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

 S47A1_RAT               Reviewed;         566 AA.
Q5I0E9; Q0KKE7;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
27-SEP-2017, entry version 99.
RecName: Full=Multidrug and toxin extrusion protein 1;
Short=MATE-1;
Short=rMATE-1;
AltName: Full=Solute carrier family 47 member 1;
Name=Slc47a1; Synonyms=Mate1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Kidney;
PubMed=16928787; DOI=10.1124/dmd.106.010876;
Ohta K.Y., Inoue K., Hayashi Y., Yuasa H.;
"Molecular identification and functional characterization of rat
multidrug and toxin extrusion type transporter 1 as an organic
cation/H+ antiporter in the kidney.";
Drug Metab. Dispos. 34:1868-1874(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND FUNCTION.
TISSUE=Kidney;
PubMed=16850272; DOI=10.1007/s11095-006-9016-3;
Terada T., Masuda S., Asaka J., Tsuda M., Katsura T., Inui K.;
"Molecular cloning, functional characterization and tissue
distribution of rat H+/organic cation antiporter MATE1.";
Pharm. Res. 23:1696-1701(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17047166; DOI=10.1152/ajprenal.00312.2006;
Tsuda M., Terada T., Asaka J., Ueba M., Katsura T., Inui K.;
"Oppositely directed H+ gradient functions as a driving force of rat
H+/organic cation antiporter MATE1.";
Am. J. Physiol. 292:F593-F598(2007).
[5]
FUNCTION.
PubMed=17582384; DOI=10.1016/j.bcp.2007.03.004;
Yokoo S., Yonezawa A., Masuda S., Fukatsu A., Katsura T., Inui K.;
"Differential contribution of organic cation transporters, OCT2 and
MATE1, in platinum agent-induced nephrotoxicity.";
Biochem. Pharmacol. 74:477-487(2007).
[6]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17296166; DOI=10.1016/j.bcp.2006.12.034;
Nishihara K., Masuda S., Ji L., Katsura T., Inui K.;
"Pharmacokinetic significance of luminal multidrug and toxin extrusion
1 in chronic renal failure rats.";
Biochem. Pharmacol. 73:1482-1490(2007).
[7]
MUTAGENESIS OF CYS-62; HIS-64; CYS-95; HIS-110; CYS-125; CYS-126;
CYS-129; HIS-209; HIS-240; CYS-251; CYS-270; CYS-356; HIS-385;
CYS-392; CYS-444; CYS-451; CYS-465; HIS-471 AND HIS-490, SUBCELLULAR
LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17327464; DOI=10.1124/mol.106.032938;
Asaka J., Terada T., Tsuda M., Katsura T., Inui K.;
"Identification of essential histidine and cysteine residues of the
H+/organic cation antiporter multidrug and toxin extrusion (MATE).";
Mol. Pharmacol. 71:1487-1493(2007).
[8]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17473959; DOI=10.1007/s11095-007-9254-z;
Koepsell H., Lips K., Volk C.;
"Polyspecific organic cation transporters: structure, function,
physiological roles, and biopharmaceutical implications.";
Pharm. Res. 24:1227-1251(2007).
-!- FUNCTION: Solute transporter for tetraethylammonium (TEA),
cimetidine, metformin, guanidine, N-methylnicotinamide (NMN) and
also the zwitterionic cephalosporin cephalexin. Not a transporter
for 1-methyl-4-phenylpyridinium (MPP), procainamide, creatinine,
guanidine, p-aminohippurate (PAH) and the anionic cephalosporin
cefalozin. MPP-transport activity has been observed in
PubMed:16928787 and PubMed:17047166 and may contradict results
observed in PubMed:16850272. Seems to also play a role in the
uptake of oxaliplatin (a new platinum anticancer agent).
Responsible for the secretion of cationic drugs across the brush
border membranes. {ECO:0000269|PubMed:16850272,
ECO:0000269|PubMed:16928787, ECO:0000269|PubMed:17047166,
ECO:0000269|PubMed:17582384}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.260 mM for TEA {ECO:0000269|PubMed:16850272,
ECO:0000269|PubMed:16928787, ECO:0000269|PubMed:17047166,
ECO:0000269|PubMed:17327464, ECO:0000269|PubMed:17473959};
KM=0.003 mM for cimetidine {ECO:0000269|PubMed:16850272,
ECO:0000269|PubMed:16928787, ECO:0000269|PubMed:17047166,
ECO:0000269|PubMed:17327464, ECO:0000269|PubMed:17473959};
pH dependence:
Optimum pH is 7.5-8.4. Active from pH 6 to 8.5.
{ECO:0000269|PubMed:16850272, ECO:0000269|PubMed:16928787,
ECO:0000269|PubMed:17047166, ECO:0000269|PubMed:17327464,
ECO:0000269|PubMed:17473959};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17296166,
ECO:0000269|PubMed:17327464}; Multi-pass membrane protein
{ECO:0000269|PubMed:17296166, ECO:0000269|PubMed:17327464}.
Note=Predominantly localized at the plasma membrane but also found
in intracellular organelles.
