI:60050; CC Evidence={ECO:0000269|PubMed:17509534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=creatinine(in) + H(+)(out) = creatinine(out) + H(+)(in); CC Xref=Rhea:RHEA:72183, ChEBI:CHEBI:15378, ChEBI:CHEBI:16737; CC Evidence={ECO:0000269|PubMed:17509534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=agmatine(in) + H(+)(out) = agmatine(out) + H(+)(in); CC Xref=Rhea:RHEA:72127, ChEBI:CHEBI:15378, ChEBI:CHEBI:58145; CC Evidence={ECO:0000269|PubMed:21128598}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72128; CC Evidence={ECO:0000305|PubMed:21128598}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72129; CC Evidence={ECO:0000305|PubMed:21128598}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.38 mM for TEA {ECO:0000269|PubMed:16330770, CC ECO:0000269|PubMed:17509534}; CC KM=0.58 mM for TEA {ECO:0000269|PubMed:18305230}; CC KM=0.1 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=7.4 uM for cimetidine {ECO:0000269|PubMed:18305230}; 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=240 uM for agmatine (at pH 8.0) {ECO:0000269|PubMed:21128598}; CC KM=830 uM for thiamine {ECO:0000269|PubMed:24961373}; CC KM=5.12 mM for ganciclovir {ECO:0000269|PubMed:16330770, CC ECO:0000269|PubMed:17509534}; CC Vmax=0.192 nmol/min/mg enzyme toward agmatine (at pH 8.0) CC {ECO:0000269|PubMed:21128598}; CC Vmax=2.94 nmol/min/mg enzyme toward thiamine CC {ECO:0000269|PubMed:24961373}; CC Vmax=1.185 nmol/min/mg enzyme toward TEA CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534}; CC Vmax=0.81 nmol/min/mg enzyme toward TEA CC {ECO:0000269|PubMed:18305230}; 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=0.104 nmol/min/mg enzyme toward cimetidine CC {ECO:0000269|PubMed:18305230}; 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 8.0 for agmatine uptake (PubMed:21128598). Optimum pH CC is 8.5. Active from pH 6 to 8.5. {ECO:0000269|PubMed:16330770, CC ECO:0000269|PubMed:17509534, ECO:0000269|PubMed:21128598}; CC -!- INTERACTION: CC Q96FL8; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12887226, EBI-713304; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16641166, CC ECO:0000269|PubMed:18305230, ECO:0000269|PubMed:19158817}; Multi-pass CC membrane protein {ECO:0000255}. Apical cell membrane CC {ECO:0000269|PubMed:16330770}; Multi-pass membrane protein CC {ECO:0000255}. Note=Localizes to the plasma membrane; at the brush CC border membranes of the proximal tubules (kidney) and at the bile CC caniculi (liver). {ECO:0000269|PubMed:16330770}. 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: Widely expressed. The highest expression is found CC in adrenal gland, and to a lower extent in liver, skeletal muscle and CC kidney. In testis, primarily localized throughout the adluminal CC compartment of the seminiferous tubules with expression at the CC peritubular myoid cells and Leydig cells (PubMed:35307651). CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17509534, CC ECO:0000269|PubMed:35307651}. CC -!- MISCELLANEOUS: Mediates the efflux of cationic compounds such as the CC model cations, tetraethylammonium (TEA), the neurotoxin 1-methyl-4- CC phenylpyridinium (MPP), the platinum-based drugs cisplatin and CC oxaliplatin, the drugs procainamide, acyclovir and topotecan, or weak CC bases that are positively charged at physiological pH, such as CC cimetidine or the antidiabetic drug metformin. CC {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16914559, CC ECO:0000269|PubMed:17495125, ECO:0000269|PubMed:17509534, CC ECO:0000269|PubMed:17582384, ECO:0000269|PubMed:18305230, CC ECO:0000269|PubMed:19158817, ECO:0000269|PubMed:21128598, CC ECO:0000269|PubMed:26979622}. CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) CC (TC 2.A.66.1) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50592.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; DB05667; Levoketoconazole. 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; DB11793; Niraparib. DR DrugBank; DB16267; Olutasidenib. 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; DB15133; Tepotinib. 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 DrugBank; DB09185; Viloxazine. 