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P32602 (SEC17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-soluble NSF attachment protein

Short name=SNAP-alpha
Alternative name(s):
N-ethylmaleimide-sensitive factor attachment protein alpha
Vesicular-fusion protein SEC17
alpha-SNAP chaperone
Gene names
Name:SEC17
Ordered Locus Names:YBL050W
ORF Names:YBL0517, YBL0505
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.6 Ref.7 Ref.8 Ref.9

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.9

Subcellular location

Membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the SNAP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 292291Alpha-soluble NSF attachment protein
PRO_0000219076

Amino acid modifications

Modified residue21N-acetylserine Ref.5
Modified residue1821Phosphoserine Ref.10

Experimental info

Sequence conflict1031A → P in AAA35029. Ref.1
Sequence conflict2191Missing in AAA35029. Ref.1

Secondary structure

................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32602 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 5002D31F80A65319

FASTA29232,803
        10         20         30         40         50         60 
MSDPVELLKR AEKKGVPSSG FMKLFSGSDS YKFEEAADLC VQAATIYRLR KELNLAGDSF 

        70         80         90        100        110        120 
LKAADYQKKA GNEDEAGNTY VEAYKCFKSG GNSVNAVDSL ENAIQIFTHR GQFRRGANFK 

       130        140        150        160        170        180 
FELGEILEND LHDYAKAIDC YELAGEWYAQ DQSVALSNKC FIKCADLKAL DGQYIEASDI 

       190        200        210        220        230        240 
YSKLIKSSMG NRLSQWSLKD YFLKKGLCQL AATDAVAAAR TLQEGQSEDP NFADSRESNF 

       250        260        270        280        290 
LKSLIDAVNE GDSEQLSEHC KEFDNFMRLD KWKITILNKI KESIQQQEDD LL 

« Hide

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. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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

EMBL
GenBank
DDBJ
M93104 Genomic DNA. Translation: AAA35029.1.
Z23261 Genomic DNA. Translation: CAA80796.1.
Z35811 Genomic DNA. Translation: CAA84870.1.
BK006936 Genomic DNA. Translation: DAA07069.1.
PIRS39837.
RefSeqNP_009503.1. NM_001178290.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQEX-ray2.90A2-292[»]
ProteinModelPortalP32602.
SMRP32602. Positions 1-290.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2496N.
IntActP32602. 33 interactions.
MINTMINT-491467.
STRINGP32602.

Proteomic databases

PeptideAtlasP32602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL050W; YBL050W; YBL050W.
GeneID852230.
KEGGsce:YBL050W.
NMPDRfig|4932.3.peg.193.

Organism-specific databases

SGDS000000146. SEC17.

Phylogenomic databases

eggNOGfuNOG07994.
GeneTreeEFGT00050000003962.
HOGENOMHBG397841.
OMAAQQYPAF.
OrthoDBEOG4XPTR6.

Gene expression databases

ArrayExpressP32602.
GenevestigatorP32602.
GermOnlineYBL050W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000744. NSF_attach.
IPR011990. TPR-like_helical.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
KOK15296.
PANTHERPTHR13768. NSF_attach. 1 hit.
PRINTSPR00448. NSFATTACHMNT.
ProtoNetSearch...

Other

NextBio970763.

Entry information

Entry nameSEC17_YEAST
AccessionPrimary (citable) accession number: P32602
Secondary accession number(s): D6VPU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families