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Multidrug and toxin extrusion protein 1 (MATE-1) (mMATE-1) (Solute carrier family 47 member 1)

 S47A1_MOUSE             Reviewed;         567 AA.
Q8K0H1; Q5SS45; Q9CQ64;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
22-NOV-2017, entry version 106.
RecName: Full=Multidrug and toxin extrusion protein 1;
Short=MATE-1;
Short=mMATE-1;
AltName: Full=Solute carrier family 47 member 1;
Name=Slc47a1; Synonyms=Mate1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16330770; DOI=10.1073/pnas.0506483102;
Otsuka M., Matsumoto T., Morimoto R., Arioka S., Omote H.,
Moriyama Y.;
"A human transporter protein that mediates the final excretion step
for toxic organic cations.";
Proc. Natl. Acad. Sci. U.S.A. 102:17923-17928(2005).
[5]
SUBCELLULAR LOCATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16641166; DOI=10.1152/ajpcell.00090.2006;
Hiasa M., Matsumoto T., Komatsu T., Moriyama Y.;
"Wide variety of locations for rodent MATE1, a transporter protein
that mediates the final excretion step for toxic organic cations.";
Am. J. Physiol. 291:C678-C686(2006).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17715386; DOI=10.1152/ajpcell.00280.2007;
Hiasa M., Matsumoto T., Komatsu T., Omote H., Moriyama Y.;
"Functional characterization of testis-specific rodent multidrug and
toxic compound extrusion 2, a class III MATE-type polyspecific
H+/organic cation exporter.";
Am. J. Physiol. 293:C1437-C1444(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Solute transporter for tetraethylammonium (TEA), 1-
methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide
(NMN), metformin, creatinine, guanidine, procainamide, topotecan,
estrone sulfate, acyclovir, ganciclovir and also the zwitterionic
cephalosporin, cephalexin and cephradin. Seems to also play a role
in the uptake of oxaliplatin (a new platinum anticancer agent).
Able to transport paraquat (PQ or N,N-dimethyl-4-4'-bipiridinium);
a widely used herbicid. Responsible for the secretion of cationic
drugs across the brush border membranes (By similarity).
{ECO:0000250, ECO:0000269|PubMed:16641166,
ECO:0000269|PubMed:17715386}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.41 mM for TEA {ECO:0000269|PubMed:16641166};
Vmax=0.6 nmol/min/mg enzyme toward TEA
{ECO:0000269|PubMed:16641166};
pH dependence:
Optimum pH is 8.0-8.5. Active from pH 6 to 8.5.
{ECO:0000269|PubMed:16641166};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330770,
ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}; Multi-
pass membrane protein {ECO:0000269|PubMed:16330770,
ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}.
Note=Predominantly localized to the plasma membrane; at the brush
border membranes of the proximal tubules (kidney) and at the bile
caniculi (liver).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8K0H1-1; Sequence=Displayed;
Name=2;
IsoId=Q8K0H1-2; Sequence=VSP_029906, VSP_029907;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in kidney and liver.
Also expressed in various cells, including brain glia-like cells
and capillaries, pancreatic duct cells, urinary bladder
epithelium, adrenal gland cortex, heart, stomach, small intestine,
thyroid gland, testes, alpha cells of the islets of Langerhans,
Leydig cells, and vitamin A-storing Ito cells. Expressed in heart,
stomach, small intestine, bladder, thyroid gland, adrenal gland
and testes (at protein level). {ECO:0000269|PubMed:16330770}.
-!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
(TC 2.A.66.1) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BC031436; Type=Frameshift; Positions=510; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK004994; BAB23729.1; -; mRNA.
EMBL; AK009038; BAB26040.1; -; mRNA.
EMBL; AL669884; CAI25734.1; -; Genomic_DNA.
EMBL; BC031436; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS24811.2; -. [Q8K0H1-1]
RefSeq; NP_080459.2; NM_026183.5. [Q8K0H1-1]
RefSeq; XP_011247491.1; XM_011249189.2. [Q8K0H1-2]
UniGene; Mm.100741; -.
