SSU1_YEAST
ID SSU1_YEAST Reviewed; 458 AA.
AC P41930; D6W3S5; P87026; Q02893; Q2VQ61; Q2VQ65; Q2VQ70; Q2VQ74; Q2VQ76;
AC Q2VQ77; Q8J1R0; Q8J1R1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 5.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Sulfite efflux pump SSU1;
DE AltName: Full=Sulfite sensitivity protein SSU1;
GN Name=SSU1; OrderedLocusNames=YPL092W; ORFNames=LPG16W;
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], SUBCELLULAR LOCATION, AND NULL MUTANT.
RC STRAIN=S288c / YPH1;
RX PubMed=9294463; DOI=10.1128/jb.179.18.5971-5974.1997;
RA Avram D., Bakalinsky A.T.;
RT "SSU1 encodes a plasma membrane protein with a central role in a network of
RT proteins conferring sulfite tolerance in Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:5971-5974(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y-9;
RA Goto-Yamamoto N., Kitano K., Shiki K., Yoshida Y., Suzuki T., Iwata T.,
RA Yamane Y., Hara S.;
RT "SSU1-R, a sulfite resistance gene of wine yeast, is an allele of SSU1 with
RT a different upstream sequence.";
RL J. Ferment. Bioeng. 86:427-433(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A, M5-7B,
RC M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2, MMW1-2,
RC MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598, YPS600, YPS602,
RC YPS604, YPS606, YPS608, and YPS610;
RX PubMed=16879422; DOI=10.1111/j.1567-1364.2006.00059.x;
RA Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.;
RT "Population structure and gene evolution in Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 6:702-715(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (STRAIN CECT 10233), AND
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 (STRAIN CECT 1485).
RC STRAIN=CECT 10233, and CECT 1485;
RX PubMed=12368245; DOI=10.1101/gr.436602;
RA Perez-Ortin J.E., Querol A., Puig S., Barrio E.;
RT "Molecular characterization of a chromosomal rearrangement involved in the
RT adaptive evolution of yeast strains.";
RL Genome Res. 12:1533-1539(2002).
RN [8]
RP FUNCTION.
RX PubMed=8082198; DOI=10.1007/bf00351667;
RA Xu X., Wightman J.D., Geller B.L., Avram D., Bakalinsky A.T.;
RT "Isolation and characterization of sulfite mutants of Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 25:488-496(1994).
RN [9]
RP FUNCTION.
RX PubMed=10870099;
RX DOI=10.1002/1097-0061(200007)16:10<881::aid-yea576>3.0.co;2-3;
RA Park H., Bakalinsky A.T.;
RT "SSU1 mediates sulphite efflux in Saccharomyces cerevisiae.";
RL Yeast 16:881-888(2000).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-448 AND SER-450, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-448 AND SER-450, 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: Involved in efflux of free sulfite. Mutations in the SSU1
CC gene cause sensitivity to sulfite. {ECO:0000269|PubMed:10870099,
CC ECO:0000269|PubMed:8082198}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9294463};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9294463}.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000305}.
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DR EMBL; U20254; AAC49577.1; -; Genomic_DNA.
DR EMBL; AB002531; BAA19568.1; -; Genomic_DNA.
DR EMBL; AY949949; AAY27351.1; -; Genomic_DNA.
DR EMBL; AY949950; AAY27352.1; -; Genomic_DNA.
DR EMBL; AY949951; AAY27353.1; -; Genomic_DNA.
DR EMBL; AY949952; AAY27354.1; -; Genomic_DNA.
DR EMBL; AY949953; AAY27355.1; -; Genomic_DNA.
DR EMBL; AY949954; AAY27356.1; -; Genomic_DNA.
DR EMBL; AY949955; AAY27357.1; -; Genomic_DNA.
DR EMBL; AY949956; AAY27358.1; -; Genomic_DNA.
DR EMBL; AY949957; AAY27359.1; -; Genomic_DNA.
DR EMBL; AY949958; AAY27360.1; -; Genomic_DNA.
DR EMBL; AY949959; AAY27361.1; -; Genomic_DNA.
DR EMBL; AY949960; AAY27362.1; -; Genomic_DNA.
DR EMBL; AY949961; AAY27363.1; -; Genomic_DNA.
DR EMBL; AY949962; AAY27364.1; -; Genomic_DNA.
DR EMBL; AY949963; AAY27365.1; -; Genomic_DNA.
DR EMBL; AY949964; AAY27366.1; -; Genomic_DNA.
DR EMBL; AY949965; AAY27367.1; -; Genomic_DNA.
DR EMBL; AY949966; AAY27368.1; -; Genomic_DNA.
DR EMBL; AY949967; AAY27369.1; -; Genomic_DNA.
DR EMBL; AY949968; AAY27370.1; -; Genomic_DNA.
DR EMBL; AY949969; AAY27371.1; -; Genomic_DNA.
DR EMBL; AY949970; AAY27372.1; -; Genomic_DNA.
DR EMBL; AY949971; AAY27373.1; -; Genomic_DNA.
