S47A1_MOUSE
ID S47A1_MOUSE Reviewed; 567 AA.
AC Q8K0H1; Q5SS45; Q9CQ64;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Multidrug and toxin extrusion protein 1;
DE Short=MATE-1;
DE Short=mMATE-1;
DE AltName: Full=Solute carrier family 47 member 1;
GN Name=Slc47a1; Synonyms=Mate1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [5]
RP SUBCELLULAR LOCATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17715386; DOI=10.1152/ajpcell.00280.2007;
RA Hiasa M., Matsumoto T., Komatsu T., Omote H., Moriyama Y.;
RT "Functional characterization of testis-specific rodent multidrug and toxic
RT compound extrusion 2, a class III MATE-type polyspecific H+/organic cation
RT exporter.";
RL Am. J. Physiol. 293:C1437-C1444(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for TEA {ECO:0000269|PubMed:16641166};
CC Vmax=0.6 nmol/min/mg enzyme toward TEA {ECO:0000269|PubMed:16641166};
CC pH dependence:
CC Optimum pH is 8.0-8.5. Active from pH 6 to 8.5.
CC {ECO:0000269|PubMed:16641166};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16330770,
CC ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}.
CC Note=Predominantly localized to the plasma membrane; at the brush
CC border membranes of the proximal tubules (kidney) and at the bile
CC caniculi (liver).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K0H1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K0H1-2; Sequence=VSP_029906, VSP_029907;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and liver. Also
CC expressed in various cells, including brain glia-like cells and
CC capillaries, pancreatic duct cells, urinary bladder epithelium, adrenal
CC gland cortex, heart, stomach, small intestine, thyroid gland, testes,
CC alpha cells of the islets of Langerhans, Leydig cells, and vitamin A-
CC storing Ito cells. Expressed in heart, stomach, small intestine,
CC bladder, thyroid gland, adrenal gland and testes (at protein level).
CC {ECO:0000269|PubMed:16330770}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC031436; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004994; BAB23729.1; -; mRNA.
DR EMBL; AK009038; BAB26040.1; -; mRNA.
DR EMBL; AL669884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031436; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS24811.2; -. [Q8K0H1-1]
DR RefSeq; NP_080459.2; NM_026183.5. [Q8K0H1-1]
DR RefSeq; XP_011247491.1; XM_011249189.2. [Q8K0H1-2]
DR AlphaFoldDB; Q8K0H1; -.
DR SMR; Q8K0H1; -.
DR STRING; 10090.ENSMUSP00000010267; -.
DR BindingDB; Q8K0H1; -.
DR ChEMBL; CHEMBL3091264; -.
DR DrugCentral; Q8K0H1; -.
DR TCDB; 2.A.66.1.18; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q8K0H1; -.
DR PhosphoSitePlus; Q8K0H1; -.
DR jPOST; Q8K0H1; -.
DR MaxQB; Q8K0H1; -.
DR PaxDb; Q8K0H1; -.
DR PeptideAtlas; Q8K0H1; -.
DR PRIDE; Q8K0H1; -.
DR ProteomicsDB; 260794; -. [Q8K0H1-1]
DR ProteomicsDB; 260795; -. [Q8K0H1-2]
DR Antibodypedia; 13691; 146 antibodies from 30 providers.
DR Ensembl; ENSMUST00000010267; ENSMUSP00000010267; ENSMUSG00000010122. [Q8K0H1-1]
DR GeneID; 67473; -.
DR KEGG; mmu:67473; -.
DR UCSC; uc007jhh.2; mouse. [Q8K0H1-2]
DR UCSC; uc007jhi.2; mouse. [Q8K0H1-1]
DR CTD; 55244; -.
DR MGI; MGI:1914723; Slc47a1.
DR VEuPathDB; HostDB:ENSMUSG00000010122; -.
DR eggNOG; KOG1347; Eukaryota.
DR GeneTree; ENSGT00940000161644; -.
DR HOGENOM; CLU_012893_1_3_1; -.
DR InParanoid; Q8K0H1; -.
DR OMA; TGNQKVG; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q8K0H1; -.
DR TreeFam; TF324441; -.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR BioGRID-ORCS; 67473; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8K0H1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K0H1; protein.
DR Bgee; ENSMUSG00000010122; Expressed in renal cortex tubule and 136 other tissues.
DR ExpressionAtlas; Q8K0H1; baseline and differential.
DR Genevisible; Q8K0H1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0042887; F:amide transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:MGI.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; ISO:MGI.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; ISO:MGI.
DR GO; GO:0015695; P:organic cation transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR GO; GO:0042908; P:xenobiotic transport; ISO:MGI.
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; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..567
FT /note="Multidrug and toxin extrusion protein 1"
FT /id="PRO_0000312846"
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..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..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..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96FL8"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029906"
FT VAR_SEQ 143..181
FT /note="LFRQDPDVSRLTQTYVMIFIPALPAAFLYTLQVKYLLNQ -> MSDTSPQAG
FT VLSRARLLQLRRHSSQRPERSGLAGLLERV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029907"
SQ SEQUENCE 567 AA; 61642 MW; EDAF1D3DB3BBD8F5 CRC64;
MERTEESAPG PGGADAASER RGLRCLLLPG FLEELRALLV LAGPAFLAQL MMFLISFISS
VFCGHLGKLE LDAVTLAIAV INVTGISVGH GLSSACDTLI SQTYGSQNLK HVGVILQRGT
LILLLCCFPC WALFINTEQI LLLFRQDPDV SRLTQTYVMI FIPALPAAFL YTLQVKYLLN
QGIVLPQIMT GIAANLVNAL ANYVFLYHLH LGVMGSALAN TISQFALAIF LFLYILWRRL
HQATWGGWSW ECLQDWASFL RLAIPSMLML CIEWWAYEVG SFLSGILGMV ELGAQSITYE
LAIIVYMIPS GFSVAANVRV GNALGAGNID QAKKSSAISL IVTELFAVTF CVLLLGCKDL
VGYIFTTDRD IVALVAQVIP IYAVSHLFEG LACTCGGILR GTGNQKVGAI VNAIGYYVIG
LPIGIALMFA AKLGVIGLWS GIIICTTCQT TCFLAFIARL NWKRACQQAQ VHANLKVNVA
LNSAVSHEPA HPVCPESHGE IMMTDLEKKD ETQLDQPMNQ QQALPIRPKD SNKLSGKQLA
LRRGLLLLGV VLVLVGGILV RVYIRIE
