ID   SEC17_YEAST             Reviewed;         292 AA.
AC   P32602; D6VPU9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   04-NOV-2026, entry version 205.
DE   RecName: Full=Alpha-soluble NSF attachment protein;
DE            Short=SNAP-alpha;
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha;
DE   AltName: Full=Vesicular-fusion protein SEC17;
DE   AltName: Full=alpha-SNAP chaperone;
GN   Name=SEC17; OrderedLocusNames=YBL050W; ORFNames=YBL0505, YBL0517;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1601878; DOI=10.1016/s0021-9258(19)49812-8;
RA   Griff I.C., Schekman R., Rothman J.E., Kaiser C.A.;
RT   "The yeast SEC17 gene product is functionally equivalent to mammalian
RT   alpha-SNAP protein.";
RL   J. Biol. Chem. 267:12106-12115(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8154187; DOI=10.1002/yea.320091210;
RA   Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT   "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT   of yeast chromosome II. Identification of 26 open reading frames, including
RT   the KIP1 and SEC17 genes.";
RL   Yeast 9:1355-1371(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-10; 52-62; 89-110 AND 121-136, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V., Peters C.;
RL   Submitted (MAY-2005) to UniProtKB.
RN   [6]
RP   FUNCTION.
RX   PubMed=8620540; DOI=10.1016/s0092-8674(00)81084-3;
RA   Mayer A., Wickner W., Haas A.;
RT   "Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and
RT   fusion of yeast vacuoles.";
RL   Cell 85:83-94(1996).
RN   [7]
RP   FUNCTION.
RX   PubMed=8670830; DOI=10.1002/j.1460-2075.1996.tb00694.x;
RA   Haas A., Wickner W.;
RT   "Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p
RT   (yeast NSF).";
RL   EMBO J. 15:3296-3305(1996).
RN   [8]
RP   FUNCTION.
RX   PubMed=9144293; DOI=10.1038/387199a0;
RA   Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A.;
RT   "Homotypic vacuolar fusion mediated by t- and v-SNAREs.";
RL   Nature 387:199-202(1997).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH CIS-SNARE COMPLEX.
RX   PubMed=15889152; DOI=10.1038/sj.emboj.7600658;
RA   Collins K.M., Thorngren N.L., Fratti R.A., Wickner W.T.;
RT   "Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex
RT   disruption or assembly for fusion.";
RL   EMBO J. 24:1775-1786(2005).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY.
RX   PubMed=10445030; DOI=10.1016/s1097-2765(00)80190-2;
RA   Rice L.M., Brunger A.T.;
RT   "Crystal structure of the vesicular transport protein Sec17: implications
RT   for SNAP function in SNARE complex disassembly.";
RL   Mol. Cell 4:85-95(1999).
CC   -!- FUNCTION: SNARE complex protein that binds to cis-SNARE complexes on
CC       membranes and is required for vesicular transport between the
CC       endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole
CC       fusion. During the priming step of membrane fusion, is released from
CC       cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs,
CC       which are required for interactions in trans during docking and fusion
CC       steps. Can displace HOPS from SNARE complexes, which may be a
CC       prerequisite for trans-SNARE complex disassembly and subsequent rounds
CC       of priming, docking and fusion. {ECO:0000269|PubMed:15889152,
CC       ECO:0000269|PubMed:8620540, ECO:0000269|PubMed:8670830,
CC       ECO:0000269|PubMed:9144293}.
CC   -!- SUBUNIT: Binds to vacuolar cis-SNARE complexes composed of the v-SNAREs
CC       NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7. Interacts with
CC       SEC18. {ECO:0000269|PubMed:15889152}.
CC   -!- INTERACTION:
CC       P32602; Q03322: TLG1; NbExp=3; IntAct=EBI-16558, EBI-38705;
CC       P32602; Q08144: TLG2; NbExp=2; IntAct=EBI-16558, EBI-19302;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR   EMBL; M93104; AAA35029.1; -; Genomic_DNA.
DR   EMBL; Z23261; CAA80796.1; -; Genomic_DNA.
