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Protein

Sulfite efflux pump SSU1

Gene

SSU1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in efflux of free sulfite. Mutations in the SSU1 gene cause sensitivity to sulfite.2 Publications

GO - Molecular functioni

  • sulfite transmembrane transporter activity Source: SGD

GO - Biological processi

  • sulfite transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33996-MONOMER.

Protein family/group databases

TCDBi2.A.16.3.1. the telurite-resistance/dicarboxylate transporter (tdt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite efflux pump SSU1
Alternative name(s):
Sulfite sensitivity protein SSU1
Gene namesi
Name:SSU1
Ordered Locus Names:YPL092W
ORF Names:LPG16W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL092W.
SGDiS000006013. SSU1.

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 3221HelicalSequence analysisAdd
BLAST
Topological domaini33 – 4816ExtracellularSequence analysisAdd
BLAST
Transmembranei49 – 6921HelicalSequence analysisAdd
BLAST
Topological domaini70 – 8920CytoplasmicSequence analysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 13525ExtracellularSequence analysisAdd
BLAST
Transmembranei136 – 15621HelicalSequence analysisAdd
BLAST
Topological domaini157 – 17620CytoplasmicSequence analysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence analysisAdd
BLAST
Topological domaini198 – 22023ExtracellularSequence analysisAdd
BLAST
Transmembranei221 – 24121HelicalSequence analysisAdd
BLAST
Topological domaini242 – 25211CytoplasmicSequence analysisAdd
BLAST
Transmembranei253 – 27523HelicalSequence analysisAdd
BLAST
Topological domaini276 – 30934ExtracellularSequence analysisAdd
BLAST
Transmembranei310 – 33021HelicalSequence analysisAdd
BLAST
Topological domaini331 – 35020CytoplasmicSequence analysisAdd
BLAST
Transmembranei351 – 37121HelicalSequence analysisAdd
BLAST
Topological domaini372 – 38716ExtracellularSequence analysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence analysisAdd
BLAST
Topological domaini409 – 45850CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Sulfite efflux pump SSU1PRO_0000072229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei444 – 4441PhosphoserineCombined sources
Modified residuei448 – 4481PhosphoserineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP41930.

Interactioni

Protein-protein interaction databases

BioGridi36089. 12 interactions.
DIPiDIP-5056N.
IntActiP41930. 1 interaction.
MINTiMINT-493602.

Structurei

3D structure databases

ProteinModelPortaliP41930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiP41930.
OMAiFPMGTMS.
OrthoDBiEOG744TK6.

Family and domain databases

InterProiIPR004695. Voltage-dep_anion_channel.
[Graphical view]
PfamiPF03595. SLAC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVANWVLALT RQFDPFMFMM VMGVGISSNI LYSFPYPARW LRICSYIMFA
60 70 80 90 100
IACLIFIAVQ ALQILHLIVY IKEKSFREYF NDFFRNMKHN LFWGTYPMGL
110 120 130 140 150
VTIINFLGAL SKANTTKSPT NARNLMIFVY VLWWYDLAVC LVIAWGISFL
160 170 180 190 200
IWHDYYPLEG IGNYPSYNIK MASENMKSVL LLDIIPLVVV ASSCGTFTMS
210 220 230 240 250
EIFFHAFNRN IQLITLVICA LTWLHAIIFV FILIAIYFWS LYINKIPPMT
260 270 280 290 300
QVFTLFLLLG PMGQGSFGVL LLTDNIKKYA GKYYPTDNIT REQEILTIAV
310 320 330 340 350
PWCFKILGMV SAMALLAMGY FFTVISVVSI LSYYNKKEIE NETGKVKRVY
360 370 380 390 400
TFHKGFWGMT FPMGTMSLGN EELYVQYNQY VPLYAFRVLG TIYGGVCVCW
410 420 430 440 450
SILCLLCTLH EYSKKMLHAA RKSSLFSESG TEKTTVSPYN SIESVEESNS