DR EMBL; AY949972; AAY27374.1; -; Genomic_DNA.
DR EMBL; AY949973; AAY27375.1; -; Genomic_DNA.
DR EMBL; AY949974; AAY27376.1; -; Genomic_DNA.
DR EMBL; AY949975; AAY27377.1; -; Genomic_DNA.
DR EMBL; AY949976; AAY27378.1; -; Genomic_DNA.
DR EMBL; AY949977; AAY27379.1; -; Genomic_DNA.
DR EMBL; U43281; AAB68207.1; -; Genomic_DNA.
DR EMBL; AY693225; AAT93244.1; -; Genomic_DNA.
DR EMBL; AJ458365; CAD30223.1; -; Genomic_DNA.
DR EMBL; AJ458367; CAD30225.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11341.1; -; Genomic_DNA.
DR PIR; S61974; S61974.
DR RefSeq; NP_015233.1; NM_001183906.1.
DR AlphaFoldDB; P41930; -.
DR BioGRID; 36089; 40.
DR DIP; DIP-5056N; -.
DR IntAct; P41930; 1.
DR MINT; P41930; -.
DR STRING; 4932.YPL092W; -.
DR TCDB; 2.A.16.3.1; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR iPTMnet; P41930; -.
DR PaxDb; P41930; -.
DR PRIDE; P41930; -.
DR DNASU; 856013; -.
DR EnsemblFungi; YPL092W_mRNA; YPL092W; YPL092W.
DR GeneID; 856013; -.
DR KEGG; sce:YPL092W; -.
DR SGD; S000006013; SSU1.
DR VEuPathDB; FungiDB:YPL092W; -.
DR eggNOG; ENOG502QT02; Eukaryota.
DR HOGENOM; CLU_030057_6_2_1; -.
DR InParanoid; P41930; -.
DR OMA; PVQSMFI; -.
DR BioCyc; YEAST:G3O-33996-MON; -.
DR PRO; PR:P41930; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P41930; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0000319; F:sulfite transmembrane transporter activity; IDA:SGD.
DR GO; GO:0000316; P:sulfite transport; IDA:SGD.
DR Gene3D; 1.50.10.150; -; 1.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR Pfam; PF03595; SLAC1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..458
FT /note="Sulfite efflux pump SSU1"
FT /id="PRO_0000072229"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 19
FT /note="M -> V (in strain: Ba194, CECT 10233, M5-7A, M5-7B,
FT M7-8D, MMR2-1, MMR2-3, MMW1-12, ORM1-1, Sgu52E, Y-9,
FT YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606,
FT YPS608 and YPS610)"
FT VARIANT 52
FT /note="A -> T (in strain: ATCC 76625 / YPH499, Ba194, Bb32,
FT M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5,
FT MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, MMW1-12, ORM1-1,
FT S288c/ YPH1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400, YPS598,
FT YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610)"
FT VARIANT 90
FT /note="N -> S (in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A,
FT M5-7B, M7-8D, MMR2-5, MMW1-15h2, MMW1-2h2, Sgu52E, Sgu52F
FT and Y-9)"
FT VARIANT 122
FT /note="A -> S (in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-
FT 15h2, MMW1-2h2 and Sgu52F)"
FT VARIANT 157
FT /note="P -> S (in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A,
FT M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15h2,
FT MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400,
FT YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610)"
FT VARIANT 164
FT /note="Y -> H (in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-
FT 15h2, MMW1-2h2 and Sgu52F)"
FT VARIANT 191
FT /note="A -> T (in strain: ATCC 76625 / YPH499,MMW1-15,
FT MMW1-2 and S288c / YPH1)"
FT VARIANT 344
FT /note="G -> E (in strain: Sgu52F)"
FT VARIANT 345
FT /note="K -> R (in strain: ATCC 76625 / YPH499, MMW1-15 and
FT MMW1-2)"
SQ SEQUENCE 458 AA; 52545 MW; FF55440526AA6E73 CRC64;
MVANWVLALT RQFDPFMFMM VMGVGISSNI LYSFPYPARW LRICSYIMFA IACLIFIAVQ
ALQILHLIVY IKEKSFREYF NDFFRNMKHN LFWGTYPMGL VTIINFLGAL SKANTTKSPT
NARNLMIFVY VLWWYDLAVC LVIAWGISFL IWHDYYPLEG IGNYPSYNIK MASENMKSVL
LLDIIPLVVV ASSCGTFTMS EIFFHAFNRN IQLITLVICA LTWLHAIIFV FILIAIYFWS
LYINKIPPMT QVFTLFLLLG PMGQGSFGVL LLTDNIKKYA GKYYPTDNIT REQEILTIAV
PWCFKILGMV SAMALLAMGY FFTVISVVSI LSYYNKKEIE NETGKVKRVY TFHKGFWGMT
FPMGTMSLGN EELYVQYNQY VPLYAFRVLG TIYGGVCVCW SILCLLCTLH EYSKKMLHAA
RKSSLFSESG TEKTTVSPYN SIESVEESNS ALDFTRLA