DR   EMBL; Z35811; CAA84870.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07069.1; -; Genomic_DNA.
DR   PIR; S39837; S39837.
DR   RefSeq; NP_009503.1; NM_001178290.1.
DR   PDB; 1QQE; X-ray; 2.90 A; A=1-292.
DR   PDB; 9CRU; EM; 3.89 A; G/H=1-292.
DR   PDB; 9CRX; EM; 3.73 A; G/H/I=1-292.
DR   PDB; 9N22; EM; 3.91 A; G/H/I=1-292.
DR   PDB; 9NG2; EM; 4.61 A; G/H/I=1-292.
DR   PDB; 9NLU; EM; 4.29 A; G/H/I=1-292.
DR   PDB; 9NLW; EM; 3.73 A; G/H/I=1-292.
DR   PDB; 9NLY; EM; 3.75 A; G/H/I=1-292.
DR   PDB; 9NLZ; EM; 4.13 A; G/H/I=1-292.
DR   AlphaFoldDB; P32602; -.
DR   EMDB; EMD-45883; -.
DR   EMDB; EMD-45885; -.
DR   EMDB; EMD-48826; -.
DR   EMDB; EMD-49380; -.
DR   EMDB; EMD-49522; -.
DR   EMDB; EMD-49524; -.
DR   EMDB; EMD-49526; -.
DR   EMDB; EMD-49527; -.
DR   SMR; P32602; -.
DR   BioGRID; 32648; 437.
DR   DIP; DIP-2496N; -.
DR   FunCoup; P32602; 1073.
DR   IntAct; P32602; 49.
DR   STRING; 4932.YBL050W; -.
DR   TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR   iPTMnet; P32602; -.
DR   PaxDb; 4932-YBL050W; -.
DR   PeptideAtlas; P32602; -.
DR   EnsemblFungi; YBL050W_mRNA; YBL050W; YBL050W.
DR   GeneID; 852230; -.
DR   KEGG; sce:YBL050W; -.
DR   AGR; SGD:S000000146; -.
DR   SGD; S000000146; SEC17.
DR   VEuPathDB; FungiDB:YBL050W; -.
DR   eggNOG; KOG1586; Eukaryota.
DR   HOGENOM; CLU_046329_0_2_1; -.
DR   InParanoid; P32602; -.
DR   OMA; AAAWYES; -.
DR   OrthoDB; 9984275at2759; -.
DR   BioCyc; YEAST:G3O-28949-MONOMER; -.
DR   Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR   Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR   Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   BioGRID-ORCS; 852230; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P32602; -.
DR   PRO; PR:P32602; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P32602; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR   GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR   GO; GO:0005483; F:soluble NSF attachment protein activity; IDA:SGD.
DR   GO; GO:0006914; P:autophagy; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0035494; P:SNARE complex disassembly; IDA:SGD.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IDA:SGD.
DR   CDD; cd15832; SNAP; 1.
DR   FunFam; 1.25.40.10:FF:000049; Alpha-soluble NSF attachment protein-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR13768:SF8; ALPHA-SOLUBLE NSF ATTACHMENT PROTEIN; 1.
DR   PANTHER; PTHR13768; SOLUBLE NSF ATTACHMENT PROTEIN SNAP; 1.
DR   Pfam; PF14938; SNAP; 1.
DR   PRINTS; PR00448; NSFATTACHMNT.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; ER-Golgi transport;
KW   Isopeptide bond; Membrane; Protein transport; Reference proteome;
KW   Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..292
FT                   /note="Alpha-soluble NSF attachment protein"
FT                   /id="PRO_0000219076"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT   CROSSLNK        261
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        103
FT                   /note="A -> P (in Ref. 1; AAA35029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="Missing (in Ref. 1; AAA35029)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           21..25
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           30..49
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           54..69
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           73..89
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           113..126
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           134..150
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           154..170
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           174..186
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           198..211
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           215..223
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           238..249
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   TURN            253..255
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           256..263
FT                   /evidence="ECO:0007829|PDB:1QQE"
FT   HELIX           271..288
FT                   /evidence="ECO:0007829|PDB:1QQE"
SQ   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
//