TRK1_YEAST
ID TRK1_YEAST Reviewed; 1235 AA.
AC P12685; D6VW56;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=High-affinity potassium transport protein;
GN Name=TRK1; OrderedLocusNames=YJL129C; ORFNames=J0693;
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=3043197; DOI=10.1128/mcb.8.7.2848-2859.1988;
RA Gaber R.F., Styles C.A., Fink G.R.;
RT "TRK1 encodes a plasma membrane protein required for high-affinity
RT potassium transport in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 8:2848-2859(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-534, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: This protein is required for high-affinity potassium
CC transport.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
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; M21328; AAA34728.1; -; Genomic_DNA.
DR EMBL; Z49404; CAA89424.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08672.1; -; Genomic_DNA.
DR PIR; S05849; PWBYH.
DR RefSeq; NP_012406.1; NM_001181562.1.
DR AlphaFoldDB; P12685; -.
DR BioGRID; 33627; 127.
DR DIP; DIP-7454N; -.
DR IntAct; P12685; 1.
DR MINT; P12685; -.
DR STRING; 4932.YJL129C; -.
DR TCDB; 2.A.38.2.1; the k(+) transporter (trk) family.
DR iPTMnet; P12685; -.
DR PaxDb; P12685; -.
DR PRIDE; P12685; -.
DR EnsemblFungi; YJL129C_mRNA; YJL129C; YJL129C.
DR GeneID; 853312; -.
DR KEGG; sce:YJL129C; -.
DR SGD; S000003665; TRK1.
DR VEuPathDB; FungiDB:YJL129C; -.
DR eggNOG; KOG1341; Eukaryota.
DR GeneTree; ENSGT00940000176441; -.
DR HOGENOM; CLU_005947_0_0_1; -.
DR InParanoid; P12685; -.
DR OMA; SGKMVNR; -.
DR BioCyc; YEAST:G3O-31579-MON; -.
DR PRO; PR:P12685; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P12685; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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 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; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1235
FT /note="High-affinity potassium transport protein"
FT /id="PRO_0000070462"
FT TRANSMEM 49..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 161..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1235 AA; 141073 MW; BCE9FDBA0BA0982B CRC64;
MHFRRTMSRV PTLASLEIRY KKSFGHKFRD FIALCGHYFA PVKKYIFPSF IAVHYFYTIS
LTLITSILLY PIKNTRYIDT LFLAAGAVTQ GGLNTVDINN LSLYQQIVLY IVCCISTPIA
VHSCLAFVRL YWFERYFDGI RDSSRRNFKM RRTKTILERE LTARTMTKNR TGTQRTSYPR
KQAKTDDFQE KLFSGEMVNR DEQDSVHSDQ NSHDISRDSS NNNTNHNGSS GSLDDFVKED
ETDDNGEYQE NNSYSTVGSS SNTVADESLN QKPKPSSLRF DEPHSKQRPA RVPSEKFAKR
RGSRDISPAD MYRSIMMLQG KHEATAEDEG PPLVIGSPAD GTRYKSNVNK LKKATGINGN
KIKIRDKGNE SNTDQNSVSS EANSTASVSD ESSLHTNFGN KVPSLRTNTH RSNSGPIAIT
DNAETDKKHG PSIQFDITKP PRKISKRVST FDDLNPKSSV LYRKKASKKY LMKHFPKARR
IRQQIKRRLS TGSIEKNSSN NVSDRKPITD MDDDDDDDDN DGDNNEEYFA DNESGDEDER
VQQSEPHSDS ELKSHQQQQE KHQLQQNLHR MYKTKSFDDN RSRAVPMERS RTIDMAEAKD
LNELARTPDF QKMVYQNWKA HHRKKPNFRK RGWNNKIFEH GPYASDSDRN YPDNSNTGNS
ILHYAESILH HDGSHKNGSE EASSDSNENI YSTNGGSDHN GLNNYPTYND DEEGYYGLHF
DTDYDLDPRH DLSKGSGKTY LSWQPTIGRN SNFLGLTRAQ KDELGGVEYR AIKLLCTILV
VYYVGWHIVA FVMLVPWIIL KKHYSEVVRD DGVSPTWWGF WTAMSAFNDL GLTLTPNSMM
SFNKAVYPLI VMIWFIIIGN TGFPILLRCI IWIMFKISPD LSQMRESLGF LLDHPRRCFT
LLFPKAATWW LLLTLAGLNI TDWILFIILD FGSTVVKSLS KGYRVLVGLF QSVSTRTAGF
SVVDLSQLHP SIQVSYMLMM YVSVLPLAIS IRRTNVYEEQ SLGLYGDMGG EPEDTDTEDD
GNDEDDDEEN ESHEGQSSQR SSSNNNNNNN RKKKKKKKTE NPNEISTKSF IGAHLRKQLS
FDLWFLFLGL FIICICEGDK IKDVQEPNFN IFAILFEIVS AYGTVGLSLG YPDTNQSFSR
QFTTLSKLVI IAMLIRGKNR GLPYSLDRAI ILPSDRLEHI DHLEGMKLKR QARTNTEDPM
TEHFKRSFTD VKHRWGALKR KTTHSRNPKR SSTTL
