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Database: UniProt
Entry: A0A674MHZ9_TAKRU
LinkDB: A0A674MHZ9_TAKRU
Original site: A0A674MHZ9_TAKRU 
ID   A0A674MHZ9_TAKRU        Unreviewed;      1051 AA.
AC   A0A674MHZ9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Solute carrier family 12 member 5b {ECO:0000313|Ensembl:ENSTRUP00000060716.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000060716.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000060716.1, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000060716.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) + K(+)(in) = chloride(out) + K(+)(out);
CC         Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00034453};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC       {ECO:0000256|ARBA:ARBA00010593}.
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DR   AlphaFoldDB; A0A674MHZ9; -.
DR   Ensembl; ENSTRUT00000069687.1; ENSTRUP00000060716.1; ENSTRUG00000011523.3.
DR   GeneTree; ENSGT00940000165387; -.
DR   Proteomes; UP000005226; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR018491; SLC12_C.
DR   InterPro; IPR004842; SLC12A_fam.
DR   NCBIfam; TIGR00930; 2a30; 1.
DR   PANTHER; PTHR11827:SF54; SOLUTE CARRIER FAMILY 12 MEMBER 5; 1.
DR   PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF03522; SLC12; 2.
DR   PRINTS; PR01081; KCLTRNSPORT.
PE   3: Inferred from homology;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Symport {ECO:0000256|ARBA:ARBA00022847};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022847}.
FT   TRANSMEM        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        538..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        562..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        595..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..278
FT                   /note="Amino acid permease/ SLC12A"
FT                   /evidence="ECO:0000259|Pfam:PF00324"
FT   DOMAIN          392..677
FT                   /note="Amino acid permease/ SLC12A"
FT                   /evidence="ECO:0000259|Pfam:PF00324"
FT   DOMAIN          691..808
FT                   /note="SLC12A transporter C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03522"
FT   DOMAIN          823..1051
FT                   /note="SLC12A transporter C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03522"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  115513 MW;  82C42CD0B137AA13 CRC64;
     MTDCEEGEGG PNSQGDGIPK ESSPFINSST ASDAEKSQQY DGKNMALFEE EMDTSPMVSS
     LLSSLANYSN LPTGSKEHEE AENSEEGPRP SKKPAPQLGT LMGVYLPCIQ NIFGVILFLR
     MTWMVGIGGV FGSFIIVFMC CSTTMLTAIS MSAIATNGVV PAGGSYYMIS RSLGPEFGGA
     VGICFYLGTT FAGAMYILGC IEILLIYIVP QAAIFKIEGL EGPEAEAALL NNMRVYGTIV
     LSFMALVVFV GVKYVNKLAL VFLACVILSI VAVYAGVIKT AVDPPVFPVC ILGNRTLVSK
     GYDICAKVVD IDNETVTTKL WRSFCDSEYL NATCDEYFNN NNVTEIQGIP GVTSGILAEN
     LFGKYLEKGA ILEKRGLPSD VDPDGPTTNS NRYVVADITS FFTLLVGIYF PSVTGIMAGS
     NRSGDLRDAQ KSIPIGTIAA ITTTSTVYMS CVVLFGACIE GVVLRDKFGE GVNGNLVIGT
     LAWPSPWVIV FGSFFSTCGA GLQSLTGAPR LLQAISRDGI IPFLRVFGHG KANGEPTWAL
     LLTAGICEIG IIIASLDAVA PILSMFFLMC YMFVNLACAL QTLLRTPNWR PRFKFYHWAL
     SFLGMSLCLS LMFICSWYYA IVAMGIATCI YKYIEFCGAE KEWGDGIRGI SLSAARFALM
     RLEEGPPHTK NWRPQILVLV SVDTEQNVEQ PRLLSLTNQL KAGKGLTIVG TSVQGTFLDS
     YTEAQRADQT LCKLMEAEKV KGFPQVVVSS NLRDGTSHLI QAGGLGGLKH NTVMVSWPHK
     WRQPEYHQQF RNFIEVVRET TVASMALLVP KNISSYPSNG ERFTEGHIDV WWIVHDGGML
     MLLPFLLRQH KVWRKCKMRI FTVAQMDDNS IQMKKDLITF LYHLRIDAQV EVVEMHDTDI
     SAYTYEKTLV MEERSQMLKQ MHLTKNEMER EVQLIQSKNA SSPTSPTGPT SPAWTDKGSA
     PVLLNPEVGK DLFNMKPNQV DVRRMHTAVR LNEVIIKKSK EAKLVLLNMP GPPRNRVGNE
     NYMAFLEVLT EGLNRVLLVR GGGREVITIY S
//
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