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; 9606-ENSP00000270570; -. DR PeptideAtlas; Q96FL8; -. DR ProteomicsDB; 76538; -. [Q96FL8-1] DR ProteomicsDB; 76539; -. [Q96FL8-2] DR ProteomicsDB; 76540; -. [Q96FL8-3] DR Pumba; Q96FL8; -. DR Antibodypedia; 13691; 169 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 AGR; HGNC:25588; -. 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; WFFVWKL; -. DR OrthoDB; 10858at2759; -. 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; 13 hits in 1150 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 152 other cell types or tissues. DR ExpressionAtlas; Q96FL8; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0015297; F:antiporter activity; IDA:UniProtKB. 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:0015101; F:organic cation transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0140968; F:polyspecific organic cation:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0022857; F:transmembrane transporter activity; TAS:Reactome. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0015847; P:putrescine transport; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:UniProtKB. DR GO; GO:0006855; P:xenobiotic transmembrane transport; IEA:Ensembl. 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 NCBIfam; TIGR00797; matE; 1. DR PANTHER; PTHR11206:SF73; MULTIDRUG AND TOXIN EXTRUSION PROTEIN 1; 1. DR PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1. DR Pfam; PF01554; MatE; 2. DR Genevisible; Q96FL8; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Antiport; 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 10 FT /note="V -> L (does not affect plasma membrane expression; FT does not affect TEA and metformin transport; FT dbSNP:rs555657341)" FT /evidence="ECO:0000269|PubMed:19158817" FT /id="VAR_087027" FT VARIANT 64 FT /note="G -> D (found in a patient with renal disease; FT uncertain significance; decreases plasma membrane FT expression; transport of TEA and metformin are reduced by FT at least 90%; dbSNP:rs77630697)" FT /evidence="ECO:0000269|PubMed:19158817" FT /id="VAR_087028" FT VARIANT 310 FT /note="A -> V (found in a patient with renal disease; FT uncertain significance; does not affect plasma membrane FT expression; decreases TEA and metformin transport; Vmax FT value for TEA transport is decreased; Km value for TEA is FT increased; dbSNP:rs1322335818)" FT /evidence="ECO:0000269|PubMed:19158817" FT /id="VAR_087029" FT VARIANT 328 FT /note="D -> A (found in a patient with renal disease; FT uncertain significance; decreases plasma membrane FT expression; decreases TEA and metformin transport; Vmax FT value for TEA transport is decreased; dbSNP:rs149774861)" FT /evidence="ECO:0000269|PubMed:19158817" FT /id="VAR_087030" FT VARIANT 338 FT /note="V -> I (in dbSNP:rs35790011)" FT /id="VAR_037587" FT VARIANT 474 FT /note="N -> S (found in a patient with renal disease; FT uncertain significance; does not affect plasma membrane FT localization; decreases TEA transport; Km value for TEA is FT increased; does not affect metformin transport; FT dbSNP:rs1480708114)" FT /evidence="ECO:0000269|PubMed:19158817" FT /id="VAR_087031" FT MUTAGEN 273 FT /note="E->A: Abolishes membrane subcellular location. FT Abolishes TEA transport." FT /evidence="ECO:0000269|PubMed:18305230" FT MUTAGEN 273 FT /note="E->D: Does not affect membrane subcellular location. FT Decreases TEA transport. Higher affinity for cimetidine and FT reduced affinity to TEA." FT /evidence="ECO:0000269|PubMed:18305230" 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 MUTAGEN 278 FT /note="E->A: Does not affect membrane subcellular location. FT Abolishes TEA transport." FT /evidence="ECO:0000269|PubMed:18305230" FT MUTAGEN 278 FT /note="E->D: Does not affect membrane subcellular location. FT Decreases TEA transport." FT /evidence="ECO:0000269|PubMed:18305230" FT MUTAGEN 299 FT /note="Y->F: Decreased TEA and metformin uptake." FT /evidence="ECO:0000269|PubMed:26979622" FT MUTAGEN 300 FT /note="E->A,D: Does not affect membrane subcellular FT location. Decreases TEA transport." FT /evidence="ECO:0000269|PubMed:18305230" FT MUTAGEN 389 FT /note="E->A,D: Does not affect membrane subcellular FT location. Decreases TEA transport." FT /evidence="ECO:0000269|PubMed:18305230" 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 //