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Protein

Protein SSO1

Gene

SSO1

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

Functioni

Required for vesicle fusion with the plasma membrane.

GO - Molecular functioni

  • phosphatidic acid binding Source: SGD
  • phosphatidylinositol-3,4-bisphosphate binding Source: SGD
  • phosphatidylinositol-3,5-bisphosphate binding Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • SNAP receptor activity Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • ascospore-type prospore assembly Source: SGD
  • intracellular protein transport Source: InterPro
  • vesicle fusion Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-34119-MONOMER.
ReactomeiR-SCE-114516. Disinhibition of SNARE formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SSO1
Gene namesi
Name:SSO1
Ordered Locus Names:YPL232W
ORF Names:P1405
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL232W.
SGDiS000006153. SSO1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 265265CytoplasmicSequence analysisAdd
BLAST
Transmembranei266 – 28722Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini288 – 2903ExtracellularSequence analysis

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
  • prospore membrane Source: SGD
  • SNARE complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Protein SSO1PRO_0000210274Add
BLAST

Proteomic databases

MaxQBiP32867.
PeptideAtlasiP32867.

PTM databases

iPTMnetiP32867.
SwissPalmiP32867.

Interactioni

GO - Molecular functioni

  • SNAP receptor activity Source: SGD

Protein-protein interaction databases

BioGridi35930. 89 interactions.
DIPiDIP-2494N.
IntActiP32867. 2 interactions.
MINTiMINT-4505526.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 6434Combined sources
Helixi70 – 10435Combined sources
Turni105 – 1073Combined sources
Helixi109 – 15143Combined sources
Helixi157 – 1637Combined sources
Helixi166 – 17611Combined sources
Helixi190 – 25667Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIOX-ray2.10A31-225[»]
3B5NX-ray1.60B/F/J189-257[»]
ProteinModelPortaliP32867.
SMRiP32867. Positions 31-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32867.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 25263t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119200.
HOGENOMiHOG000246774.
InParanoidiP32867.
KOiK08486.
OMAiQAKRQYM.
OrthoDBiEOG7X6MB5.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYNNPYQLE TPFEESYELD EGSSAIGAEG HDFVGFMNKI SQINRDLDKY
60 70 80 90 100
DHTINQVDSL HKRLLTEVNE EQASHLRHSL DNFVAQATDL QFKLKNEIKS
110 120 130 140 150
AQRDGIHDTN KQAQAENSRQ RFLKLIQDYR IVDSNYKEEN KEQAKRQYMI
160 170 180 190 200
IQPEATEDEV EAAISDVGGQ QIFSQALLNA NRRGEAKTAL AEVQARHQEL
210 220 230 240 250
LKLEKSMAEL TQLFNDMEEL VIEQQENVDV IDKNVEDAQL DVEQGVGHTD
260 270 280 290
KAVKSARKAR KNKIRCWLIV FAIIVVVVVV VVVPAVVKTR
Length:290
Mass (Da):33,106
Last modified:February 1, 1995 - v2
Checksum:i6E4C6D35C3CD9D94
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971E → G no nucleotide entry (PubMed:2900835).Curated
Sequence conflicti105 – 1051G → V no nucleotide entry (PubMed:2900835).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67729 mRNA. Translation: CAA47959.1.
X76890 Genomic DNA. Translation: CAA54217.1.
X94561 Genomic DNA. Translation: CAA64255.1.
Z73588 Genomic DNA. Translation: CAA97949.1.
J03936 Genomic DNA. No translation available.
BK006949 Genomic DNA. Translation: DAA11204.1.
PIRiS39569.
RefSeqiNP_015092.1. NM_001184046.1.

Genome annotation databases

EnsemblFungiiYPL232W; YPL232W; YPL232W.
GeneIDi855844.
KEGGisce:YPL232W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67729 mRNA. Translation: CAA47959.1.
X76890 Genomic DNA. Translation: CAA54217.1.
X94561 Genomic DNA. Translation: CAA64255.1.
Z73588 Genomic DNA. Translation: CAA97949.1.
J03936 Genomic DNA. No translation available.
BK006949 Genomic DNA. Translation: DAA11204.1.
PIRiS39569.
RefSeqiNP_015092.1. NM_001184046.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIOX-ray2.10A31-225[»]
3B5NX-ray1.60B/F/J189-257[»]
ProteinModelPortaliP32867.
SMRiP32867. Positions 31-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35930. 89 interactions.
DIPiDIP-2494N.
IntActiP32867. 2 interactions.
MINTiMINT-4505526.

PTM databases

iPTMnetiP32867.
SwissPalmiP32867.

Proteomic databases

MaxQBiP32867.
PeptideAtlasiP32867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL232W; YPL232W; YPL232W.
GeneIDi855844.
KEGGisce:YPL232W.

Organism-specific databases

EuPathDBiFungiDB:YPL232W.
SGDiS000006153. SSO1.

Phylogenomic databases

GeneTreeiENSGT00760000119200.
HOGENOMiHOG000246774.
InParanoidiP32867.
KOiK08486.
OMAiQAKRQYM.
OrthoDBiEOG7X6MB5.

Enzyme and pathway databases

BioCyciYEAST:G3O-34119-MONOMER.
ReactomeiR-SCE-114516. Disinhibition of SNARE formation.

Miscellaneous databases

EvolutionaryTraceiP32867.
PROiP32867.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport."
    Aalto M.K., Ronne H., Keraenen S.
    EMBO J. 12:4095-4104(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 26787 / X2180-1B.
  2. Schueller H.-J.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence."
    Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.
    J. Biol. Chem. 263:12315-12325(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSO1_YEAST
AccessioniPrimary (citable) accession number: P32867
Secondary accession number(s): D6W3D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 450 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. 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.