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Alpha-soluble NSF attachment protein (SNAP-alpha) (N-ethylmaleimide-sensitive factor attachment protein alpha) (Vesicular-fusion protein SEC17) (alpha-SNAP chaperone)

 SEC17_YEAST             Reviewed;         292 AA.
P32602; D6VPU9;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 166.
RecName: Full=Alpha-soluble NSF attachment protein;
Short=SNAP-alpha;
AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha;
AltName: Full=Vesicular-fusion protein SEC17;
AltName: Full=alpha-SNAP chaperone;
Name=SEC17; OrderedLocusNames=YBL050W; ORFNames=YBL0505, YBL0517;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1601878;
Griff I.C., Schekman R., Rothman J.E., Kaiser C.A.;
"The yeast SEC17 gene product is functionally equivalent to mammalian
alpha-SNAP protein.";
J. Biol. Chem. 267:12106-12115(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8154187; DOI=10.1002/yea.320091210;
Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
"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.";
Yeast 9:1355-1371(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 2-10; 52-62; 89-110 AND 121-136, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (MAY-2005) to UniProtKB.
[6]
FUNCTION.
PubMed=8620540; DOI=10.1016/S0092-8674(00)81084-3;
Mayer A., Wickner W., Haas A.;
"Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede
docking and fusion of yeast vacuoles.";
Cell 85:83-94(1996).
[7]
FUNCTION.
PubMed=8670830;
Haas A., Wickner W.;
"Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and
Sec18p (yeast NSF).";
EMBO J. 15:3296-3305(1996).
[8]
FUNCTION.
PubMed=9144293; DOI=10.1038/387199a0;
Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A.;
"Homotypic vacuolar fusion mediated by t- and v-SNAREs.";
Nature 387:199-202(1997).
[9]
FUNCTION, AND INTERACTION WITH CIS-SNARE COMPLEX.
PubMed=15889152; DOI=10.1038/sj.emboj.7600658;
Collins K.M., Thorngren N.L., Fratti R.A., Wickner W.T.;
"Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex
disruption or assembly for fusion.";
EMBO J. 24:1775-1786(2005).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-292.
PubMed=10445030; DOI=10.1016/S1097-2765(00)80190-2;
Rice L.M., Brunger A.T.;
"Crystal structure of the vesicular transport protein Sec17:
implications for SNAP function in SNARE complex disassembly.";
Mol. Cell 4:85-95(1999).
-!- 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
disassembly and subsequent rounds of priming, docking and fusion.
{ECO:0000269|PubMed:15889152, ECO:0000269|PubMed:8620540,
ECO:0000269|PubMed:8670830, ECO:0000269|PubMed:9144293}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:15889152}.
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
-!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M93104; AAA35029.1; -; Genomic_DNA.
EMBL; Z23261; CAA80796.1; -; Genomic_DNA.
EMBL; Z35811; CAA84870.1; -; Genomic_DNA.
EMBL; BK006936; DAA07069.1; -; Genomic_DNA.
PIR; S39837; S39837.
RefSeq; NP_009503.1; NM_001178290.1.
PDB; 1QQE; X-ray; 2.90 A; A=1-292.
PDBsum; 1QQE; -.
ProteinModelPortal; P32602; -.
SMR; P32602; -.
BioGrid; 32648; 403.
DIP; DIP-2496N; -.
IntAct; P32602; 38.
MINT; P32602; -.
STRING; 4932.YBL050W; -.
TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P32602; -.
MaxQB; P32602; -.
PaxDb; P32602; -.
PRIDE; P32602; -.
EnsemblFungi; YBL050W; YBL050W; YBL050W.
GeneID; 852230; -.
KEGG; sce:YBL050W; -.
EuPathDB; FungiDB:YBL050W; -.
SGD; S000000146; SEC17.
GeneTree; ENSGT00390000005826; -.
HOGENOM; HOG000165015; -.
KO; K15296; -.
OMA; MADNEQK; -.
OrthoDB; EOG092C4020; -.
BioCyc; YEAST:G3O-28949-MONOMER; -.
Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
Reactome; R-SCE-6811438; Intra-Golgi traffic.
EvolutionaryTrace; P32602; -.
PRO; PR:P32602; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
GO; GO:0031201; C:SNARE complex; IPI:SGD.
GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
GO; GO:0005483; F:soluble NSF attachment protein activity; IDA:SGD.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:0006914; P:autophagy; IMP:SGD.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0035494; P:SNARE complex disassembly; IDA:SGD.
GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IDA:SGD.
CDD; cd15832; SNAP; 1.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR000744; NSF_attach.
InterPro; IPR011990; TPR-like_helical_dom_sf.
PANTHER; PTHR13768; PTHR13768; 1.
PRINTS; PR00448; NSFATTACHMNT.
SUPFAM; SSF48452; SSF48452; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; ER-Golgi transport; Isopeptide bond;
Membrane; Protein transport; Reference proteome; Transport;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 292 Alpha-soluble NSF attachment protein.
/FTId=PRO_0000219076.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 103 103 A -> P (in Ref. 1; AAA35029).
{ECO:0000305}.
CONFLICT 219 219 Missing (in Ref. 1; AAA35029).
{ECO:0000305}.
HELIX 4 14 {ECO:0000244|PDB:1QQE}.
HELIX 21 25 {ECO:0000244|PDB:1QQE}.
HELIX 30 49 {ECO:0000244|PDB:1QQE}.
HELIX 54 69 {ECO:0000244|PDB:1QQE}.
HELIX 73 89 {ECO:0000244|PDB:1QQE}.
HELIX 93 109 {ECO:0000244|PDB:1QQE}.
HELIX 113 129 {ECO:0000244|PDB:1QQE}.
HELIX 134 150 {ECO:0000244|PDB:1QQE}.
HELIX 154 170 {ECO:0000244|PDB:1QQE}.
HELIX 174 186 {ECO:0000244|PDB:1QQE}.
TURN 192 194 {ECO:0000244|PDB:1QQE}.
HELIX 195 197 {ECO:0000244|PDB:1QQE}.
HELIX 198 211 {ECO:0000244|PDB:1QQE}.
HELIX 215 223 {ECO:0000244|PDB:1QQE}.
HELIX 224 226 {ECO:0000244|PDB:1QQE}.
HELIX 238 249 {ECO:0000244|PDB:1QQE}.
TURN 253 255 {ECO:0000244|PDB:1QQE}.
HELIX 256 263 {ECO:0000244|PDB:1QQE}.
HELIX 271 288 {ECO:0000244|PDB:1QQE}.
SEQUENCE 292 AA; 32803 MW; 5002D31F80A65319 CRC64;
MSDPVELLKR AEKKGVPSSG FMKLFSGSDS YKFEEAADLC VQAATIYRLR KELNLAGDSF
LKAADYQKKA GNEDEAGNTY VEAYKCFKSG GNSVNAVDSL ENAIQIFTHR GQFRRGANFK
FELGEILEND LHDYAKAIDC YELAGEWYAQ DQSVALSNKC FIKCADLKAL DGQYIEASDI
YSKLIKSSMG NRLSQWSLKD YFLKKGLCQL AATDAVAAAR TLQEGQSEDP NFADSRESNF
LKSLIDAVNE GDSEQLSEHC KEFDNFMRLD KWKITILNKI KESIQQQEDD LL


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