S47A1_RABIT
ID S47A1_RABIT Reviewed; 568 AA.
AC A7KAU2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 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, AND FUNCTION.
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: Solute transporter for tetraethylammonium (TEA), 1-methyl-4-
CC phenylpyridinium (MPP), cimetidine, procainamide. Responsible for the
CC secretion of cationic drugs across the brush border membranes.
CC {ECO:0000269|PubMed:17442726}.
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 -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and liver;
CC restricted to the apical membrane or renal proximal tubule (RPT) cells
CC and the canicular membrane of liver cells.
CC {ECO:0000269|PubMed:17442726}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; EF120627; ABO33757.1; -; mRNA.
DR RefSeq; NP_001103289.1; NM_001109819.1.
DR AlphaFoldDB; A7KAU2; -.
DR SMR; A7KAU2; -.
DR PRIDE; A7KAU2; -.
DR Ensembl; ENSOCUT00000061436; ENSOCUP00000049141; ENSOCUG00000030971.
DR GeneID; 100125995; -.
DR KEGG; ocu:100125995; -.
DR GeneTree; ENSGT00940000161644; -.
DR InParanoid; A7KAU2; -.
DR OrthoDB; 743037at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000030971; Expressed in aorta and 8 other tissues.
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..568
FT /note="Multidrug and toxin extrusion protein 1"
FT /id="PRO_0000312848"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96FL8"
SQ SEQUENCE 568 AA; 61331 MW; C8689E845DA7577A CRC64;
MEAPVELGPG GRQASPERRH WLRCLVLSDF REELRALLVL ACPAFLAQLM VFLISFVSSV
FCGHLSKLEL NAVTLAIAVI NVMGVSVGFG LSSACDTLIS QTYGSRNLKH VGVILQRGSL
ILLLCCLPCW ALFLNTQHIL LLFRQDPAVS RLTQTYVTIF IPALPATFLY TLQVKYLLNQ
GIVLPQVVTG VAANLVNALA NYLFVYQLHL GVMGSALANT VAQFTLALLL FLYILRSKVY
QATWGGWSLE CLQDWASFFR LAIPSMLMLC MEWWAYEIGS FLSGILGMVE LGAQSVTYEL
AVIVYMIPMG LSVAVNVRVG NALGAGNIEQ AKKSSAVALL VTELIAVVFC VMLLSCKDLV
GYIFTSDRDI IALVAQVTPI YAVSHLFESL AGTSGGILRG SGNQKFGAIV NAIGYYVVGL
PIGIALMFAA KLGVIGLWLG IVVCAVSQAV CFLGFIARLN WTKACQQARV HANLTVNTAS
NGNSAVLPDQ PHPVGPDSHG GIVLRDADRK EGAELNEQVH PELPLPVRPE DSAHLSGKQL
ALRRGLLLLG VILVLLAGIL VKVYVRTQ
