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Protein

Sporulation-specific protein 20

Gene

SPO20

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 to maintain the prospore membrane to the nucleus during sporulation in order to capture the daughter nuclei and form the spores. Mediates the fusion of exocytic vesicles with the plasma membrane during sporulation through its interactions with the t-SNARE SSO1 and v-SNARE SNC2.3 Publications

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • syntaxin binding Source: GO_Central

GO - Biological processi

  • ascospore-type prospore assembly Source: SGD
  • exocytosis Source: GO_Central
  • vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32723-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation-specific protein 20
Gene namesi
Name:SPO20
Ordered Locus Names:YMR017W
ORF Names:YM9711.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR017W.
SGDiS000004619. SPO20.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: GO_Central
  • prospore membrane Source: SGD
  • SNARE complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661K → E: Strong decrease of the sporulation rate and loss of lipid binding; when associated with E-68; E-71 and E-73. 1 Publication
Mutagenesisi67 – 671L → P or N: Strong decrease of the sporulation rate. 1 Publication
Mutagenesisi68 – 681K → E: Strong decrease of the sporulation rate and loss of lipid binding; when associated with E-66; E-71 and E-73. 1 Publication
Mutagenesisi70 – 701L → N: Strong decrease of the sporulation rate. 1 Publication
Mutagenesisi71 – 711R → E: Strong decrease of the sporulation rate and loss of lipid binding; when associated with E-66; E-68 and E-73. 1 Publication
Mutagenesisi73 – 731K → E: Strong decrease of the sporulation rate and loss of lipid binding; when associated with E-66; E-68 and E-71. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Sporulation-specific protein 20PRO_0000213614Add
BLAST

Interactioni

Subunit structurei

Interacts with the t-SNARE SSO1 and the v-SNARE SNC2.1 Publication

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

BioGridi35188. 17 interactions.
DIPiDIP-4511N.
IntActiQ04359. 1 interaction.
MINTiMINT-538495.

Structurei

3D structure databases

ProteinModelPortaliQ04359.
SMRiQ04359. Positions 178-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini330 – 39263t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 5047Inhibitory regionAdd
BLAST
Regioni51 – 9545Positive regulatory regionAdd
BLAST

Domaini

The inhibitory region sequesters the protein in the nucleus.
The positive regulatory region is essential and contains an amphipathic helix with hydrophobic and positive charged faces involved in the localization of the protein to the membranes through its binding to phospholipids.

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00530000067410.
InParanoidiQ04359.
OrthoDBiEOG7S227Z.

Family and domain databases

InterProiIPR000727. T_SNARE_dom.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFRKILASK SHHSRHHNQH HKNLKLQNHR YVLISNITGS HETKYLSPFR
60 70 80 90 100
MDNCSGSRRR DRLHVKLKSL RNKIHKQLHP NCRFDDATKT SDDKCVSYEV
110 120 130 140 150
PERDGLATIS LEEVFPKSNR CQIPEENLGE TDSVIHRDLG NFANENDYPQ
160 170 180 190 200
WRKVESQYNL ENVQPEEDEI VDRLRSEIRS TKLKSVKTTS RTLEKAIEAR
210 220 230 240 250
CTGKRVLQQL SCQSNQLTKI ESNCDMLKIQ SNVADRKIDE LAHENRSLLA
260 270 280 290 300
LKSPNPFRKK REREKRDQIY NLKLKHRHLQ QETMKRAQDS DKNLAINLSS
310 320 330 340 350
EYGRYGQGVE RQRILRDAQK YQFEADEEDN QMEIDLYGNL EQIKAVSGDL
360 370 380 390
KIMAHAFGRE FEAQNTRMFD IENNVQQADN ALQAKRYRLE KVIGKRW
Length:397
Mass (Da):46,621
Last modified:November 1, 1997 - v1
Checksum:iCFE6769B82725B49
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591R → K in AAT92904 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49211 Genomic DNA. Translation: CAA89119.1.
AY692885 Genomic DNA. Translation: AAT92904.1.
BK006946 Genomic DNA. Translation: DAA09915.1.
PIRiS54018.
RefSeqiNP_013730.1. NM_001182513.1.

Genome annotation databases

EnsemblFungiiYMR017W; YMR017W; YMR017W.
GeneIDi855031.
KEGGisce:YMR017W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49211 Genomic DNA. Translation: CAA89119.1.
AY692885 Genomic DNA. Translation: AAT92904.1.
BK006946 Genomic DNA. Translation: DAA09915.1.
PIRiS54018.
RefSeqiNP_013730.1. NM_001182513.1.

3D structure databases

ProteinModelPortaliQ04359.
SMRiQ04359. Positions 178-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35188. 17 interactions.
DIPiDIP-4511N.
IntActiQ04359. 1 interaction.
MINTiMINT-538495.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR017W; YMR017W; YMR017W.
GeneIDi855031.
KEGGisce:YMR017W.

Organism-specific databases

EuPathDBiFungiDB:YMR017W.
SGDiS000004619. SPO20.

Phylogenomic databases

GeneTreeiENSGT00530000067410.
InParanoidiQ04359.
OrthoDBiEOG7S227Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-32723-MONOMER.

Miscellaneous databases

PROiQ04359.

Family and domain databases

InterProiIPR000727. T_SNARE_dom.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "A conserved domain is present in different families of vesicular fusion proteins: a new superfamily."
    Weimbs T., Low S.H., Chapin S.J., Mostov K.E., Bucher P., Hofmann K.
    Proc. Natl. Acad. Sci. U.S.A. 94:3046-3051(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  5. "Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast."
    Neiman A.M.
    J. Cell Biol. 140:29-37(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae."
    Neiman A.M., Katz L., Brennwald P.J.
    Genetics 155:1643-1655(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SSO1 AND SNC2.
  7. "Positive and negative regulation of a SNARE protein by control of intracellular localization."
    Nakanishi H., de los Santos P., Neiman A.M.
    Mol. Biol. Cell 15:1802-1815(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAINS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-66; LEU-67; LYS-68; LEU-70; ARG-71 AND LYS-73.

Entry informationi

Entry nameiSPO20_YEAST
AccessioniPrimary (citable) accession number: Q04359
Secondary accession number(s): D6VZJ1, Q6B245
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 126 of the entry and version 1 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.