ALDFTRLA
Length:458
Mass (Da):52,545
Last modified:May 1, 2007 - v5
Checksum:iFF55440526AA6E73
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191M → V in strain: Ba194, CECT 10233, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMW1-12, ORM1-1, Sgu52E, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610.
Natural varianti52 – 521A → T in strain: ATCC 76625 / YPH499, Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, MMW1-12, ORM1-1, S288c/ YPH1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610.
Natural varianti90 – 901N → S in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-5, MMW1-15h2, MMW1-2h2, Sgu52E, Sgu52F and Y-9.
Natural varianti122 – 1221A → S in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-15h2, MMW1-2h2 and Sgu52F.
Natural varianti157 – 1571P → S in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15h2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610.
Natural varianti164 – 1641Y → H in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-15h2, MMW1-2h2 and Sgu52F.
Natural varianti191 – 1911A → T in strain: ATCC 76625 / YPH499,MMW1-15, MMW1-2 and S288c / YPH1.
Natural varianti344 – 3441G → E in strain: Sgu52F.
Natural varianti345 – 3451K → R in strain: ATCC 76625 / YPH499, MMW1-15 and MMW1-2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20254 Genomic DNA. Translation: AAC49577.1.
AB002531 Genomic DNA. Translation: BAA19568.1.
AY949949 Genomic DNA. Translation: AAY27351.1.
AY949950 Genomic DNA. Translation: AAY27352.1.
AY949951 Genomic DNA. Translation: AAY27353.1.
AY949952 Genomic DNA. Translation: AAY27354.1.
AY949953 Genomic DNA. Translation: AAY27355.1.
AY949954 Genomic DNA. Translation: AAY27356.1.
AY949955 Genomic DNA. Translation: AAY27357.1.
AY949956 Genomic DNA. Translation: AAY27358.1.
AY949957 Genomic DNA. Translation: AAY27359.1.
AY949958 Genomic DNA. Translation: AAY27360.1.
AY949959 Genomic DNA. Translation: AAY27361.1.
AY949960 Genomic DNA. Translation: AAY27362.1.
AY949961 Genomic DNA. Translation: AAY27363.1.
AY949962 Genomic DNA. Translation: AAY27364.1.
AY949963 Genomic DNA. Translation: AAY27365.1.
AY949964 Genomic DNA. Translation: AAY27366.1.
AY949965 Genomic DNA. Translation: AAY27367.1.
AY949966 Genomic DNA. Translation: AAY27368.1.
AY949967 Genomic DNA. Translation: AAY27369.1.
AY949968 Genomic DNA. Translation: AAY27370.1.
AY949969 Genomic DNA. Translation: AAY27371.1.
AY949970 Genomic DNA. Translation: AAY27372.1.
AY949971 Genomic DNA. Translation: AAY27373.1.
AY949972 Genomic DNA. Translation: AAY27374.1.
AY949973 Genomic DNA. Translation: AAY27375.1.
AY949974 Genomic DNA. Translation: AAY27376.1.
AY949975 Genomic DNA. Translation: AAY27377.1.
AY949976 Genomic DNA. Translation: AAY27378.1.
AY949977 Genomic DNA. Translation: AAY27379.1.
U43281 Genomic DNA. Translation: AAB68207.1.
AY693225 Genomic DNA. Translation: AAT93244.1.
AJ458365 Genomic DNA. Translation: CAD30223.1.
AJ458367 Genomic DNA. Translation: CAD30225.1.
BK006949 Genomic DNA. Translation: DAA11341.1.
PIRiS61974.
RefSeqiNP_015233.1. NM_001183906.1.

