ID A0A401S384_CHIPU Unreviewed; 1082 AA.
AC A0A401S384;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GCC24867.1};
GN ORFNames=chiPu_0003270 {ECO:0000313|EMBL:GCC24867.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC24867.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC24867.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC24867.1}.
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DR EMBL; BEZZ01000069; GCC24867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S384; -.
DR STRING; 137246.A0A401S384; -.
DR OMA; ICEMGIL; -.
DR Proteomes; UP000287033; 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:UP000287033};
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 113..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..291
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 415..690
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 704..811
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 820..1082
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 119528 MW; 1684619C87198C49 CRC64;
MPTNFTVLPV DDEGAPKEGT SLAAENDPEV LASGDGIPKE SSPFINSTDI DKGTMYEGKN
LALFEEEMDR NPMVSSLLNR LANYTNLTQG VREHEEAENN EESRKKEIKA PQMGTFIGVY
LPCLQNILGV ILFLRLTWIV GAAGIFGSFW IVFICCACTL LTAISMSAIA TNGVVPAGGS
YYMISRSLGP EFGGAVGLCF YLGTTFAGAM YILGTIEILL TYIVPSAAIF KADDPSQETQ
TMLNNMRVYG TCTITLMATV VFVGVKYVNK LALVFLACVI LSILAIYAGV IKTAFSPPDF
PLCMLGNRTL ASKAFDICAK ISTVGNQTVT TQLWRLFCDS PYLNATCDEY FNLNNVTIIQ
GIPGIASGVI SENIWSTYGS QGELLEKRGL PSVPASESAT NTRLPYVFSD IATYFTMLVG
IYFPSVTGIM AGSNRSGDLK DAQKSIPTGT LLAIITTSFI YLSSIILFGA CIEGVLLRDK
FGDSVDGNLV IGTLAWPSPW VIVIGSFFST CGAGLQSLTG APRLMQAIAR DGIIPFLRVF
GHGKANGEPT WALLLTAGIC EIGILIASLD SVAPILSMFF LMCYMFVNLA CALQTLLKTP
NWRPRFTYYH WTLSFLGMSL CLALMFICSW YYALVAMVIA GCIYKYIEYR GAEKEWGDGI
RGLSLNAARY ALLRLEDGPP HTKNWRPQLL ILLNLDTEQN VKHPRLLSFT TQLKAGKGLT
IVGSVLEGTF LDRHADVQNA EQNIKTLMGL EKTKGFCHVV VSSNRRDGVS HLIQSSGLGG
MKHNTVLVAW PELWRQTDGP TGWKNFVDMV CETTAAHQAL LVTKNIDSFP TNQERFAGGT
IDIWWIVHDG GLLMLLPFLL SQHKVWKKCK MRIFTVAQID DNSIQMKKDL QLFLYQLRLD
AEVEVVEMLD NDISAFTYER TLVMEQRSQM LKQMQLSKNE REREAQLIHD RNAAAHSSGT
DRLSVSPEGV HMTWTKEKIT AEKNKNKESL SPEGVRDIFN MRPEWGNLNQ SNVRRMHTAV
KLNEVVVNRS QDARLVLLNM PGPPKNRQGD ENYMEFLEVL TEGLNRVLMV RGGGSEVITI
YS
//
