Reviewed,
UniProtKB/Swiss-Prot P32602 (SEC17_YEAST)
Last modified
November 24, 2009.
Version 92.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alpha-soluble NSF attachment protein Short name=SNAP-alpha Alternative name(s): N-ethylmaleimide-sensitive factor attachment protein alpha alpha-SNAP chaperone Vesicular-fusion protein SEC17 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 292 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactions in trans during docking and fusion steps. Can displace HOPS from SNARE complexes, which may be a prerequisite for trans-SNARE complex dissassembly and subsequent rounds of priming, docking and fusion. Ref.5 Ref.6 Ref.7 Ref.8 |
| Subunit structure | Binds to vacuolar cis-SNARE complexes composed of the v-SNAREs NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7. Interacts with SEC18. Ref.8 |
| Subcellular location | |
| Sequence similarities | Belongs to the SNAP family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GOS1 | P38736 | 1 | EBI-16558,EBI-24365 | |
| SEC22 | P22214 | 1 | EBI-16558,EBI-16577 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.4 | ||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 292 | 291 | Alpha-soluble NSF attachment protein | PRO_0000219076 | |||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.4 | ||||||||||||||||||||||||||||||||||||||||
| Modified residue | 182 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 103 | 1 | A → P in AAA35029. Ref.1 | ||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 219 | 1 | Missing in AAA35029. Ref.1 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 14 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 21 – 25 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 30 – 49 | 20 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 54 – 69 | 16 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 73 – 89 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 109 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 113 – 129 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 134 – 150 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 154 – 170 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 174 – 186 | 13 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 192 – 194 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 195 – 197 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 198 – 211 | 14 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 215 – 223 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 224 – 226 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 238 – 249 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 253 – 255 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 256 – 263 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 271 – 288 | 18 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein." Griff I.C., Schekman R., Rothman J.E., Kaiser C.A. J. Biol. Chem. 267:12106-12115(1992) [PubMed: 1601878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes." Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F. Yeast 9:1355-1371(1993) [PubMed: 8154187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K.EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | Bienvenut W.V., Peters C. Submitted (MAY-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 52-62; 89-110 AND 121-136, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. |
| [5] | "Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles." Mayer A., Wickner W., Haas A. Cell 85:83-94(1996) [PubMed: 8620540] [Abstract] Cited for: FUNCTION. |
| [6] | "Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)." Haas A., Wickner W. EMBO J. 15:3296-3305(1996) [PubMed: 8670830] [Abstract] Cited for: FUNCTION. |
| [7] | "Homotypic vacuolar fusion mediated by t- and v-SNAREs." Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A. Nature 387:199-202(1997) [PubMed: 9144293] [Abstract] Cited for: FUNCTION. |
| [8] | "Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion." Collins K.M., Thorngren N.L., Fratti R.A., Wickner W.T. EMBO J. 24:1775-1786(2005) [PubMed: 15889152] [Abstract] Cited for: FUNCTION, INTERACTION WITH CIS-SNARE COMPLEX. |
| [9] | "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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, MASS SPECTROMETRY. |
| [10] | "Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly." Rice L.M., Brunger A.T. Mol. Cell 4:85-95(1999) [PubMed: 10445030] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-292. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M93104 Genomic DNA. Translation: AAA35029.1. Z23261 Genomic DNA. Translation: CAA80796.1. Z35811 Genomic DNA. Translation: CAA84870.1. | |||||||||||||
| PIR | S39837. | ||||||||||||
| RefSeq | NP_009503.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP:2496N. | ||||||||||||
| IntAct | P32602. 31 interactions. | ||||||||||||
| STRING | P32602. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | P32602. | ||||||||||||
| PRIDE | P32602. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | YBL050W; YBL050W; YBL050W; Saccharomyces cerevisiae. [Genome view] | ||||||||||||
| GeneID | 852230. | ||||||||||||
| KEGG | sce:YBL050W. | ||||||||||||
| NMPDR | fig|4932.3.peg.193. | ||||||||||||
Organism-specific databases | |||||||||||||
| CYGD | YBL050w. | ||||||||||||
| SGD | S000000146. SEC17. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P32602. | ||||||||||||
| OMA | GNTRVEE | ||||||||||||
| OrthoDB | EOG9N325R | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P32602. | ||||||||||||
| Genevestigator | P32602. | ||||||||||||
| GermOnline | YBL050W. Saccharomyces cerevisiae. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000744. NSF_attach. [Graphical view] | ||||||||||||
| PANTHER | PTHR13768. NSF_attach. 1 hit. | ||||||||||||
| Pfam | PF02071. NSF. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00448. NSFATTACHMNT. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 970763. | ||||||||||||
Entry information
| Entry name | SEC17_YEAST | ||||||||
| Accession | Primary (citable) accession number: P32602 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome II Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names |

Clusters with


