ID A0A668AZ72_9TELE Unreviewed; 1077 AA.
AC A0A668AZ72;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Solute carrier family 12 member 4 {ECO:0000313|Ensembl:ENSMMDP00005054381.1};
GN Name=SLC12A4 {ECO:0000313|Ensembl:ENSMMDP00005054381.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005054381.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005054381.1}
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; A0A668AZ72; -.
DR Ensembl; ENSMMDT00005055429.1; ENSMMDP00005054381.1; ENSMMDG00005023724.1.
DR GeneTree; ENSGT00940000157672; -.
DR Proteomes; UP000472263; Unplaced.
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:SF46; SOLUTE CARRIER FAMILY 12 MEMBER 4; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 3.
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:UP000472263};
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 118..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..261
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 359..659
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 673..791
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 805..876
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 968..1077
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
SQ SEQUENCE 1077 AA; 119670 MW; 2CF07911F20131C7 CRC64;
FCQSFYVTSV PFLNSTDATK KNDFYDKNLA LFEEELDIRP KVSSLLSRLV NYTNITQGAK
EHEEEESAEA SLRKAPKSPN MGTLMGVYLP CLQNIFGVIL FLRLTWIVGT AGIVQSLLIV
LMCCSCTMLT AISMSAIATN GVVPAGGAYF MISRSLGPEF GGAVGLCFYL GTTFAAAMYI
LGAIEIFLKY LVPQGTMTIF HATDPHGGDS AMLNNMRVYG SLCLSLMAVV VFVGVKYVNK
LASLFLACVI ISIVSIYAGA IKSITHPPEF PICMLGNRTL VRDFDVCAKT VVQGNYTVPS
NLSEKFCPLG NMSSAQCDEY FSQNNVTEVQ GIPGLASGII RENMWGDYLQ KGEILEKAGL
QSVDVHGAME NFAMYVSADI ATSFTLLVGI FFPSATGIMA GSNRSGDLRD AQKSIPVGTI
LAITTTSLVY FSSVVLFGAC IEGVVLRDKF GDAVSNNLVV GTLSWPSPWV IVIGSFFSTV
GAGLQSLTGA PRLLQAIAKD NIIPFLRVFG HGKANGEPTW ALLLTGLIAE LGILIASLDM
VAPILSMFFL MCYLFVNLAC AVQTLLRTPN WRPRFKYYHW ALSFLGMSMC LALMFISSWY
YAIVAMGIAG MIYKYIEYQG AEKEWGDGIR GLSLSAARYA LLRLEVGPPH TKNWRPQLLV
LLKLDEDLHV KYPRLLTFAS QLKAGKGLTI VGSVIQGNFL DSYGETQAAE QAIKNMMEIE
RVKGFCQVVV ASKVREGIAH LIQSCGLGGM KHNTVVMGWP YGWRQSEDPR AWKTFINTVR
CTTAAHLALM VPKNVSFYPS NHERFTDGNI DVWWIVHDGG MLMLLPFLLK QHKVWRKCKM
RIFTVAQMDD NSIQMKKDLA TFLYQLRIEA EVEVVEMHDS DISAYTYERT LMMEQRSQML
RQMRLSSAER DREVCLSFLQ IYTCLCIEYG VSSCSLGPLQ AQLVKDRHSL IRMGSLYSDE
EEEVAEPPPE KVQMTWTKEK CEAERRNRNN TPENFRELIS LKPDQSNVRR MHTAVKLNEV
IVNRSHDARL VLLNMPGPPR NTDGDENYME FLEVLTEGLE RVLLVRGGGR EVITIYS
//