ID A0A4W5NB69_9TELE Unreviewed; 1066 AA.
AC A0A4W5NB69;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Solute carrier family 12 member 7b {ECO:0000313|Ensembl:ENSHHUP00000048102.1};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000048102.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000048102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A4W5NB69; -.
DR Ensembl; ENSHHUT00000049850.1; ENSHHUP00000048102.1; ENSHHUG00000028866.1.
DR GeneTree; ENSGT00940000157657; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
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:SF47; SOLUTE CARRIER FAMILY 12 MEMBER 7; 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:UP000314982};
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 104..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 567..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..283
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 407..682
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 696..801
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 813..1066
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
SQ SEQUENCE 1066 AA; 118083 MW; 017D9BED7B65D3A3 CRC64;
IERKGTLLSN QLSLFESILT FNLFHSTDDG SAPRESSPFI NNTDNDKGNL YDGKNMALFE
EEMDSNPMVS SLLNKLANYT NLTQGVKEHE EDGLVSRRAA KNPALGTLIG VYLPCLQNIL
GVILFLRLTW IVGTAGIMES LAIVVMTCSC TMLTAISMSA IATNGVVPAG GSYYMISRSL
GPEFGGAVGL CFYLGTTFAG SMYILGTIEI LLTYIVPSAA IFKAEKKEDE AEALLNNMRV
YGTCCLTLMS LVVFVGVKYV NKLALVFLAC VILSILAIYA GVIKTAFEPP DFPFFVCQII
CLLGNRTLQN HNFDQCLKTM EVDNVTVTTK LWSLFCDSPD LNATCNEYFT LNNVTVIQGI
PGLTSGVIRD NIWGDYGPNG MLVENKHQAS EPAADTSQDI YMPYVANDIT TFFTLLVGIY
FPSVTGIMAG SNRSGDLRDA QKSIPIGTIM AIATTTFICI FNDSNNSPAI QVFGDSVKGN
LVIGILAWPS PWVIVIGSFF SCCGAGLQSL TGAPRLLQAI ARDGIVPFLQ VFGHGKANGE
PTWALLLTGG ICEIGILIAS LDAVAPILSM FFLMCYLFVN LACALQTLLR TPNWRPRFKF
YHWALSFLGA SLCLSLMFIS SWYYALVAML IAGCIYKYIE YRGAEKEWGD GINGLSLNAA
RYALIRLEEA PPHTKNWRPQ MLLLLNLDSD HAVKHPRLLS FCTQLKAGKG LTIVGSVLEG
TYMTKEAEVK KAEQNIKSSM TTERTKGFCH VVASSNLRDG FSHLIQTAGL GGMKHNTVLM
AWPGTWKQSN DPRNPYHMTV RETTAAHQAL LVAKNVDSFP TNTDRLGQGT IDVWWVVHDG
GLLMLLPFLL RQHKVWRKCK MRIFTVANMD DNSIQMKKDL QMFLYHLRLD AEVEVVEMHD
SDISAFTYEK TLVMEQRSQM LKQMQLSRTE REREAQLIHD RNTASHAALN DKADAGPDRV
HMTWTKDKFL TERNRNRAEA NMGVRDIFNM KPNQSNVRRM HTAVKLNEVV VNKSQGAHLV
LLNMPGPPKN RGGDENYMEF LEVLLEGLNR VLLVRGGGRE VITIYS
//