ProteinModelPortal; Q8K0H1; -.
SMR; Q8K0H1; -.
STRING; 10090.ENSMUSP00000010267; -.
BindingDB; Q8K0H1; -.
ChEMBL; CHEMBL3091264; -.
TCDB; 2.A.66.1.18; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
iPTMnet; Q8K0H1; -.
PhosphoSitePlus; Q8K0H1; -.
PaxDb; Q8K0H1; -.
PeptideAtlas; Q8K0H1; -.
PRIDE; Q8K0H1; -.
Ensembl; ENSMUST00000010267; ENSMUSP00000010267; ENSMUSG00000010122. [Q8K0H1-1]
GeneID; 67473; -.
KEGG; mmu:67473; -.
UCSC; uc007jhh.2; mouse. [Q8K0H1-2]
UCSC; uc007jhi.2; mouse. [Q8K0H1-1]
CTD; 55244; -.
MGI; MGI:1914723; Slc47a1.
eggNOG; KOG1347; Eukaryota.
eggNOG; COG0534; LUCA.
GeneTree; ENSGT00390000015713; -.
HOGENOM; HOG000060313; -.
HOVERGEN; HBG056043; -.
InParanoid; Q8K0H1; -.
KO; K03327; -.
OMA; LCMEWWA; -.
OrthoDB; EOG091G06X2; -.
PhylomeDB; Q8K0H1; -.
TreeFam; TF324441; -.
Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
PRO; PR:Q8K0H1; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000010122; -.
CleanEx; MM_SLC47A1; -.
ExpressionAtlas; Q8K0H1; baseline and differential.
Genevisible; Q8K0H1; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; IBA:GO_Central.
GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central.
GO; GO:0005451; F:monovalent cation:proton antiporter activity; IBA:GO_Central.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
InterPro; IPR002528; MATE_fam.
Pfam; PF01554; MatE; 2.
TIGRFAMs; TIGR00797; matE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Membrane; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 567 Multidrug and toxin extrusion protein 1.
/FTId=PRO_0000312846.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.
TRANSMEM 38 58 Helical. {ECO:0000255}.
TOPO_DOM 59 72 Extracellular. {ECO:0000255}.
TRANSMEM 73 93 Helical. {ECO:0000255}.
TOPO_DOM 94 120 Cytoplasmic. {ECO:0000255}.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TOPO_DOM 142 152 Extracellular. {ECO:0000255}.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TOPO_DOM 174 187 Cytoplasmic. {ECO:0000255}.
TRANSMEM 188 208 Helical. {ECO:0000255}.
TOPO_DOM 209 216 Extracellular. {ECO:0000255}.
TRANSMEM 217 237 Helical. {ECO:0000255}.
TOPO_DOM 238 257 Cytoplasmic. {ECO:0000255}.
TRANSMEM 258 277 Helical. {ECO:0000255}.
TOPO_DOM 278 295 Extracellular. {ECO:0000255}.
TRANSMEM 296 316 Helical. {ECO:0000255}.
TOPO_DOM 317 336 Cytoplasmic. {ECO:0000255}.
TRANSMEM 337 357 Helical. {ECO:0000255}.
TOPO_DOM 358 370 Extracellular. {ECO:0000255}.
TRANSMEM 371 391 Helical. {ECO:0000255}.
TOPO_DOM 392 408 Cytoplasmic. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 437 Extracellular. {ECO:0000255}.
TRANSMEM 438 458 Helical. {ECO:0000255}.
TOPO_DOM 459 543 Cytoplasmic. {ECO:0000255}.
TRANSMEM 544 564 Helical. {ECO:0000255}.
TOPO_DOM 565 567 Extracellular. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q96FL8}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_029906.
VAR_SEQ 143 181 LFRQDPDVSRLTQTYVMIFIPALPAAFLYTLQVKYLLNQ
-> MSDTSPQAGVLSRARLLQLRRHSSQRPERSGLAGLLER
V (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_029907.
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


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