IST2_YEAST
ID IST2_YEAST Reviewed; 946 AA.
AC P38250; D6VQ87; P89499;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Increased sodium tolerance protein 2;
GN Name=IST2; OrderedLocusNames=YBR086C; ORFNames=YBR0809;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 243.
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 FUNCTION, INTERACTION WITH BTN2, AND SUBCELLULAR LOCATION.
RX PubMed=15701790; DOI=10.1128/ec.4.2.281-288.2005;
RA Kim Y., Chattopadhyay S., Locke S., Pearce D.A.;
RT "Interaction among Btn1p, Btn2p, and Ist2p reveals potential interplay
RT among the vacuole, amino acid levels, and ion homeostasis in the yeast
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:281-288(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11030653; DOI=10.1126/science.290.5490.341;
RA Takizawa P.A., DeRisi J.L., Wilhelm J.E., Vale R.D.;
RT "Plasma membrane compartmentalization in yeast by messenger RNA transport
RT and a septin diffusion barrier.";
RL Science 290:341-344(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-701; SER-704; SER-720;
RP THR-726; SER-729 AND SER-757, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638 AND SER-757, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-757 AND SER-793, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-701; SER-704; SER-720;
RP THR-726; SER-729; TYR-730; SER-793; SER-844; SER-847 AND THR-850, 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: May be involved in ion homeostasis together with BTN1 or
CC BTN2. {ECO:0000269|PubMed:15701790}.
CC -!- SUBUNIT: Interacts with BTN2. {ECO:0000269|PubMed:15701790}.
CC -!- INTERACTION:
CC P38250; P53286: BTN2; NbExp=2; IntAct=EBI-21520, EBI-3796;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11030653,
CC ECO:0000269|PubMed:15701790}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11030653, ECO:0000269|PubMed:15701790}.
CC Note=Correct localization requires BTN2. Localizes to the mother cell
CC in small budded cells and to the bud in medium and large budded cells.
CC Transported to the bud tip by an actomyosin based process.
CC Compartmentalization maintained by a septin mediated membrane diffusion
CC barrier at the mother-bud neck.
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; X78993; CAA55593.1; -; Genomic_DNA.
DR EMBL; Z35955; CAA85034.1; -; Genomic_DNA.
DR EMBL; Z35956; CAA85037.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07207.1; -; Genomic_DNA.
DR PIR; S48255; S48255.
DR RefSeq; NP_009643.2; NM_001178434.1.
DR AlphaFoldDB; P38250; -.
DR SMR; P38250; -.
DR BioGRID; 32792; 203.
DR DIP; DIP-6714N; -.
DR IntAct; P38250; 8.
DR MINT; P38250; -.
DR STRING; 4932.YBR086C; -.
DR TCDB; 1.A.17.1.19; the calcium-dependent chloride channel (ca-clc) family.
DR iPTMnet; P38250; -.
DR MaxQB; P38250; -.
DR PaxDb; P38250; -.
DR PRIDE; P38250; -.
DR EnsemblFungi; YBR086C_mRNA; YBR086C; YBR086C.
DR GeneID; 852382; -.
DR KEGG; sce:YBR086C; -.
DR SGD; S000000290; IST2.
DR VEuPathDB; FungiDB:YBR086C; -.
DR eggNOG; KOG2513; Eukaryota.
DR HOGENOM; CLU_014462_0_0_1; -.
DR InParanoid; P38250; -.
DR OMA; MFSTIWP; -.
DR BioCyc; YEAST:G3O-29053-MON; -.
DR Reactome; R-SCE-2672351; Stimuli-sensing channels.
DR PRO; PR:P38250; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38250; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:SGD.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007632; Anoctamin.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..946
FT /note="Increased sodium tolerance protein 2"
FT /id="PRO_0000084261"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 701
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 730
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 850
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 243
FT /note="I -> Y (in Ref. 1; CAA55593 and 2; CAA85034/
FT CAA85037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 105854 MW; 79E90CA4DF89585F CRC64;
MSQTITSLDP NCVIVFNKTS SANEKSLNVE FKRLNIHSII EPGHDLQTSY AFIRIHQDNA
KPLFSFLQNL DFIESIIPYH DTELSDDLHK LISISKSKIL EAPKQYELYN LSNLTNNPKQ
SLYFAFLQNY IKWLIPFSFF GLSIRFLSNF TYEFNSTYSL FAILWTLSFT AFWLYKYEPF
WSDRLSKYSS FSTIEFLQDK QKAQKKASSV IMLKKCCFIP VALLFGAILL SFQLYCFALE
IFIKQIYNGP MISILSFLPT ILICTFTPVL TVIYNKYFVE PMTKWENHSS VVNAKKSKEA
KNFVIIFLSS YVPLLITLFL YLPMGHLLTA EIRTKVFNAF SILARLPTHD SDFIIDTKRY
EDQFFYFIVI NQLIQFSMEN FVPSLVSIAQ QKINGPNPNF VKAESEIGKA QLSSSDMKIW
SKVKSYQTDP WGATFDLDAN FKKLLLQFGY LVMFSTIWPL APFICLIVNL IVYQVDLRKA
VLYSKPEYFP FPIYDKPSSV SNTQKLTVGL WNSVLVMFSI LGCVITATLT YMYQSCNIPG
VGAHTSIHTN KAWYLANPIN HSWINIVLYA VFIEHVSVAI FFLFSSILKS SHDDVANGIV
PKHVVNVQNP PKQEVFEKIP SPEFNSNNEK ELVQRKGSAN EKLHQELGEK QPASSANGYE
AHAATHANND PSSLSSASSP SLSSSSSSSK TGVVKAVDND TAGSAGKKPL ATESTEKRNS
LVKVPTVGSY GVAGATLPET IPTSKNYYLR FDEDGKSIRD AKSSAESSNA TNNNTLGTES
KLLPDGDAVD ALSRKIDQIP KIAVTGGENN ENTQAKDDAA TKTPLIKDAN IKPVVNAAVN
DNQSKVSVAT EQTKKTEVST KNGPSRSIST KETKDSARPS NNNTTTTTTT DATQPHHHHH
HHRHRDAGVK NVTNNSKTTE SSSSSSAAKE KPKHKKGLLH KLKKKL
