S47A2_MOUSE
ID S47A2_MOUSE Reviewed; 573 AA.
AC Q3V050; B2RXN1; Q5SS46;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Multidrug and toxin extrusion protein 2;
DE Short=MATE-2;
DE Short=mMATE-2;
DE AltName: Full=H(+)/organic cation antiporter kidney-specific;
DE AltName: Full=Solute carrier family 47 member 2;
GN Name=Slc47a2; Synonyms=Mate2;
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 [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Solute transporter for tetraethylammonium (TEA), cimetidine,
CC choline, procainamide, cimetidine, quinidine, guanidine, N-
CC methylnicotinamide (NMN). Responsible for the secretion of cationic
CC drugs across the brush border membranes. {ECO:0000269|PubMed:17715386}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.710 mM for TEA {ECO:0000269|PubMed:17715386};
CC Vmax=0.004 nmol/min/mg enzyme toward TEA
CC {ECO:0000269|PubMed:17715386};
CC pH dependence:
CC Optimum pH is 8.5. Active from pH 6 to 8.5.
CC {ECO:0000269|PubMed:17715386};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Localized to the plasma membrane and to the
CC intracellular organelles. {ECO:0000269|PubMed:17715386}.
CC -!- TISSUE SPECIFICITY: Expressed in testis; especially in testicular
CC Leydig cells. {ECO:0000269|PubMed:17715386}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK133432; BAE21655.1; -; mRNA.
DR EMBL; AL669884; CAI25733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC147619; AAI47620.1; -; mRNA.
DR EMBL; BC157913; AAI57914.1; -; mRNA.
DR CCDS; CCDS24810.1; -.
DR RefSeq; NP_001028714.1; NM_001033542.2.
DR AlphaFoldDB; Q3V050; -.
DR SMR; Q3V050; -.
DR STRING; 10090.ENSMUSP00000090710; -.
DR DrugCentral; Q3V050; -.
DR GuidetoPHARMACOLOGY; 1217; -.
DR TCDB; 2.A.66.1.16; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR jPOST; Q3V050; -.
DR PaxDb; Q3V050; -.
DR PRIDE; Q3V050; -.
DR ProteomicsDB; 260796; -.
DR Ensembl; ENSMUST00000093029; ENSMUSP00000090710; ENSMUSG00000069855.
DR GeneID; 380701; -.
DR KEGG; mmu:380701; -.
DR UCSC; uc007jhg.1; mouse.
DR CTD; 146802; -.
DR MGI; MGI:3588190; Slc47a2.
DR VEuPathDB; HostDB:ENSMUSG00000069855; -.
DR eggNOG; KOG1347; Eukaryota.
DR GeneTree; ENSGT00940000163327; -.
DR InParanoid; Q3V050; -.
DR OMA; EFWILLK; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q3V050; -.
DR TreeFam; TF324441; -.
DR BioGRID-ORCS; 380701; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Slc47a2; mouse.
DR PRO; PR:Q3V050; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3V050; protein.
DR Bgee; ENSMUSG00000069855; Expressed in spermatocyte and 20 other tissues.
DR ExpressionAtlas; Q3V050; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
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 Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..573
FT /note="Multidrug and toxin extrusion protein 2"
FT /id="PRO_0000312852"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 573 AA; 61789 MW; B18968B12E84F805 CRC64;
MEPAEDSLGA TIQPPELVRV PRGRSLRILL GLRGALSPDV RREAAALVAL AGPVFLAQLM
IFLISIVSSI FCGHLGKVEL DAVTLAVSVV NVTGISVGTG LASACDTLMS QSFGGKNLKR
VGVILQRGIL ILLLCCFPCW AIFLNTERLL LLLRQDPDVA RLAQVYVMIC IPALPAAFLF
QLQTRYLQSQ GIIMPQVIVG IAANVVNVGM NAFLLYALDL GVVGSAWANT TSQFFLSALL
FLYVWWKRIH IHTWGGWTRE CFQEWSSYTR LAIPSMFMVC IEWWTFEIGT FLAGLVNVTE
LGAQAVIYEL ASVAYMVPFG FGVAASVRVG NALGAGNADQ ARCSCTTVLL CAGVCALLVG
ILLAALKDVV AYIFTNDKDI ISLVSQVMPI FAPFHLFDAL AGTCGGVLRG TGKQKIGAVL
NTIGYYGFGF PIGVSLMFAA KLGIIGLWAG LIVCVSFQAF SYLIYILRTN WSRVAEQAQV
RAGLKSTKEL IPTPADLPIL EREVMDGVIL PDIIRPESQT GQLVVEENSQ CAVPTVGEVL
TGRQLVFYRG MALTVSVAVL IAGIVVRVFN DRG
