ID   S47A2_RABIT             Reviewed;         601 AA.
AC   A7KAU3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   08-NOV-2023, entry version 54.
DE   RecName: Full=Multidrug and toxin extrusion protein 2;
DE            Short=MATE-2;
DE   AltName: Full=MATE2-K {ECO:0000303|PubMed:17442726};
DE   AltName: Full=Solute carrier family 47 member 2;
GN   Name=SLC47A2; Synonyms=MATE2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=17442726; DOI=10.1152/ajprenal.00102.2007;
RA   Zhang X., Cherrington N.J., Wright S.H.;
RT   "Molecular identification and functional characterization of rabbit MATE1
RT   and MATE2-K.";
RL   Am. J. Physiol. 293:F360-F370(2007).
CC   -!- FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation
CC       antiporter (PubMed:17442726). Mediates the efflux of cationic
CC       compounds, such as the model cations, tetraethylammonium (TEA) and 1-
CC       methyl-4-phenylpyridinium (MPP+), the platinum-based drug oxaliplatin
CC       or weak bases that are positively charged at physiological pH,
CC       cimetidine or the antidiabetic drug metformin. Mediates the efflux of
CC       the endogenous compounds creatinine, thiamine and estrone-3-sulfate.
CC       Plays a physiological role in the excretion of drugs, toxins and
CC       endogenous metabolites through the kidney (By similarity).
CC       {ECO:0000250|UniProtKB:Q86VL8, ECO:0000269|PubMed:17442726}.
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:0000250|UniProtKB:Q86VL8};
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:0000250|UniProtKB:Q86VL8};
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:0000250|UniProtKB:Q86VL8};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:17442726};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VL8};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q86VL8}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Detected in the renal urinary tubules.
CC       {ECO:0000250|UniProtKB:Q86VL8}.
CC   -!- TISSUE SPECIFICITY: Expressed in renal cortical tissues.
CC       {ECO:0000269|PubMed:17442726}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
CC       (TC 2.A.66.1) family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-30 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; EF121852; ABP96920.1; -; mRNA.
DR   RefSeq; NP_001103290.2; NM_001109820.2.
DR   AlphaFoldDB; A7KAU3; -.
DR   SMR; A7KAU3; -.
DR   STRING; 9986.ENSOCUP00000010244; -.
DR   PaxDb; 9986-ENSOCUP00000010244; -.
DR   GeneID; 100125996; -.
DR   KEGG; ocu:100125996; -.
DR   CTD; 146802; -.
DR   eggNOG; KOG1347; Eukaryota.
DR   InParanoid; A7KAU3; -.
DR   OrthoDB; 10858at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015695; P:organic cation transport; IDA:UniProtKB.
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   NCBIfam; TIGR00797; matE; 1.
DR   PANTHER; PTHR11206:SF81; MULTIDRUG AND TOXIN EXTRUSION PROTEIN 2; 1.
DR   PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR   Pfam; PF01554; MatE; 2.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..601
FT                   /note="Multidrug and toxin extrusion protein 2"
FT                   /id="PRO_0000311954"
FT   TOPO_DOM        1..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..402
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        481..577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        599..601
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   601 AA;  64175 MW;  571A84BF28E95F02 CRC64;
     MNTAFAGFDE NRAGRRAPGC TGRPAFGLGM DSQQDVVNLD QGGCCPALRK LLPRGFWDEA
     RALFVLSGPL FLFQVLNFLT YVVGTVFCGH LGKVELASVT LGVAFVNVCG VSVGAGLSSA
     CDTLMSQSFG SPNKKHVGVI LQRGSLILLL CCLPCWALFL NTQHILLLFR QDPAVSRLTQ
     DYAMIFIPGL PAIFLYSLLA KYLQNQGIVW PQVLSGVVGN CVNGVANYAL VSVLNLGVRG
     SAYANTISQF VQAAFLFLHI VLKKLHLETW EGWSSQCLRD WGPFLSLAIP SMLMMCVEWW
     AYEIGSFLMG LLGVVDLSGQ AIIYEVATVV YMIPMGLGMA VCVRVGTALG AADTLQAKRS
     AVSGLLCTAG TSLVVGTLLG LLNSQLGYIF TSDEEVIALV NQVLPIYIVF QLVEAVCCVF
     GGVLRGTGKQ AFGAIVNAIM YYIVGLPLGI VLTFVVGMRI MGLWLGMLTC IFLAAVTFVV
     YAVQLDWKLA AEEAQKHAGL QQQQQQQQQQ GAECTAPSPG PDKAVVSSVA TGCNPGIALT
     MYSRPGCHVD FYGRPEAAPA PAAPASRLSV RQLLFRRGAA LAASVAVLMA GLLVRVLTTG
     Y
//