ID A3LSV6_PICST Unreviewed; 700 AA.
AC A3LSV6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Outward-rectifier potassium channel {ECO:0000313|EMBL:ABN65961.2};
GN Name=TOK1 {ECO:0000313|EMBL:ABN65961.2};
GN ORFNames=PICST_31186 {ECO:0000313|EMBL:ABN65961.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65961.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65961.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|RuleBase:RU003857}.
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DR EMBL; CP000498; ABN65961.2; -; Genomic_DNA.
DR RefSeq; XP_001383990.2; XM_001383953.1.
DR AlphaFoldDB; A3LSV6; -.
DR STRING; 322104.A3LSV6; -.
DR GeneID; 4839043; -.
DR KEGG; pic:PICST_31186; -.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_013394_2_0_1; -.
DR InParanoid; A3LSV6; -.
DR OMA; RVFFVSW; -.
DR OrthoDB; 5010334at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 2.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003:SF291; POTASSIUM CHANNEL SUBFAMILY K MEMBER 18; 1.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:ABN65961.2};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 81..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..320
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 383..454
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 480..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 80055 MW; 04E05209BA630663 CRC64;
MDLGITQFRR HVKAAQRAVT PSREPTFSLN NYDDKLLPLL YHTPRNKVKQ KDVPMIVKNS
LAMPITTVTS MKVRPGEPNF VYWYFVSSYF PLISACLGPL ANMISIISLV QHWRIEKATG
KEVSDEPGLI VLNSMSLVFG ILANISLLMN FSGTIKYLIT QVVSIICFLG AVVVLMVDII
ITNRDFIGQD PKYSRSEGFW FAVFTTFYYF CCAVTLLVNF LGYKLNKYPA TFNLDTKQRT
LMIYTICFAI WSVFGSVVMA HMIDDLTYGS SLYYCIVSFL TIGLGDILPK TPGAKVMVLI
LSLIGVLIMG LIVAMIRQVV MTSGGPTIFW NHIERDREKL LAKLKREHTP LTADQAFHKM
RVIRRRAHVH QLNVSLASTI IIFMVFWLIG ATVFHFCEGW SYFNGVYFCF LCLITIGYGD
YAPKTPLGRV FFVSWAVAAV PLMTILISNV GDKLFGLANH LSFMVSKALF RDDDEDDYHK
RRRQSEEVSD DIEREVNIEE DEEDYELSST GKDVGSNHKD DFSAFINGSP LDYSLHQPDH
QQTIQLQQVR QKITTKMLNQ KETYENILSF LNQLKPLISD SVENPLKRYS HSEWSELLDS
LNKEDVIIKH PDGTETVIAP ITVNAEYNYF WLSERSPLRL PLKEPNYLIM KVFFKIEKDL
NDLIDAEVED MEQLRSVMSN SSVQNVEMLN RTHHEKKGHL
//
