Reviewed, UniProtKB/Swiss-Prot P32602 (SEC17_YEAST)

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

Name:	SEC17
Ordered Locus Names:	YBL050W
ORF Names:	YBL0517, YBL0505

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	Membrane; Peripheral membrane protein.
Sequence similarities	Belongs to the SNAP family.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Membrane
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ER to Golgi vesicle-mediated transport Inferred from genetic interaction. Source: SGD intracellular protein transport Inferred from electronic annotation. Source: InterPro piecemeal microautophagy of nucleus Inferred from mutant phenotype. Source: SGD vacuole fusion, non-autophagic Ref.5 Inferred from mutant phenotype. Source: SGD
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: InterPro endoplasmic reticulum Inferred from electronic annotation. Source: InterPro extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peripheral to membrane of membrane fraction Ref.1 Inferred from direct assay. Source: SGD
Molecular function	soluble NSF attachment protein activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

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

1

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292

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P32602-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 5002D31F80A65319	FASTA	292	32,803
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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

EMBLGenBankDDBJ

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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QQE	X-ray	2.90	A	2-292	[»]

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

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 92 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)