ID A0A401Q212_SCYTO Unreviewed; 475 AA.
AC A0A401Q212;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Multidrug and toxin extrusion protein {ECO:0000256|RuleBase:RU004914};
GN ORFNames=scyTo_0016951 {ECO:0000313|EMBL:GCB79390.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB79390.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB79390.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000256|ARBA:ARBA00010199,
CC ECO:0000256|RuleBase:RU004914}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU004914}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB79390.1}.
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DR EMBL; BFAA01010643; GCB79390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Q212; -.
DR STRING; 75743.A0A401Q212; -.
DR OMA; EFWILLK; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 PANTHER; PTHR11206:SF153; ETHIONINE RESISTANCE-CONFERRING PROTEIN 1; 1.
DR PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR Pfam; PF01554; MatE; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU004914};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Transmembrane {ECO:0000256|RuleBase:RU004914};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004914}.
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
FT TRANSMEM 456..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004914"
SQ SEQUENCE 475 AA; 51328 MW; CF6A3FDF314A9A36 CRC64;
MTDLMQVASS TAPQTPGTCG NLFLRKIRRI LPGNFWQEAK DLTRLAGPVF LAQLMILLLN
VVSTIFCGHL GKVELDAVSL ATAMVNVSGI SVGAGLSIAC DTLISQTFGS KNLKRIGVIL
QRGILILMIA CFPCWAIFIN TENILLAFKQ SPEVAKLTST YVMIFVPALP AVFLYQLEMR
YLQNQGITMP QILTGFIANI FNALVNYLLL NVLALGVQGS AAANVVSQYC QTSLLFGYIR
WRKLHVKTWE GIISEVQLGA QCVLYQILSI VYMAPLGFSV AAAVRVGTAL GAGNPEKAKN
SAKVALWCIV LRGAGMQRLG AIGNLVGFYL IGFPIGISLM FAAKLGIIGF WYGIIICVFC
QFTFYQIVIC RMNWNEASNQ ALINAGVKKD VGPSHSTSGG QTENISTGAH PGNIAVIEVG
PVENNVGPEH LRRESFAPKT SVCEILTVKQ LIIRRGLAFL SGPLILAIGL LLKNM
//
