ID A0A3Q1BHV7_AMPOC Unreviewed; 1160 AA.
AC A0A3Q1BHV7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Solute carrier family 12 member 5-like {ECO:0000313|Ensembl:ENSAOCP00000013173.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000013173.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000013173.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1BHV7; -.
DR Ensembl; ENSAOCT00000021156.1; ENSAOCP00000013173.1; ENSAOCG00000017716.1.
DR GeneTree; ENSGT00940000165387; -.
DR Proteomes; UP000257160; 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: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; 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:UP000257160};
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 168..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..321
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 430..720
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 734..851
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 865..990
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 1092..1160
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 126937 MW; C7722B29FC704723 CRC64;
MSQRFTVSKS DGDRRPSDIQ GGEVNQLFEG DEPEISGGGG GAEGEAAAGA EVVVVLKGDS
NPKESSPFIN SSDAAAEKSQ QYDGKNMALF EEEMDTSPMV SSLLSSLANY SNLPQGSKEH
EEAENNEAES SRKKPVKAPQ LGTLMGVYLP CIQNIFGVIL FLRMTWLVGI GGVIGTFVIV
FMCCATTMLT AISMSAIATN GVVPAGGSYY MISRSLGPEF GGAVGICFYL GTTYAGAMYI
LGAIELLLIY IVPKAAIFPL EGLEGAEAEA ALLNNMRVYG TILLTSMATV VFVGVKYVNK
LALVFLACVI LSILAVYAGV IKTGIDPPDF PVCVLGNRTL VWKTFDVCAK TIETANGTVT
TQLWSMFCDS PLLNATCDKY FASNNVTQIQ GIPGVTSGIL AENLFGNYYE KGDLIARKNM
ESAMDQDDPL TNANRYVLAD ITSFFTLLVG IYFPSVTGIM AGSNRSGDLR DAQKSIPIGT
IAAITTTSTV YMSSVILFGA CIEGVVLRDK FGEGVHGNLV IGTLAWPSPW VIVIGSFFST
CGAGLQSLTG APRLLQAIAK DGIVPALRIF GHGKANGEPT WSLLLTACIC ESGILIASLD
SVAPILSMFF LMCYMFVNLA CALQTLLRTP NWRPRFKFYH WALSFLGMSL CLTLMFLCSW
YYALVAMVIA GSIYKYIEFA GAEKEWGDGI RGLSLSAARY ALMRLEEGPP HTKNWRPQLL
VLVNTDAEQN IEQPRLLSLT NQLKAGKGLT IVGTALEGTF LENHEQAQRA EQALHKLMET
ERVKGFCQVT VSSNLRDATS HLLQASGLGG LKHNAVLVSW PRNWKQGDEH QTWRNFIELV
RETTAAHLAL LVPKNISAFP SNGERFTEGH IDVWWIVHDG GMLMLLPFLL RQHKVWRKCK
MRIFTVAQMD DNSIQMKKDL TTFLYHLRID AMVEVVEMHD SDISAYTYEK TLVMEQRSQM
LKQINLTKNE REREIQSITD SSRGSIRRKN PAAVTTQLSV TEDPPAASKE EKPEEEVQLI
HDNTTPASPA TPATPLTPGE AAQSPGEQVQ MTWTEKCDGE PAKPPGAATP EGIKDIFNMK
PEWENLNQFN VRRMHTALRL NEVIIKKSSE AKLVLLNMPG PPKNRTGDEN YMEFLEVLTE
GLNRVLLVRG GGREVITIYS
//