-!- TISSUE SPECIFICITY: Highly expressed in kidney and placenta,
moderately in stomach, colon, lung, spleen, skeletal muscle and
prostate, and slightly in spleen. In the kidney, found in medulla
and cortex, especially in the proximal convoluted and straight
tubules. No expression was observed in heart, brain, small
intestine and liver. {ECO:0000269|PubMed:16850272,
ECO:0000269|PubMed:16928787, ECO:0000269|PubMed:17296166}.
-!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
(TC 2.A.66.1) family. {ECO:0000305}.
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EMBL; AB248823; BAF02626.1; -; mRNA.
EMBL; AB248824; BAF02627.1; -; mRNA.
EMBL; BC088413; AAH88413.1; -; mRNA.
RefSeq; NP_001014140.1; NM_001014118.2.
UniGene; Rn.17240; -.
STRING; 10116.ENSRNOP00000054704; -.
TCDB; 2.A.66.1.15; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
PaxDb; Q5I0E9; -.
Ensembl; ENSRNOT00000086579; ENSRNOP00000074897; ENSRNOG00000057404.
GeneID; 360539; -.
KEGG; rno:360539; -.
UCSC; RGD:1311123; rat.
CTD; 55244; -.
RGD; 1311123; Slc47a1.
eggNOG; KOG1347; Eukaryota.
eggNOG; COG0534; LUCA.
GeneTree; ENSGT00390000015713; -.
HOGENOM; HOG000060313; -.
HOVERGEN; HBG056043; -.
InParanoid; Q5I0E9; -.
KO; K03327; -.
OMA; LCMEWWA; -.
OrthoDB; EOG091G06X2; -.
PhylomeDB; Q5I0E9; -.
TreeFam; TF324441; -.
Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
PRO; PR:Q5I0E9; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000057404; -.
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; IDA:RGD.
GO; GO:0015238; F:drug transmembrane transporter activity; IDA:RGD.
GO; GO:0005451; F:monovalent cation:proton antiporter activity; IMP:RGD.
GO; GO:0006855; P:drug transmembrane transport; IDA:RGD.
GO; GO:0015893; P:drug transport; IDA:RGD.
GO; GO:0015695; P:organic cation transport; IDA:RGD.
InterPro; IPR002528; MATE_fam.
Pfam; PF01554; MatE; 2.
TIGRFAMs; TIGR00797; matE; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 566 Multidrug and toxin extrusion protein 1.
/FTId=PRO_0000312849.
TRANSMEM 37 57 Helical. {ECO:0000255}.
TRANSMEM 72 92 Helical. {ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TRANSMEM 257 276 Helical. {ECO:0000255}.
TRANSMEM 295 315 Helical. {ECO:0000255}.
TRANSMEM 336 356 Helical. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TRANSMEM 437 457 Helical. {ECO:0000255}.
TRANSMEM 543 563 Helical. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q96FL8}.
MUTAGEN 62 62 C->G,F,L,M: Reduction of in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 64 64 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 95 95 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 110 110 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 125 125 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 126 126 C->G,F,L,M: Reduction of TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 129 129 C->G: Modest reduction of TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 209 209 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 240 240 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 251 251 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 270 270 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 356 356 C->G: Modest reduction of TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 385 385 H->Q,F,L,M,P,S,W: Important reduction of
TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 392 392 C->G: Modest reduction of TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 444 444 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 451 451 C->G: Modest reduction of TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 465 465 C->G: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 471 471 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
MUTAGEN 490 490 H->Q: No change in TEA uptake.
{ECO:0000269|PubMed:17327464}.
CONFLICT 529 529 D -> Y (in Ref. 1; BAF02627).
{ECO:0000305}.
SEQUENCE 566 AA; 61440 MW; 67C9486E9F606A21 CRC64;
MEVLEEPAPG PGGADAAERR GLRRLLLSGF QEELRALLVL AGPAFLAQLM MFLISFISSV
FCGHLGKLEL DAVTLAIAVI NVTGISVGHG LSSACDTLIS QTYGSQNLKH VGVILQRGTL
ILLLCCFPCW ALFINTEQIL LLFRQDPDVS RLTQTYVMVF IPALPAAFLY TLQVKYLLNQ
GIVLPQVITG IAANLVNALA NYLFLHQLHL GVMGSALANT ISQFALAIFL FLYILWRKLH
HATWGGWSWE CLQDWASFLQ LAIPSMLMLC IEWWAYEVGS FLSGILGMVE LGAQSITYEL
AIIVYMIPAG FSVAANVRVG NALGAGNIDQ AKKSSAISLI VTELFAVTFC VLLLGCKDLV
GYIFTTDWDI VALVAQVVPI YAVSHLFEAL ACTCGGVLRG TGNQKVGAIV NAIGYYVIGL
PIGISLMFVA KLGVIGLWSG IIICSVCQTS CFLVFIARLN WKLACQQAQV HANLKVNVAL
NSAVSQEPAH PVGPESHGEI MMTDLEKKDE IQLDQQMNQQ QALPVHPKDS NKLSGKQLAL
RRGLLFLGVV LVLVGGILVR VYIRTE


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