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   27-MAR-2024, entry version 173.
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.
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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; 228.
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; 4932-YBR086C; -.
DR   PeptideAtlas; P38250; -.
DR   EnsemblFungi; YBR086C_mRNA; YBR086C; YBR086C.
DR   GeneID; 852382; -.
DR   KEGG; sce:YBR086C; -.
DR   AGR; SGD:S000000290; -.
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   OrthoDB; 49329at2759; -.
DR   BioCyc; YEAST:G3O-29053-MONOMER; -.
DR   Reactome; R-SCE-2672351; Stimuli-sensing channels.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 852382; 6 hits in 10 CRISPR screens.
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: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   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR049452; Anoctamin_TM.
DR   PANTHER; PTHR12308; ANOCTAMIN; 1.
DR   PANTHER; PTHR12308:SF73; INCREASED SODIUM TOLERANCE PROTEIN 2; 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;
FT                   CAA85034/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
//