ID A0A1F8ACG0_9EURO Unreviewed; 821 AA.
AC A0A1F8ACG0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Potassium transport protein {ECO:0000256|PIRNR:PIRNR002450};
GN ORFNames=ABOM_003575 {ECO:0000313|EMBL:OGM49430.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM49430.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM49430.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000256|ARBA:ARBA00009137, ECO:0000256|PIRNR:PIRNR002450}.
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:OGM49430.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LYCR01000009; OGM49430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8ACG0; -.
DR STRING; 109264.A0A1F8ACG0; -.
DR OrthoDB; 11415at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IEA:UniProtKB-UniRule.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004773; K/Na_transp_Trk/HKT.
DR InterPro; IPR015958; Trk_fungi.
DR NCBIfam; TIGR00934; 2a38euk; 1.
DR PANTHER; PTHR31064:SF30; HIGH-AFFINITY POTASSIUM TRANSPORT PROTEIN-RELATED; 1.
DR PANTHER; PTHR31064; POTASSIUM TRANSPORT PROTEIN DDB_G0292412-RELATED; 1.
DR Pfam; PF02386; TrkH; 1.
DR PIRSF; PIRSF002450; K+_transpter_TRK; 2.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR002450};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002450};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRNR:PIRNR002450};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|PIRNR:PIRNR002450};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR002450};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR002450};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR002450}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 400..424
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 469..498
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 531..553
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 598..615
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 658..676
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002450"
FT REGION 131..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 92985 MW; 5E1018405D135D0B CRC64;
MFSSFIRGVS SVKSQVPLLR NLSLNYILIH YIYIIAIAII TSIIIYPGND LAYIDALFFA
AGAATQSGLN TVDFNLLRTY QQVILYWVSM LTTPIFINTV LVFVRLYWFE KRFQHVVRDA
RALRQTRSRM RTISEDKDTQ NHSREEAGVG SRAIVVLREN QGDSQDREQP DAIDKTPSDS
DSGPSSSAAR DESGHTSEQE TDVNNNLRRE FGSLRVPAQL SPEHHIAFLE NQRRSKGALR
IPSPREYDRG GVPEALEEEE GEGAEAASKT SDQSDDPPSP RHVEEEEEDQ VGPMEGPHIT
INEPDMIRTR TRNSTFPRLD TRPTVRETRD LGDPSPLART TTRRPTFTGV FRSLTQERDR
NTLPYLSWNA TVGRNSQFVD LTEEQRDELG GIEYRALKTL AVVLISYYVF FHLLGIICLV
PWILTTRWGV VVTSIGQGRP WWAIFTAASS FNDVGFSITP DSMISFQEAV FPLLLLAFLI
IIGNTGFPCM LRLIIWLLSK LVRKESSLWE ELKFLLDHPR RCFTLLFPRN ATWWLFAILV
ALNGIDLIFF IILDLKDSAV TSLSTGIKIL DGLYQAACTR TAGFSVVSIA ELHPAVQVSY
MIMMYISVFP IAISLRRTNV YEEKSLGVYP SEEDDNEENQ TAPSYIGAHL RRQLSFDLWY
VFLGLFIITI VEGGRLERQD DYSFQIWSVL FEVVSAYGTV GLSMGYPGVN ASFASQFQTL
SKLVIIAMQV RGRHRGLPYS LDRAILLPSE ALNHHEIADA ERRMRRRASS LSQMSTDHRQ
SQAQENGVST GHDPRDKNTS WFSGSPILRR QSTLRSQRSQ R
//
