TRK1_SCHPO
ID TRK1_SCHPO Reviewed; 841 AA.
AC P47946;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Potassium transport protein 1;
GN Name=trk1; Synonyms=trk; ORFNames=SPAC3F10.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7642145; DOI=10.1016/0378-1119(95)00274-a;
RA Soldatenkov V.A., Velasco J.A., Avila M.A., Dritschilo A., Notario V.;
RT "Isolation and characterization of SpTRK, a gene from Schizosaccharomyces
RT pombe predicted to encode a K+ transporter protein.";
RL Gene 161:97-101(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=10629185; DOI=10.1128/jb.182.2.394-399.2000;
RA Calero F., Gomez N., Arino J., Ramos J.;
RT "Trk1 and Trk2 define the major K(+) transport system in fission yeast.";
RL J. Bacteriol. 182:394-399(2000).
CC -!- FUNCTION: Together with TRK2, defines the major, high-affinity
CC potassium influx transport system. Involved in maintenance of the
CC proper sodium/potassium ratio in the cell and in regulating the plasma
CC membrane potential. {ECO:0000269|PubMed:10629185}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
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DR EMBL; L36563; AAC41667.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93300.1; -; Genomic_DNA.
DR PIR; S50225; S50225.
DR PIR; T38703; T38703.
DR RefSeq; NP_593934.1; NM_001019362.2.
DR AlphaFoldDB; P47946; -.
DR BioGRID; 279483; 34.
DR STRING; 4896.SPAC3F10.02c.1; -.
DR iPTMnet; P47946; -.
DR SwissPalm; P47946; -.
DR PaxDb; P47946; -.
DR PRIDE; P47946; -.
DR EnsemblFungi; SPAC3F10.02c.1; SPAC3F10.02c.1:pep; SPAC3F10.02c.
DR GeneID; 2543048; -.
DR KEGG; spo:SPAC3F10.02c; -.
DR PomBase; SPAC3F10.02c; trk1.
DR VEuPathDB; FungiDB:SPAC3F10.02c; -.
DR eggNOG; KOG1341; Eukaryota.
DR HOGENOM; CLU_005947_0_1_1; -.
DR InParanoid; P47946; -.
DR OMA; TKFPQRR; -.
DR PhylomeDB; P47946; -.
DR PRO; PR:P47946; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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; IGI:PomBase.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:PomBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:PomBase.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..841
FT /note="Potassium transport protein 1"
FT /id="PRO_0000070461"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 173..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3..27
FT /note="LNYIQRWFKWVIPTFGFLAIHYIYI -> QVGDTNFWIQGNSLYLH (in
FT Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="I -> V (in Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> Y (in Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="R -> H (in Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> I (in Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="D -> V (in Ref. 1; AAC41667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 96045 MW; 42D08CFE21C6A5D5 CRC64;
MVLNYIQRWF KWVIPTFGFL AIHYIYIISL TIIASILLFT GGTTTKIKYI DALFLASSAT
TQTGLNSVDL NSLSIWQQFI LYGFTAITVP IWMHGSISFI RLYWFRRKFK DVVRQNRTRK
FQRKLRKSLM KKSEDDEEQG VRGRKIRVML PYLHSLRSPT SLKNFSRFDT HDSTNNPYFP
DNPPSPKADI SKDEYFGKYL PKKSDTLDMD LESHNMTFHD YEPSIENKNY DFGSSHSASM
QMYEMDDLHP RLRRQSSFIS SVNPLEADDT RETLSEGALV QESLPMAYSY SDTNLVVSRD
SFTLTGDDNL FPEGGLRPAN TIDGIVRSSL SSSSLSKDTE PSTVDMHIAF TGLNKPTIER
ERNLKLRKKS RFYKKSLRSR FSRGLHRPIR WTKSFTSNRR NLTLERVLSS AFAKKREPSI
SSRHTTMSLP YLSYNPTVDR NSAFVALSKE QRDELGGIEY RALKCVCSMV TLYFIIFNIA
AFVTFIVFAY TAVGSREVID SYDLRRGWWA LFSSASSFND LGFSLIPSSF VPMNRNIFLL
LISSLFIIAG NTGFPCFFRT FIWTTYKLYP FSFEKKEAMA FLLDHPRRCF TLLFPSGATW
VLFFVLLLLN VIDLVLFMVL DTGSKAVASL PKGIRVVNAI FQSVCTRTAG FTSVSISELH
PAVLVSYMVM MYISVYPVAI NMRNTNVYEE RSLGVYRTED DEGKSFLKDH LTEQLSYDLW
YIFLGLFIIC ICEGGKISNP LDTDFSIFTV LFEVVSAYGT VGLSTGLSSS NCSLSARFTT
ISKLVIIALE LRGRHRGLPR AVDRAILLPS EKNNLKEEED YQRRHGFSID NARGSIAVSR
D
