TRK2_YEAST
ID TRK2_YEAST Reviewed; 889 AA.
AC P28584; D6VXB1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Low-affinity potassium transport protein;
GN Name=TRK2; Synonyms=RPD2; OrderedLocusNames=YKR050W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2072919; DOI=10.1128/mcb.11.8.4266-4273.1991;
RA Ko C.H., Gaber R.F.;
RT "TRK1 and TRK2 encode structurally related K+ transporters in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 11:4266-4273(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: This protein is required for low-affinity potassium
CC transport.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
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DR EMBL; M65215; AAA35172.1; -; Genomic_DNA.
DR EMBL; Z28275; CAA82128.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09201.1; -; Genomic_DNA.
DR PIR; A41259; A41259.
DR RefSeq; NP_012976.1; NM_001179840.1.
DR AlphaFoldDB; P28584; -.
DR BioGRID; 34181; 86.
DR DIP; DIP-5225N; -.
DR IntAct; P28584; 3.
DR MINT; P28584; -.
DR STRING; 4932.YKR050W; -.
DR TCDB; 2.A.38.2.3; the k(+) transporter (trk) family.
DR PaxDb; P28584; -.
DR PRIDE; P28584; -.
DR EnsemblFungi; YKR050W_mRNA; YKR050W; YKR050W.
DR GeneID; 853924; -.
DR KEGG; sce:YKR050W; -.
DR SGD; S000001758; TRK2.
DR VEuPathDB; FungiDB:YKR050W; -.
DR eggNOG; KOG1341; Eukaryota.
DR GeneTree; ENSGT00940000176441; -.
DR HOGENOM; CLU_005947_0_1_1; -.
DR InParanoid; P28584; -.
DR OMA; MLIRGRH; -.
DR BioCyc; YEAST:G3O-32020-MON; -.
DR PRO; PR:P28584; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P28584; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140107; F:high-affinity potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:SGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:SGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:SGD.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004773; K/Na_transp_Trk/HKT.
DR InterPro; IPR015958; Trk_fungi.
DR Pfam; PF02386; TrkH; 1.
DR PIRSF; PIRSF002450; K+_transpter_TRK; 1.
DR TIGRFAMs; TIGR00934; 2a38euk; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..889
FT /note="Low-affinity potassium transport protein"
FT /id="PRO_0000070464"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..657
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 189..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 889 AA; 101087 MW; 4A41448C9560276C CRC64;
MPTAKRTSSR ASLALPFQLR LVHKKSWGHR LRDFISGFLK SCRPIAKYVF PNFIVVHYIY
LITLSIIGSI LLYPCKNTAF IDVLFLAAGA STQGGLATKS TNDFNLYQQI VVYVITLLST
PILIHGFLAF VRLYWFERYF DNIRDISKQN FKLRRTMTLQ QRELSGSSGN AARSRSFKDN
LFRGKFVSRE DPRQSASDVP MDSPDTSALS SISPLNVSSS KEESSDTQSS PPNFSSKRQP
SDVDPRDIYK SIMMLQKQQE KSNANSTDSF SSETNGPAFI VQERHERRAP HCSLKRHSVL
PSSQELNKLA QTKSFQKLLG LRRDEGDHDY FDGAPHKYMV TKKKKISRTQ SCNIPTYTAS
PSPKTSGQVV ENHRNLAKSA PSSFVDEEMS FSPQESLNLQ FQAHPPKPKR REGDIGHPFT
RTMSTNYLSW QPTFGRNSVF IGLTKQQKEE LGGVEYRALR LLCCILMVYY IGFNILAFVT
IVPWACTRHH YSEIIRRNGV SPTWWGFFTA MSAFSNLGLS LTADSMVSFD TAPYPLIFMM
FFIIIGNTGF PIMLRFIIWI MFKTSRDLSQ FKESLGFLLD HPRRCFTLLF PSGPTWWLFT
TLVVLNATDW ILFIILDFNS AVVRQVAKGY RALMGLFQSV CTRTAGFNVV DLSKLHPSIQ
VSYMLMMYVS VLPLAISIRR TNVYEEQSLG LYDSGQDDEN ITHEDDIKET DHDGESEERD
TVSTKSKPKK QSPKSFVGAH LRRQLSFDLW YLFLGLFIIC ICEGRKIEDV NKPDFNVFAI
LFEVVSAYGT VGLSLGYPNT NTSLSAQFTV LSKLVIIAML IRGRNRGLPY TLDRAIMLPS
DKLEQIDRLQ DMKAKGKLLA KVGEDPMTTY VKKRSHKLKK IATKFWGKH
