ID A0A667XGK3_9TELE Unreviewed; 1048 AA.
AC A0A667XGK3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Solute carrier family 12 member 7a {ECO:0000313|Ensembl:ENSMMDP00005014307.1};
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:ENSMMDP00005014307.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005014307.1}
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; A0A667XGK3; -.
DR Ensembl; ENSMMDT00005014704.1; ENSMMDP00005014307.1; ENSMMDG00005004290.1.
DR GeneTree; ENSGT00940000157657; -.
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: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: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 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 576..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..257
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 382..657
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 671..788
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 789..1048
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 116543 MW; 227CB6E04C7F05B6 CRC64;
MSVLLGDDNR RESSPFINSE NDRGQYYDGK NMEEMDSNPM VSSLLNKLAN YTNLPQGVRE
HEEAENEDGV RRVTVMGPQM GTFIGVYLPC MQNILGVILF LRLTWIVGTA GILGSFAIVS
MCCACTLLTA ISMSAIATNG VVPAGGSYYM ISRSLGPEFG GAVGLCFYLG TTFAGSMYIL
GTIEILLTYI VPDAAIFVAA TKEDESAAML NNMRVYGSCC LALMALVVFV GVKYVNKLAL
VFLAWVVLSI MAIYAGVIRT VIEPPDFPIC LLGNRTLKND QFDKCLKTEV VKNITYTTDL
WSLFCESKHL NATCDDYFSV NNVTEIQGIP GLLSGVIKEN LWGDYGPVEM LIEKKSMPSV
AVKDNTNDIY KPYVFNDIAT YFTLLVGIYF PSVTGIMAGS NRSGDLRDAQ RSIPIGTILA
IATTSFIYIS CVVLFGACIE GVVLRDKFGD SVKKNLVVGT LAWPSPWVIV IGSFFSCCGA
GLQSLTGAPR LLQAIARDGI VPFLQVFGHG KANGEPTWAL LLTAGICEIG ILIASLDAVA
PILSMFFLMC YLFVNLACAV QTLLRTPNWR PRFKFYHWTL SFLGMSLCLS LMFISSWYYA
LVAMVIAGCI YKYIEYRGAE KEWGDGIRGL SLNAARYALI RLEESPPHTK NWRPQLLVLC
KLDPDMLVKH PRLLSFTSQL KAGKGLTIVC SVLEGTYMTR GNDAKTGEEN LKAAMSAERT
KGFAHVVVAS NLRDGFSLLI QSAGLGGMKH NAVLMAWPAG WKQAPDSYAW KNFIETVRET
TSAHQALLVA KNIDHFPGNQ ERLKEGTIDV WWIVHDGGLL MLLPFLLRQH KVWRKCKMRI
FTVAQIDDNS IQMKKDLQMF LYHLRLDAEV EVVEMHGSDI SAFTYEKTLV MEQRSQMLRQ
MQLSRTERER EAQLIHDRNT ASHSALNDKS ATTSPENVHM TWTKDKLVNE RTKNREGNVG
VKDIFNMKPE WENLNQSNVR RMHTAVKLNE AVVNKSQNSQ LVLLNMPGPP KNKEGDENYM
EFLEVLMEGL DRVLLVRGGG REVITIYS
//