TRK2_SCHPO
ID TRK2_SCHPO Reviewed; 880 AA.
AC Q10065; Q9UTH7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Potassium transport protein 2;
GN Name=trk2; ORFNames=SPAC1639.02c, SPAC1F5.12;
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 [MRNA].
RA Lichtenberg H., Martinez P., Ljungdahl P., Luehring H.;
RT "Comparative physiology of potassium transport in Schizosaccharomyces pombe
RT and Saccharomyces cerevisiae.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
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 TRK1, 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 {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB55290.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF266750; AAF74294.1; -; mRNA.
DR EMBL; CU329670; CAB55290.3; ALT_SEQ; Genomic_DNA.
DR PIR; T38083; T38083.
DR AlphaFoldDB; Q10065; -.
DR STRING; 4896.SPAC1639.02c.1; -.
DR iPTMnet; Q10065; -.
DR PaxDb; Q10065; -.
DR PRIDE; Q10065; -.
DR PomBase; SPAC1639.02c; trk2.
DR eggNOG; KOG1341; Eukaryota.
DR HOGENOM; CLU_005947_0_1_1; -.
DR InParanoid; Q10065; -.
DR PhylomeDB; Q10065; -.
DR PRO; PR:Q10065; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:PomBase.
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:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0071473; P:cellular response to cation stress; TAS:PomBase.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IGI:PomBase.
DR GO; GO:0042391; P:regulation of membrane potential; IMP: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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..880
FT /note="Potassium transport protein 2"
FT /id="PRO_0000070463"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 157..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 880 AA; 99848 MW; 2CD17CF1FE24F128 CRC64;
MQLSGFSTNG SGSLNTIVCE KLLFKPNFVQ DSFIIGMTIL CSVILYGSGN LRYIDALLLA
SGSCTQTGLQ PVDLTQISIY QQLTILLFGV LSTPITVNLG LTLFKLYFYN KRYDMVITNN
KLRMTYTYHT VRRRDTPEPS KVGNRKIRVL LDQGNQMHRP VAPETKAEEA EHQENEKHHR
HHFRLRKFAN AIDRPSFFRG NTMPALPSYA GVRNSQENED RTEALSPALG KRRMASIDNG
SLSVVQNNAR NNPVDFYIPS SFEESSFQTI PEDFEPQVHD HENQTQLNHH LDNNSSISSH
NPSLETANDG NQETVSSSNS NYSTTRVDND PHVASYSPQN SNFDHQAAAT TNDAHQNVVR
GSAITIAPTP VPRHNRRPIY FADDTNGAEQ EKGAHRLDGR GRKRGKSFAV TPTLHRNERS
MSVLPFQLAK SFTSALPRRL TFNRTHTKAS TMSLPYLSYN ATVGRNSAFY ALTPVEREEL
AGIEYESLRI LTVILVVYFL FWHILGLVAF LIFIYTAKTS GRVVTDGGIN RGWWAAFTSS
SLFDNLGYSL NSDSLNSFQK AIFPQVLGTI LIFLGNTFFP IMLRFIIWIM IRTTRFSPNF
QQALYFLFEH PRRSFTLLFP SKTTWVLFLN LTLLNFASFF FFMVLDLGNS YVDKIPVGYR
IMNAIFQNAA TRSAGFTVVD LSQIAPAVMV TYMFMMYISA YPIAMSIRQT NVYEERSLGI
YAADTENDDD NNINNNNNDN NTPKRKNFLM DHIQRQLSHD LWYLFLGYFI ITIVEGRRLE
SEAEPQFTLF AILFEVISGY GTVGLSLGYK NDPSLTAQFR KISKLVMVAL QIRGRHRGLP
SALDRAVLMP SDKNFDREEE DYMRRHGKKN TNRADPVPSS
