S47A1_PONAB
ID S47A1_PONAB Reviewed; 570 AA.
AC Q5RFD2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Multidrug and toxin extrusion protein 1;
DE Short=MATE-1;
DE AltName: Full=Solute carrier family 47 member 1;
GN Name=SLC47A1; Synonyms=MATE1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Predominantly localized at the plasma
CC membrane but also found in intracellular organelles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; CR857226; CAH89525.1; -; mRNA.
DR RefSeq; NP_001124662.1; NM_001131190.2.
DR AlphaFoldDB; Q5RFD2; -.
DR SMR; Q5RFD2; -.
DR STRING; 9601.ENSPPYP00000009916; -.
DR GeneID; 100171505; -.
DR KEGG; pon:100171505; -.
DR CTD; 55244; -.
DR eggNOG; KOG1347; Eukaryota.
DR InParanoid; Q5RFD2; -.
DR OrthoDB; 743037at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..570
FT /note="Multidrug and toxin extrusion protein 1"
FT /id="PRO_0000312847"
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..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..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..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 508..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96FL8"
SQ SEQUENCE 570 AA; 62009 MW; 6DE41106E9353BE8 CRC64;
MEAPEEPAPV RGGPEATLEI HGSRFLRLSA FREELRALLV LAGPAFLVQL MVFLISFISS
VFCGHLGKLE LDAVTLAIAV INVTGVSVGF GLSSACDTLI SQTYGSQNLK HVGVILQRSA
LILLLCCFPC WALFLNTQHI LLLFRQDPDV SRLTQTYVTI FIPALPATFL YMLQVKYLLN
QGIVLPQIVT GVAANLVNAL ANYLFLHQLH LGAIGSALAN LISQYTLALL LFFYILGKKL
HQATWGGWSL ECLQDWASFL HLAVPSMLML CMEWWAYEVG SFLSGILGMV ELGAQSIVYE
LAIIVYMVPA GFSVAASVRV GNALGAGDME QARKSSTVSL LITVLFAVAF SVLLLSCKDH
VGYIFTTDRD IINLVAQVVP IYAVSHLFEA LACTSGGVLR GSGNQKVGAI VNTIGYYVVG
LPIGIALMFA TKLGVMGLWS GIIICTVFQA VCFLGFIIQL NWKKACQQAQ VHANLKVNNV
PRSGNSALPQ DPLHPGCPEN LEGILTNDVG KTGETQSDQQ MRQEEPLPEH PQDSAKLSRK
QLVLRRGLLL LGVFLILLVG ILVRFYVRIQ