Genome annotation databases

EnsemblFungiiYPL092W; YPL092W; YPL092W.
GeneIDi856013.
KEGGisce:YPL092W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20254 Genomic DNA. Translation: AAC49577.1.
AB002531 Genomic DNA. Translation: BAA19568.1.
AY949949 Genomic DNA. Translation: AAY27351.1.
AY949950 Genomic DNA. Translation: AAY27352.1.
AY949951 Genomic DNA. Translation: AAY27353.1.
AY949952 Genomic DNA. Translation: AAY27354.1.
AY949953 Genomic DNA. Translation: AAY27355.1.
AY949954 Genomic DNA. Translation: AAY27356.1.
AY949955 Genomic DNA. Translation: AAY27357.1.
AY949956 Genomic DNA. Translation: AAY27358.1.
AY949957 Genomic DNA. Translation: AAY27359.1.
AY949958 Genomic DNA. Translation: AAY27360.1.
AY949959 Genomic DNA. Translation: AAY27361.1.
AY949960 Genomic DNA. Translation: AAY27362.1.
AY949961 Genomic DNA. Translation: AAY27363.1.
AY949962 Genomic DNA. Translation: AAY27364.1.
AY949963 Genomic DNA. Translation: AAY27365.1.
AY949964 Genomic DNA. Translation: AAY27366.1.
AY949965 Genomic DNA. Translation: AAY27367.1.
AY949966 Genomic DNA. Translation: AAY27368.1.
AY949967 Genomic DNA. Translation: AAY27369.1.
AY949968 Genomic DNA. Translation: AAY27370.1.
AY949969 Genomic DNA. Translation: AAY27371.1.
AY949970 Genomic DNA. Translation: AAY27372.1.
AY949971 Genomic DNA. Translation: AAY27373.1.
AY949972 Genomic DNA. Translation: AAY27374.1.
AY949973 Genomic DNA. Translation: AAY27375.1.
AY949974 Genomic DNA. Translation: AAY27376.1.
AY949975 Genomic DNA. Translation: AAY27377.1.
AY949976 Genomic DNA. Translation: AAY27378.1.
AY949977 Genomic DNA. Translation: AAY27379.1.
U43281 Genomic DNA. Translation: AAB68207.1.
AY693225 Genomic DNA. Translation: AAT93244.1.
AJ458365 Genomic DNA. Translation: CAD30223.1.
AJ458367 Genomic DNA. Translation: CAD30225.1.
BK006949 Genomic DNA. Translation: DAA11341.1.
PIRiS61974.
RefSeqiNP_015233.1. NM_001183906.1.

3D structure databases

ProteinModelPortaliP41930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36089. 12 interactions.
DIPiDIP-5056N.
IntActiP41930. 1 interaction.
MINTiMINT-493602.

Protein family/group databases

TCDBi2.A.16.3.1. the telurite-resistance/dicarboxylate transporter (tdt) family.

PTM databases

iPTMnetiP41930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL092W; YPL092W; YPL092W.
GeneIDi856013.
KEGGisce:YPL092W.

Organism-specific databases

EuPathDBiFungiDB:YPL092W.
SGDiS000006013. SSU1.

Phylogenomic databases

InParanoidiP41930.
OMAiFPMGTMS.
OrthoDBiEOG744TK6.

Enzyme and pathway databases

BioCyciYEAST:G3O-33996-MONOMER.

Miscellaneous databases

NextBioi980905.
PROiP41930.

Family and domain databases

InterProiIPR004695. Voltage-dep_anion_channel.
[Graphical view]
PfamiPF03595. SLAC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SSU1 encodes a plasma membrane protein with a central role in a network of proteins conferring sulfite tolerance in Saccharomyces cerevisiae."
    Avram D., Bakalinsky A.T.
    J. Bacteriol. 179:5971-5974(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, NULL MUTANT.
    Strain: S288c / YPH1.
  2. "SSU1-R, a sulfite resistance gene of wine yeast, is an allele of SSU1 with a different upstream sequence."
    Goto-Yamamoto N., Kitano K., Shiki K., Yoshida Y., Suzuki T., Iwata T., Yamane Y., Hara S.
    J. Ferment. Bioeng. 86:427-433(1998)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Y-9.
  3. "Population structure and gene evolution in Saccharomyces cerevisiae."
    Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.
    FEMS Yeast Res. 6:702-715(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "Molecular characterization of a chromosomal rearrangement involved in the adaptive evolution of yeast strains."
    Perez-Ortin J.E., Querol A., Puig S., Barrio E.
    Genome Res. 12:1533-1539(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (STRAIN CECT 10233), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 (STRAIN CECT 1485).
    Strain: CECT 10233 and CECT 1485.
  8. "Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae."
    Xu X., Wightman J.D., Geller B.L., Avram D., Bakalinsky A.T.
    Curr. Genet. 25:488-496(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "SSU1 mediates sulphite efflux in Saccharomyces cerevisiae."
    Park H., Bakalinsky A.T.
    Yeast 16:881-888(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-448 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-448 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSU1_YEAST
AccessioniPrimary (citable) accession number: P41930
Secondary accession number(s): D6W3S5
, P87026, Q02893, Q2VQ61, Q2VQ65, Q2VQ70, Q2VQ74, Q2VQ76, Q2VQ77, Q8J1R0, Q8J1R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 1, 2007
Last modified: May 11, 2016
This is version 115 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.